prompt_front: Now, answer the following question based on the text below, only give me the answer and do not output any other words.

Question: What algorithm is engaged in the PLMS-PPIC method?

Read the following text and answer briefly.

Context 1: \section{Introduction}\label{S1}

The multiple access interferences (MAI) is the root of user
limitation in CDMA systems \cite{R1,R3}  The parallel least mean
square-partial parallel interference cancelation (PLMS-PPIC) method
is a multiuser detector for code division multiple access (CDMA)
receivers which reduces the effect of MAI in bit detection  In this
method and similar to its former versions like LMS-PPIC \cite{R5}
(see also \cite{RR5}), a weighted value of the MAI of other users is
subtracted before making the decision for a specific user in
different stages \cite{cohpaper}  In both of these methods, the
normalized least mean square (NLMS) algorithm is engaged
\cite{Haykin96}  The $m^{\rm th}$ element of the weight vector in
each stage is the true transmitted binary value of the $m^{\rm th}$
user divided by its hard estimate value from the previous stage  The
magnitude of all weight elements in all stages are equal to unity 
Unlike the LMS-PPIC, the PLMS-PPIC method tries to keep this
property in each iteration by using a set of NLMS algorithms with
different step-sizes instead of one NLMS algorithm used in LMS-PPIC 
In each iteration, the parameter estimate of the NLMS algorithm is
chosen whose element magnitudes of cancelation weight estimate have
the best match with unity  In PLMS-PPIC implementation it is assumed
that the receiver knows the phases of all user channels  However in
practice, these phases are not known and should be estimated  In
this paper we improve the PLMS-PPIC procedure \cite{cohpaper} in
such a way that when there is only a partial information of the
channel phases, this modified version simultaneously estimates the
phases and the cancelation weights  The partial information is the
quarter of each channel phase in $(0,2\pi)$ 

The rest of the paper is organized as follows: In section \ref{S4}
the modified version of PLMS-PPIC with capability of channel phase
estimation is introduced  In section \ref{S5} some simulation
examples illustrate the results of the proposed method  Finally the
paper is concluded in section \ref{S6} 

\section{Multistage Parallel Interference Cancelation: Modified PLMS-PPIC Method}\label{S4}

We assume $M$ users synchronously send their symbols
$\alpha_1,\alpha_2,\cdots,\alpha_M$ via a base-band CDMA
transmission system where $\alpha_m\in\{-1,1\}$  The $m^{th}$ user
has its own code $p_m( )$ of length $N$, where $p_m(n)\in \{-1,1\}$,
for all $n$  It means that for each symbol $N$ bits are transmitted
by each user and the processing gain is equal to $N$  At the
receiver we assume that perfect power control scheme is applied 
Without loss of generality, we also assume that the power gains of
all channels are equal to unity and users' channels do not change
during each symbol transmission (it can change from one symbol
transmission to the next one) and the channel phase $\phi_m$ of
$m^{th}$ user is unknown for all $m=1,2,\cdots,M$ (see
\cite{cohpaper} for coherent transmission)  According to the above
assumptions the received signal is
\begin{equation}
\label{e1} r(n)=\sum\limits_{m=1}^{M}\alpha_m
e^{j\phi_m}p_m(n)+v(n),~~~~n=1,2,\cdots,N,
\end{equation}
where $v(n)$ is the additive white Gaussian noise with zero mean and
variance $\sigma^2$  Multistage parallel interference cancelation
method uses $\alpha^{s-1}_1,\alpha^{s-1}_2,\cdots,\alpha^{s-1}_M$,
the bit estimates outputs of the previous stage, $s-1$, to estimate
the related MAI of each user  It then subtracts it from the received
signal $r(n)$ and makes a new decision on each user variable
individually to make a new variable set
$\alpha^{s}_1,\alpha^{s}_2,\cdots,\alpha^{s}_M$ for the current
stage $s$  Usually the variable set of the first stage (stage $0$)
is the output of a conventional detector  The output of the last
stage is considered as the final estimate of transmitted bits  In
the following we explain the structure of a modified version of the
PLMS-PIC method \cite{cohpaper} with simultaneous capability of
estimating the cancelation weights and the channel phases 

Assume $\alpha_m^{(s-1)}\in\{-1,1\}$ is a given estimate of
$\alpha_m$ from stage $s-1$  Define
\begin{equation}
\label{e6} w^s_{m}=\frac{\alpha_m}{\alpha_m^{(s-1)}}e^{j\phi_m} 
\end{equation}
From (\ref{e1}) and (\ref{e6}) we have
\begin{equation}
\label{e7} r(n)=\sum\limits_{m=1}^{M}w^s_m\alpha^{(s-1)}_m
p_m(n)+v(n) 
\end{equation}
Define
\begin{subequations}
\begin{eqnarray}
\label{e8} W^s&=&[w^s_{1},w^s_{2},\cdots,w^s_{M}]^T,\\
\label{e9}
\!\!\!\!\!\!\!\!\!\!\!\!\!\!\!\!\!\!\!\!X^{s}(n)\!\!\!&=&\!\!\![\alpha^{(s-1)}_1p_1(n),\alpha^{(s-1)}_2p_2(n),\cdots,\alpha^{(s-1)}_Mp_M(n)]^T 
\end{eqnarray}
\end{subequations}
where $T$ stands for transposition  From equations (\ref{e7}),
(\ref{e8}) and (\ref{e9}), we have
\begin{equation}
\label{e10} r(n)=W^{s^T}X^{s}(n)+v(n) 
\end{equation}
Given the observations $\{r(n),X^{s}(n)\}^{N}_{n=1}$, in modified
PLMS-PPIC, like the PLMS-PPIC \cite{cohpaper}, a set of NLMS
adaptive algorithm are used to compute
\begin{equation}
\label{te1} W^{s}(N)=[w^{s}_1(N),w^{s}_2(N),\cdots,w^{s}_M(N)]^T,
\end{equation}
which is an estimate of $W^s$ after iteration $N$  To do so, from
(\ref{e6}), we have
\begin{equation}
\label{e13} |w^s_{m}|=1 ~~~m=1,2,\cdots,M,
\end{equation}
which is equivalent to
\begin{equation}
\label{e14} \sum\limits_{m=1}^{M}||w^s_{m}|-1|=0 
\end{equation}
We divide $\Psi=\left(0,1-\sqrt{\frac{M-1}{M}}\right]$, a sharp
range for $\mu$ (the step-size of the NLMS algorithm) given in
\cite{sg2005}, into $L$ subintervals and consider $L$ individual
step-sizes $\Theta=\{\mu_1,\mu_2,\cdots,\mu_L\}$, where
$\mu_1=\frac{1-\sqrt{\frac{M-1}{M}}}{L}, \mu_2=2\mu_1,\cdots$, and
$\mu_L=L\mu_1$  In each stage, $L$ individual NLMS algorithms are
executed ($\mu_l$ is the step-size of the $l^{th}$ algorithm)  In
stage $s$ and at iteration $n$, if
$W^{s}_k(n)=[w^s_{1,k},\cdots,w^s_{M,k}]^T$, the parameter estimate
of the $k^{\rm th}$ algorithm, minimizes our criteria, then it is
considered as the parameter estimate at time iteration $n$  In other
words if the next equation holds
\begin{equation}
\label{e17} W^s_k(n)=\arg\min\limits_{W^s_l(n)\in I_{W^s}
}\left\{\sum\limits_{m=1}^{M}||w^s_{m,l}(n)|-1|\right\},
\end{equation}
where $W^{s}_l(n)=W^{s}(n-1)+\mu_l \frac{X^s(n)}{\|X^s(n)\|^2}e(n),
~~~ l=1,2,\cdots,k,\cdots,L-1,L$ and
$I_{W^s}=\{W^s_1(n),\cdots,W^s_L(n)\}$, then we have
$W^s(n)=W^s_k(n)$, and therefore all other algorithms replace their
weight estimate by $W^{s}_k(n)$  At time instant $n=N$, this
procedure gives $W^s(N)$, the final estimate of $W^s$, as the true
parameter of stage $s$ 

Now consider $R=(0,2\pi)$ and divide it into four equal parts
$R_1=(0,\frac{\pi}{2})$, $R_2=(\frac{\pi}{2},\pi)$,
$R_3=(\pi,\frac{3\pi}{2})$ and $R_4=(\frac{3\pi}{2},2\pi)$  The
partial information of channel phases (given by the receiver) is in
a way that it shows each $\phi_m$ ($m=1,2,\cdots,M$) belongs to
which one of the four quarters $R_i,~i=1,2,3,4$  Assume
$W^{s}(N)=[w^{s}_1(N),w^{s}_2(N),\cdots,w^{s}_M(N)]^T$ is the weight
estimate of the modified algorithm PLMS-PPIC at time instant $N$ of
the stage $s$  From equation (\ref{e6}) we have
\begin{equation}
\label{tt3}
\phi_m=\angle({\frac{\alpha^{(s-1)}_m}{\alpha_m}w^s_m}) 
\end{equation}
We estimate $\phi_m$ by $\hat{\phi}^s_m$, where
\begin{equation}
\label{ee3}
\hat{\phi}^s_m=\angle{(\frac{\alpha^{(s-1)}_m}{\alpha_m}w^s_m(N))} 
\end{equation}
Because $\frac{\alpha^{(s-1)}_m}{\alpha_m}=1$ or $-1$, we have
\begin{eqnarray}
\hat{\phi}^s_m=\left\{\begin{array}{ll} \angle{w^s_m(N)} &
\mbox{if}~
\frac{\alpha^{(s-1)}_m}{\alpha_m}=1\\
\pm\pi+\angle{w^s_m(N)} & \mbox{if}~
\frac{\alpha^{(s-1)}_m}{\alpha_m}=-1\end{array}\right 
\end{eqnarray}
Hence $\hat{\phi}^s_m\in P^s=\{\angle{w^s_m(N)},
\angle{w^s_m(N)+\pi, \angle{w^s_m(N)}-\pi}\}$  If $w^s_m(N)$
sufficiently converges to its true value $w^s_m$, the same region
for $\hat{\phi}^s_m$ and $\phi_m$ is expected  In this case only one
of the three members of $P^s$ has the same region as $\phi_m$  For
example if $\phi_m \in (0,\frac{\pi}{2})$, then $\hat{\phi}^s_m \in
(0,\frac{\pi}{2})$ and therefore only $\angle{w^s_m(N)}$ or
$\angle{w^s_m(N)}+\pi$ or $\angle{w^s_m(N)}-\pi$ belongs to
$(0,\frac{\pi}{2})$  If, for example, $\angle{w^s_m(N)}+\pi$ is such
a member between all three members of $P^s$, it is the best
candidate for phase estimation  In other words,
\[\phi_m\approx\hat{\phi}^s_m=\angle{w^s_m(N)}+\pi \]
We admit that when there is a member of $P^s$ in the quarter of
$\phi_m$, then $w^s_m(N)$ converges  What would happen when non of
the members of $P^s$ has the same quarter as $\phi_m$? This
situation will happen when the absolute difference between $\angle
w^s_m(N)$ and $\phi_m$ is greater than $\pi$  It means that
$w^s_m(N)$ has not converged yet  In this case where we can not
count on $w^s_m(N)$, the expected value is the optimum choice for
the channel phase estimation, e g  if $\phi_m \in (0,\frac{\pi}{2})$
then $\frac{\pi}{4}$ is the estimation of the channel phase
$\phi_m$, or if $\phi_m \in (\frac{\pi}{2},\pi)$ then
$\frac{3\pi}{4}$ is the estimation of the channel phase $\phi_m$ 
The results of the above discussion are summarized in the next
equation
\begin{eqnarray}
\nonumber \hat{\phi}^s_m = \left\{\begin{array}{llll} \angle
{w^s_m(N)} & \mbox{if}~
\angle{w^s_m(N)}, \phi_m\in R_i,~~i=1,2,3,4\\
\angle{w^s_m(N)}+\pi & \mbox{if}~ \angle{w^s_m(N)}+\pi, \phi_m\in
R_i,~~i=1,2,3,4\\
\angle{w^n_m(N)}-\pi & \mbox{if}~ \angle{w^s_m(N)}-\pi, \phi_m\in
R_i,~~i=1,2,3,4\\
\frac{(i-1)\pi+i\pi}{4} & \mbox{if}~ \phi_m\in
R_i,~~\angle{w^s_m(N)},\angle
{w^s_m(N)}\pm\pi\notin R_i,~~i=1,2,3,4 \\
\end{array}\right 
\end{eqnarray}
Having an estimation of the channel phases, the rest of the proposed
method is given by estimating $\alpha^{s}_m$ as follows:
\begin{equation}
\label{tt4}
\alpha^{s}_m=\mbox{sign}\left\{\mbox{real}\left\{\sum\limits_{n=1}^{N}
q^s_m(n)e^{-j\hat{\phi}^s_m}p_m(n)\right\}\right\},
\end{equation}
where
\begin{equation} \label{tt5}
q^{s}_{m}(n)=r(n)-\sum\limits_{m^{'}=1,m^{'}\ne
m}^{M}w^{s}_{m^{'}}(N)\alpha^{(s-1)}_{m^{'}} p_{m^{'}}(n) 
\end{equation}
The inputs of the first stage $\{\alpha^{0}_m\}_{m=1}^M$ (needed for
computing $X^1(n)$) are given by
\begin{equation}
\label{qte5}
\alpha^{0}_m=\mbox{sign}\left\{\mbox{real}\left\{\sum\limits_{n=1}^{N}
r(n)e^{-j\hat{\phi}^0_m}p_m(n)\right\}\right\} 
\end{equation}
Assuming $\phi_m\in R_i$, then
\begin{equation}
\label{qqpp} \hat{\phi}^0_m =\frac{(i-1)\pi+i\pi}{4} 
\end{equation}
Table \ref{tab4} shows the structure of the modified PLMS-PPIC
method  It is to be notified that
\begin{itemize}
\item Equation (\ref{qte5}) shows the conventional bit detection
method when the receiver only knows the quarter of channel phase in
$(0,2\pi)$  \item With $L=1$ (i e  only one NLMS algorithm), the
modified PLMS-PPIC can be thought as a modified version of the
LMS-PPIC method 
\end{itemize}

In the following section some examples are given to illustrate the
effectiveness of the proposed method 

\section{Simulations}\label{S5}

In this section we have considered some simulation examples 
Examples \ref{ex2}-\ref{ex4} compare the conventional, the modified
LMS-PPIC and the modified PLMS-PPIC methods in three cases: balanced
channels, unbalanced channels and time varying channels  In all
examples, the receivers have only the quarter of each channel phase 
Example \ref{ex2} is given to compare the modified LMS-PPIC and the
PLMS-PPIC in the case of balanced channels 

\begin{example}{\it Balanced channels}:
\label{ex2}
\begin{table}
\caption{Channel phase estimate of the first user (example
\ref{ex2})} \label{tabex5} \centerline{{
\begin{tabular}{|c|c|c|c|c|}
\hline
\multirow{6}{*}{\rotatebox{90}{$\phi_m=\frac{3\pi}{8},M=15~~$}} & N(Iteration) & Stage Number& NLMS & PNLMS  \\
&&&&\\
\cline{2-5} & \multirow{2}{*}{64}& s = 2 &  $\hat{\phi}^s_m=\frac{3 24\pi}{8}$ & $\hat{\phi}^s_m=\frac{3 18\pi}{8}$ \\
\cline{3-5} & & s = 3 & $\hat{\phi}^s_m=\frac{3 24\pi}{8}$ & $\hat{\phi}^s_m=\frac{3 18\pi}{8}$ \\
\cline{2-5} & \multirow{2}{*}{256}& s = 2 &  $\hat{\phi}^s_m=\frac{2 85\pi}{8}$ & $\hat{\phi}^s_m=\frac{2 88\pi}{8}$ \\
\cline{3-5} & & s = 3 & $\hat{\phi}^s_m=\frac{2 85\pi}{8}$ & $\hat{\phi}^s_m=\frac{2 88\pi}{8}$ \\
\cline{2-5} \hline
\end{tabular} }}
\end{table}
Consider the system model (\ref{e7}) in which $M$ users
synchronously send their bits to the receiver through their
channels  It is assumed that each user's information consists of
codes of length $N$  It is also assumd that the signal to noise
ratio (SNR) is 0dB  In this example there is no power-unbalanced or
channel loss is assumed  The step-size of the NLMS algorithm in
modified LMS-PPIC method is $\mu=0 1(1-\sqrt{\frac{M-1}{M}})$ and
the set of step-sizes of the parallel NLMS algorithms in modified
PLMS-PPIC method are
$\Theta=\{0 01,0 05,0 1,0 2,\cdots,1\}(1-\sqrt{\frac{M-1}{M}})$,
i e  $\mu_1=0 01(1-\sqrt{\frac{M-1}{M}}),\cdots,
\mu_4=0 2(1-\sqrt{\frac{M-1}{M}}),\cdots,
\mu_{12}=(1-\sqrt{\frac{M-1}{M}})$  Figure~\ref{Figexp1NonCoh}
illustrates the bit error rate (BER) for the case of two stages and
for $N=64$ and $N=256$  Simulations also show that there is no
remarkable difference between results in two stage and three stage
scenarios  Table~\ref{tabex5} compares the average channel phase
estimate of the first user in each stage and over $10$ runs of
modified LMS-PPIC and PLMS-PPIC, when the the number of users is
$M=15$ 
\end{example}

Although LMS-PPIC and PLMS-PPIC, as well as their modified versions,
are structured based on the assumption of no near-far problem
(examples \ref{ex3} and \ref{ex4}), these methods and especially the
second one have remarkable performance in the cases of unbalanced
and/or time varying channels 

\begin{example}{\it Unbalanced channels}:
\label{ex3}
\begin{table}
\caption{Channel phase estimate of the first user (example
\ref{ex3})} \label{tabex6} \centerline{{
\begin{tabular}{|c|c|c|c|c|}
\hline
\multirow{6}{*}{\rotatebox{90}{$\phi_m=\frac{3\pi}{8},M=15~~$}} & N(Iteration) & Stage Number& NLMS & PNLMS  \\
&&&&\\
\cline{2-5} & \multirow{2}{*}{64}& s=2 &  $\hat{\phi}^s_m=\frac{2 45\pi}{8}$ & $\hat{\phi}^s_m=\frac{2 36\pi}{8}$ \\
\cline{3-5} & & s=3 & $\hat{\phi}^s_m=\frac{2 71\pi}{8}$ & $\hat{\phi}^s_m=\frac{2 80\pi}{8}$ \\
\cline{2-5} & \multirow{2}{*}{256}& s=2 &  $\hat{\phi}^s_m=\frac{3 09\pi}{8}$ & $\hat{\phi}^s_m=\frac{2 86\pi}{8}$ \\
\cline{3-5} & & s=3 & $\hat{\phi}^s_m=\frac{2 93\pi}{8}$ & $\hat{\phi}^s_m=\frac{3 01\pi}{8}$ \\
\cline{2-5} \hline
\end{tabular} }}
\end{table}
Consider example \ref{ex2} with power unbalanced and/or channel loss
in transmission system, i e  the true model at stage $s$ is
\begin{equation}
\label{ve7} r(n)=\sum\limits_{m=1}^{M}\beta_m
w^s_m\alpha^{(s-1)}_m c_m(n)+v(n),
\end{equation}
where $0<\beta_m\leq 1$ for all $1\leq m \leq M$  Both the LMS-PPIC
and the PLMS-PPIC methods assume the model (\ref{e7}), and their
estimations are based on observations $\{r(n),X^s(n)\}$, instead of
$\{r(n),\mathbf{G}X^s(n)\}$, where the channel gain matrix is
$\mathbf{G}=\mbox{diag}(\beta_1,\beta_2,\cdots,\beta_m)$  In this
case we repeat example \ref{ex2}  We randomly get each element of
$G$ from $[0,0 3]$  Figure~\ref{Figexp2NonCoh} illustrates the BER
versus the number of users  Table~\ref{tabex6} compares the channel
phase estimate of the first user in each stage and over $10$ runs of
modified LMS-PPIC and modified PLMS-PPIC for $M=15$ 
\end{example}

\begin{example}
\label{ex4} {\it Time varying channels}: Consider example \ref{ex2}
with time varying Rayleigh fading channels  In this case we assume
the maximum Doppler shift of $40$HZ, the three-tap
frequency-selective channel with delay vector of $\{2\times
10^{-6},2 5\times 10^{-6},3\times 10^{-6}\}$sec and gain vector of
$\{-5,-3,-10\}$dB  Figure~\ref{Figexp3NonCoh} shows the average BER
over all users versus $M$ and using two stages 
\end{example}


\section{Conclusion}\label{S6}

In this paper, parallel interference cancelation using adaptive
multistage structure and employing a set of NLMS algorithms with
different step-sizes is proposed, when just the quarter of the
channel phase of each user is known  In fact, the algorithm has been
proposed for coherent transmission with full information on channel
phases in \cite{cohpaper}  This paper is a modification on the
previously proposed algorithm  Simulation results show that the new
method has a remarkable performance for different scenarios
including Rayleigh fading channels even if the channel is
unbalanced 





ground_truth: The normalized least mean square (NLMS) algorithm.

prompt_front: Now, answer the following question based on the text below, only give me the answer and do not output any other words.

Question: What are the three synthetic types of vitamin K?

Read the following text and answer briefly.

Context 2: Vitamin K - Wikipedia
(Redirected from Vitamin k)
This article needs more medical references for verification or relies too heavily on primary sources  Please review the contents of the article and add the appropriate references if you can  Unsourced or poorly sourced material may be challenged and removed  (November 2015)
This article is about the family of vitamers  For vitamin K1 the form usually used as a supplement, see Phytomenadione 
Vitamin K structures  MK-4 and MK-7 are both subtypes of K2 
Vitamin K deficiency, Warfarin overdose
Vitamin K is a group of structurally similar, fat-soluble vitamins the human body requires for complete synthesis of certain proteins that are prerequisites for blood coagulation and which the body also needs for controlling binding of calcium in bones and other tissues  The vitamin K-related modification of the proteins allows them to bind calcium ions, which they cannot do otherwise  Without vitamin K, blood coagulation is seriously impaired, and uncontrolled bleeding occurs  Low levels of vitamin K also weaken bones and promote calcification of arteries and other soft tissues[citation needed] 
Chemically, the vitamin K family comprises 2-methyl-1,4-naphthoquinone (3-) derivatives  Vitamin K includes two natural vitamers: vitamin K1 and vitamin K2 [1] Vitamin K2, in turn, consists of a number of related chemical subtypes, with differing lengths of carbon side chains made of isoprenoid groups of atoms 
Vitamin K1, also known as phylloquinone, is made by plants, and is found in highest amounts in green leafy vegetables because it is directly involved in photosynthesis  It may be thought of as the plant form of vitamin K  It is active as a vitamin in animals and performs the classic functions of vitamin K, including its activity in the production of blood-clotting proteins  Animals may also convert it to vitamin K2 
Bacteria in the gut flora can also convert K1 into vitamin K2  In addition, bacteria typically lengthen the isoprenoid side chain of vitamin K2 to produce a range of vitamin K2 forms, most notably the MK-7 to MK-11 homologues of vitamin K2  All forms of K2 other than MK-4 can only be produced by bacteria, which use these forms in anaerobic respiration  The MK-7 and other bacterially derived forms of vitamin K2 exhibit vitamin K activity in animals, but MK-7's extra utility over MK-4, if any, is unclear and is a matter of investigation 
Three synthetic types of vitamin K are known: vitamins K3, K4, and K5  Although the natural K1 and all K2 homologues and synthetic K4 and K5 have proven nontoxic, the synthetic form K3 (menadione) has shown toxicity [2]
1 2 Cardiovascular health
1 4 Coumarin poisoning
4 1 Conversion of vitamin K1 to vitamin K2
4 2 Vitamin K2
6 Absorption and dietary need
7 Dietary reference intake
10 Biochemistry
10 1 Function in animals
10 2 Gamma-carboxyglutamate proteins
10 3 Methods of assessment
10 4 Function in bacteria
11 Injection in newborns
11 3 Controversy
A review of 2014 concluded that there is positive evidence that monotherapy using MK-4, one of the forms of Vitamin K2, reduces fracture incidence in post-menopausal women with osteoporosis, and suggested further research on the combined use of MK-4 with bisphosphonates  In contrast, an earlier review article of 2013 concluded that there is no good evidence that vitamin K supplementation helps prevent osteoporosis or fractures in postmenopausal women [3]
A Cochrane systematic review of 2006 suggested that supplementation with Vitamin K1 and with MK4 reduces bone loss; in particular, a strong effect of MK-4 on incident fractures among Japanese patients was emphasized [4]
A review article of 2016 suggested to consider, as one of several measures for bone health, increasing the intake of foods rich in vitamins K1 and K2 [5]
Cardiovascular health[edit]
Adequate intake of vitamin K is associated with the inhibition of arterial calcification and stiffening,[6] but there have been few interventional studies and no good evidence that vitamin K supplementation is of any benefit in the primary prevention of cardiovascular disease [7]
One 10-year population study, the Rotterdam Study, did show a clear and significant inverse relationship between the highest intake levels of menaquinone (mainly MK-4 from eggs and meat, and MK-8 and MK-9 from cheese) and cardiovascular disease and all-cause mortality in older men and women [8]
Vitamin K has been promoted in supplement form with claims it can slow tumor growth; there is however no good medical evidence that supports such claims [9]
Coumarin poisoning[edit]
Vitamin K is part of the suggested treatment regime for poisoning by rodenticide (coumarin poisoning) [10]
Although allergic reaction from supplementation is possible, no known toxicity is associated with high doses of the phylloquinone (vitamin K1) or menaquinone (vitamin K2) forms of vitamin K, so no tolerable upper intake level (UL) has been set [11]
Blood clotting (coagulation) studies in humans using 45 mg per day of vitamin K2 (as MK-4)[12] and even up to 135 mg per day (45 mg three times daily) of K2 (as MK-4),[13] showed no increase in blood clot risk  Even doses in rats as high as 250 mg/kg, body weight did not alter the tendency for blood-clot formation to occur [14]
Unlike the safe natural forms of vitamin K1 and vitamin K2 and their various isomers, a synthetic form of vitamin K, vitamin K3 (menadione), is demonstrably toxic at high levels  The U S  FDA has banned this form from over-the-counter sale in the United States because large doses have been shown to cause allergic reactions, hemolytic anemia, and cytotoxicity in liver cells [2]
Phylloquinone (K1)[15][16] or menaquinone (K2) are capable of reversing the anticoagulant activity of the anticoagulant warfarin (tradename Coumadin)  Warfarin works by blocking recycling of vitamin K, so that the body and tissues have lower levels of active vitamin K, and thus a deficiency of vitamin K 
Supplemental vitamin K (for which oral dosing is often more active than injectable dosing in human adults) reverses the vitamin K deficiency caused by warfarin, and therefore reduces the intended anticoagulant action of warfarin and related drugs [17] Sometimes small amounts of vitamin K are given orally to patients taking warfarin so that the action of the drug is more predictable [17] The proper anticoagulant action of the drug is a function of vitamin K intake and drug dose, and due to differing absorption must be individualized for each patient [citation needed] The action of warfarin and vitamin K both require two to five days after dosing to have maximum effect, and neither warfarin or vitamin K shows much effect in the first 24 hours after they are given [18]
The newer anticoagulants dabigatran and rivaroxaban have different mechanisms of action that do not interact with vitamin K, and may be taken with supplemental vitamin K [19][20]
Vitamin K2 (menaquinone)  In menaquinone, the side chain is composed of a varying number of isoprenoid residues  The most common number of these residues is four, since animal enzymes normally produce menaquinone-4 from plant phylloquinone 
A sample of phytomenadione for injection, also called phylloquinone
The three synthetic forms of vitamin K are vitamins K3 (menadione), K4, and K5, which are used in many areas, including the pet food industry (vitamin K3) and to inhibit fungal growth (vitamin K5) [21]
Conversion of vitamin K1 to vitamin K2[edit]
Vitamin K1 (phylloquinone) – both forms of the vitamin contain a functional naphthoquinone ring and an aliphatic side chain  Phylloquinone has a phytyl side chain 
The MK-4 form of vitamin K2 is produced by conversion of vitamin K1 in the testes, pancreas, and arterial walls [22] While major questions still surround the biochemical pathway for this transformation, the conversion is not dependent on gut bacteria, as it occurs in germ-free rats[23][24] and in parenterally-administered K1 in rats [25][26] In fact, tissues that accumulate high amounts of MK-4 have a remarkable capacity to convert up to 90% of the available K1 into MK-4 [27][28] There is evidence that the conversion proceeds by removal of the phytyl tail of K1 to produce menadione as an intermediate, which is then condensed with an activated geranylgeranyl moiety (see also prenylation) to produce vitamin K2 in the MK-4 (menatetrione) form [29]
Vitamin K2[edit]
Main article: Vitamin K2
Vitamin K2 (menaquinone) includes several subtypes  The two subtypes most studied are menaquinone-4 (menatetrenone, MK-4) and menaquinone-7 (MK-7) 
Vitamin K1, the precursor of most vitamin K in nature, is a stereoisomer of phylloquinone, an important chemical in green plants, where it functions as an electron acceptor in photosystem I during photosynthesis  For this reason, vitamin K1 is found in large quantities in the photosynthetic tissues of plants (green leaves, and dark green leafy vegetables such as romaine lettuce, kale and spinach), but it occurs in far smaller quantities in other plant tissues (roots, fruits, etc )  Iceberg lettuce contains relatively little  The function of phylloquinone in plants appears to have no resemblance to its later metabolic and biochemical function (as "vitamin K") in animals, where it performs a completely different biochemical reaction 
Vitamin K (in animals) is involved in the carboxylation of certain glutamate residues in proteins to form gamma-carboxyglutamate (Gla) residues  The modified residues are often (but not always) situated within specific protein domains called Gla domains  Gla residues are usually involved in binding calcium, and are essential for the biological activity of all known Gla proteins [30]
At this time[update], 17 human proteins with Gla domains have been discovered, and they play key roles in the regulation of three physiological processes:
Blood coagulation: prothrombin (factor II), factors VII, IX, and X, and proteins C, S, and Z[31]
Bone metabolism: osteocalcin, also called bone Gla protein (BGP), matrix Gla protein (MGP),[32] periostin,[33] and the recently discovered Gla-rich protein (GRP) [34][35]
Vascular biology: growth arrest-specific protein 6 (Gas6)[36]
Unknown function: proline-rich γ-carboxyglutamyl proteins (PRGPs) 1 and 2, and transmembrane γ-carboxy glutamyl proteins (TMGs) 3 and 4 [37]
Like other lipid-soluble vitamins (A, D and E), vitamin K is stored in the fatty tissue of the human body 
Absorption and dietary need[edit]
Previous theory held that dietary deficiency is extremely rare unless the small intestine was heavily damaged, resulting in malabsorption of the molecule  Another at-risk group for deficiency were those subject to decreased production of K2 by normal intestinal microbiota, as seen in broad spectrum antibiotic use [38] Taking broad-spectrum antibiotics can reduce vitamin K production in the gut by nearly 74% in people compared with those not taking these antibiotics [39] Diets low in vitamin K also decrease the body's vitamin K concentration [40] Those with chronic kidney disease are at risk for vitamin K deficiency, as well as vitamin D deficiency, and particularly those with the apoE4 genotype [41] Additionally, in the elderly there is a reduction in vitamin K2 production [42]
The National Academy of Medicine (NAM) updated an estimate of what constitutes an adequate intake (AI) for vitamin K in 2001  The NAM does not distinguish between K1 and K2 – both are counted as vitamin K  At that time there was not sufficient evidence to set the more rigorous estimated average requirement (EAR) or recommended dietary allowance (RDA) given for most of the essential vitamins and minerals  The current daily AIs for vitamin K for adult women and men are 90 μg and 120 μg respectively  The AI for pregnancy and lactation is 90 μg  For infants up to 12 months the AI is 2–2 5 μg, and for children aged 1 to 18 years the AI increases with age from 30 to 75 μg  As for safety, the FNB also sets tolerable upper intake levels (known as ULs) for vitamins and minerals when evidence is sufficient  In the case of vitamin K no UL is set, as evidence for adverse effects is not sufficient  Collectively EARs, RDAs, AIs and ULs are referred to as dietary reference intakes [43] The European Food Safety Authority reviewed the same safety question and did not set an UL [44]
For U S  food and dietary supplement labeling purposes, the amount in a serving is expressed as a percentage of daily value (%DV)  For vitamin K labeling purposes the daily value was 80 μg, but as of May 2016 it has been revised upwards to 120 μg  A table of the pre-change adult daily values is provided at reference daily intake  Food and supplement companies have until 28 July 2018 to comply with the change 
See also: Vitamin K2 § Dietary sources
K1 (μg)[45]
Kale, cooked
Collards, cooked
Collards, raw
Swiss chard, cooked
Swiss chard, raw
Turnip greens, raw
Romaine lettuce, raw
Table from "Important information to know when you are taking: Warfarin (Coumadin) and Vitamin K", Clinical Center, National Institutes of Health Drug Nutrient Interaction Task Force [46]
Vitamin K1 is found chiefly in leafy green vegetables such as dandelion greens (which contain 778 4 μg per 100 g, or 741% of the recommended daily amount), spinach, swiss chard, lettuce and Brassica vegetables (such as cabbage, kale, cauliflower, broccoli, and brussels sprouts) and often the absorption is greater when accompanied by fats such as butter or oils; some fruits, such as avocados, kiwifruit and grapes, are also high in vitamin K  By way of reference, two tablespoons of parsley contains 153% of the recommended daily amount of vitamin K [47] Some vegetable oils, notably soybean oil, contain vitamin K, but at levels that would require relatively large calorie consumption to meet the USDA-recommended levels [48] colonic bacteria synthesize a significant portion of humans' vitamin K needs; newborns often receive a vitamin K shot at birth to tide them over until their colons become colonized at five to seven days of age from the consumption of breast milk 
The tight binding of vitamin K1 to thylakoid membranes in chloroplasts makes it less bioavailable  For example, cooked spinach has a 5% bioavailability of phylloquinone, however, fat added to it increases bioavailability to 13% due to the increased solubility of vitamin K in fat [49]
Main article: Vitamin K deficiency
Average diets are usually not lacking in vitamin K, and primary deficiency is rare in healthy adults  Newborn infants are at an increased risk of deficiency  Other populations with an increased prevalence of vitamin K deficiency include those who suffer from liver damage or disease (e g  alcoholics), cystic fibrosis, or inflammatory bowel diseases, or have recently had abdominal surgeries  Secondary vitamin K deficiency can occur in people with bulimia, those on stringent diets, and those taking anticoagulants  Other drugs associated with vitamin K deficiency include salicylates, barbiturates, and cefamandole, although the mechanisms are still unknown  Vitamin K1 deficiency can result in coagulopathy, a bleeding disorder [50]Symptoms of K1 deficiency include anemia, bruising, nosebleeds and bleeding of the gums in both sexes, and heavy menstrual bleeding in women 
Osteoporosis[51][52] and coronary heart disease[53][54] are strongly associated with lower levels of K2 (menaquinone)  Vitamin K2 (as menaquinones MK-4 through MK-10) intake level is inversely related to severe aortic calcification and all-cause mortality [8]
Function in animals[edit]
Mechanism of action of vitamin K1 
The function of vitamin K2 in the animal cell is to add a carboxylic acid functional group to a glutamate (Glu) amino acid residue in a protein, to form a gamma-carboxyglutamate (Gla) residue  This is a somewhat uncommon posttranslational modification of the protein, which is then known as a "Gla protein"  The presence of two −COOH (carboxylic acid) groups on the same carbon in the gamma-carboxyglutamate residue allows it to chelate calcium ions  The binding of calcium ions in this way very often triggers the function or binding of Gla-protein enzymes, such as the so-called vitamin K-dependent clotting factors discussed below 
Within the cell, vitamin K undergoes electron reduction to a reduced form called vitamin K hydroquinone, catalyzed by the enzyme vitamin K epoxide reductase (VKOR) [55] Another enzyme then oxidizes vitamin K hydroquinone to allow carboxylation of Glu to Gla; this enzyme is called gamma-glutamyl carboxylase[56][57] or the vitamin K-dependent carboxylase  The carboxylation reaction only proceeds if the carboxylase enzyme is able to oxidize vitamin K hydroquinone to vitamin K epoxide at the same time  The carboxylation and epoxidation reactions are said to be coupled  Vitamin K epoxide is then reconverted to vitamin K by VKOR  The reduction and subsequent reoxidation of vitamin K coupled with carboxylation of Glu is called the vitamin K cycle [58] Humans are rarely deficient in vitamin K1 because, in part, vitamin K1 is continuously recycled in cells [59]
Warfarin and other 4-hydroxycoumarins block the action of VKOR [60] This results in decreased concentrations of vitamin K and vitamin K hydroquinone in tissues, such that the carboxylation reaction catalyzed by the glutamyl carboxylase is inefficient  This results in the production of clotting factors with inadequate Gla  Without Gla on the amino termini of these factors, they no longer bind stably to the blood vessel endothelium and cannot activate clotting to allow formation of a clot during tissue injury  As it is impossible to predict what dose of warfarin will give the desired degree of clotting suppression, warfarin treatment must be carefully monitored to avoid overdose 
Gamma-carboxyglutamate proteins[edit]
Main article: Gla domain
The following human Gla-containing proteins ("Gla proteins") have been characterized to the level of primary structure: blood coagulation factors II (prothrombin), VII, IX, and X, anticoagulant proteins C and S, and the factor X-targeting protein Z  The bone Gla protein osteocalcin, the calcification-inhibiting matrix Gla protein (MGP), the cell growth regulating growth arrest specific gene 6 protein (Gas6), and the four transmembrane Gla proteins (TMGPs), the function of which is at present unknown  Gas6 can function as a growth factor to activate the Axl receptor tyrosine kinase and stimulate cell proliferation or prevent apoptosis in some cells  In all cases in which their function was known, the presence of the Gla residues in these proteins turned out to be essential for functional activity 
Gla proteins are known to occur in a wide variety of vertebrates: mammals, birds, reptiles, and fish  The venom of a number of Australian snakes acts by activating the human blood-clotting system  In some cases, activation is accomplished by snake Gla-containing enzymes that bind to the endothelium of human blood vessels and catalyze the conversion of procoagulant clotting factors into activated ones, leading to unwanted and potentially deadly clotting 
Another interesting class of invertebrate Gla-containing proteins is synthesized by the fish-hunting snail Conus geographus [61] These snails produce a venom containing hundreds of neuroactive peptides, or conotoxins, which is sufficiently toxic to kill an adult human  Several of the conotoxins contain two to five Gla residues [62]
Methods of assessment[edit]
Vitamin K status can be assessed by:
The prothrombin time (PT) test measures the time required for blood to clot  A blood sample is mixed with citric acid and put in a fibrometer; delayed clot formation indicates a deficiency  This test is insensitive to mild deficiency, as the values do not change until the concentration of prothrombin in the blood has declined by at least 50% [63]
Undercarboxylated prothrombin (PIVKA-II); in a study of 53 newborns, found "PT (prothrombin time) is a less sensitive marker than PIVKA II",[64] and as indicated above, PT is unable to detect subclinical deficiencies that can be detected with PIVKA-II testing 
Plasma phylloquinone was found to be positively correlated with phylloquinone intake in elderly British women, but not men,[65] but an article by Schurgers et al  reported no correlation between FFQ[further explanation needed] and plasma phylloquinone [66]
Urinary γ-carboxyglutamic acid responds to changes in dietary vitamin K intake  Several days are required before any change can be observed  In a study by Booth et al , increases of phylloquinone intakes from 100 μg to between 377 and 417 μg for five days did not induce a significant change  Response may be age-specific [67]
Undercarboxylated osteocalcin (UcOc) levels have been inversely correlated with stores of vitamin K[68] and bone strength in developing rat tibiae  Another study following 78 post-menopausal Korean women found a supplement regimen of vitamins K and D, and calcium, but not a regimen of vitamin D and calcium, was inversely correlated with reduced UcOc levels [69]
Function in bacteria[edit]
Many bacteria, such as Escherichia coli found in the large intestine, can synthesize vitamin K2 (menaquinone-7 or MK-7, up to MK-11),[70] but not vitamin K1 (phylloquinone)  In these bacteria, menaquinone transfers two electrons between two different small molecules, during oxygen-independent metabolic energy production processes (anaerobic respiration) [71] For example, a small molecule with an excess of electrons (also called an electron donor) such as lactate, formate, or NADH, with the help of an enzyme, passes two electrons to menaquinone  The menaquinone, with the help of another enzyme, then transfers these two electrons to a suitable oxidant, such fumarate or nitrate (also called an electron acceptor)  Adding two electrons to fumarate or nitrate converts the molecule to succinate or nitrite plus water, respectively 
Some of these reactions generate a cellular energy source, ATP, in a manner similar to eukaryotic cell aerobic respiration, except the final electron acceptor is not molecular oxygen, but fumarate or nitrate  In aerobic respiration, the final oxidant is molecular oxygen (O2), which accepts four electrons from an electron donor such as NADH to be converted to water  E  coli, as facultative anaerobes, can carry out both aerobic respiration and menaquinone-mediated anaerobic respiration 
Injection in newborns[edit]
The blood clotting factors of newborn babies are roughly 30–60% that of adult values; this may be due to the reduced synthesis of precursor proteins and the sterility of their guts  Human milk contains 1–4 μg/L of vitamin K1, while formula-derived milk can contain up to 100 μg/L in supplemented formulas  Vitamin K2 concentrations in human milk appear to be much lower than those of vitamin K1  Occurrence of vitamin K deficiency bleeding in the first week of the infant's life is estimated at 0 25–1 7%, with a prevalence of 2–10 cases per 100,000 births [72] Premature babies have even lower levels of the vitamin, so they are at a higher risk from this deficiency 
Bleeding in infants due to vitamin K deficiency can be severe, leading to hospitalization, blood transfusions, brain damage, and death  Supplementation can prevent most cases of vitamin K deficiency bleeding in the newborn  Intramuscular administration is more effective in preventing late vitamin K deficiency bleeding than oral administration [73][74]
As a result of the occurrences of vitamin K deficiency bleeding, the Committee on Nutrition of the American Academy of Pediatrics has recommended 0 5–1 mg of vitamin K1 be administered to all newborns shortly after birth [74]
In the UK vitamin K supplementation is recommended for all newborns within the first 24 hours [75] This is usually given as a single intramuscular injection of 1 mg shortly after birth but as a second-line option can be given by three oral doses over the first month [76]
Controversy arose in the early 1990s regarding this practice, when two studies suggested a relationship between parenteral administration of vitamin K and childhood cancer,[77] however, poor methods and small sample sizes led to the discrediting of these studies, and a review of the evidence published in 2000 by Ross and Davies found no link between the two [78] Doctors reported emerging concerns in 2013,[79] after treating children for serious bleeding problems  They cited lack-of newborn vitamin K administration, as the reason that the problems occurred, and recommended that breastfed babies could have an increased risk unless they receive a preventative dose 
In the early 1930s, Danish scientist Henrik Dam investigated the role of cholesterol by feeding chickens a cholesterol-depleted diet [80] He initially replicated experiments reported by scientists at the Ontario Agricultural College (OAC) [81] McFarlane, Graham and Richardson, working on the chick feed program at OAC, had used chloroform to remove all fat from chick chow  They noticed that chicks fed only fat-depleted chow developed hemorrhages and started bleeding from tag sites [82] Dam found that these defects could not be restored by adding purified cholesterol to the diet  It appeared that – together with the cholesterol – a second compound had been extracted from the food, and this compound was called the coagulation vitamin  The new vitamin received the letter K because the initial discoveries were reported in a German journal, in which it was designated as Koagulationsvitamin  Edward Adelbert Doisy of Saint Louis University did much of the research that led to the discovery of the structure and chemical nature of vitamin K [83] Dam and Doisy shared the 1943 Nobel Prize for medicine for their work on vitamin K (K1 and K2) published in 1939  Several laboratories synthesized the compound(s) in 1939 [84]
For several decades, the vitamin K-deficient chick model was the only method of quantifying vitamin K in various foods: the chicks were made vitamin K-deficient and subsequently fed with known amounts of vitamin K-containing food  The extent to which blood coagulation was restored by the diet was taken as a measure for its vitamin K content  Three groups of physicians independently found this: Biochemical Institute, University of Copenhagen (Dam and Johannes Glavind), University of Iowa Department of Pathology (Emory Warner, Kenneth Brinkhous, and Harry Pratt Smith), and the Mayo Clinic (Hugh Butt, Albert Snell, and Arnold Osterberg) [85]
The first published report of successful treatment with vitamin K of life-threatening hemorrhage in a jaundiced patient with prothrombin deficiency was made in 1938 by Smith, Warner, and Brinkhous [86]
The precise function of vitamin K was not discovered until 1974, when three laboratories (Stenflo et al ,[87] Nelsestuen et al ,[88] and Magnusson et al [89]) isolated the vitamin K-dependent coagulation factor prothrombin (factor II) from cows that received a high dose of a vitamin K antagonist, warfarin  It was shown that, while warfarin-treated cows had a form of prothrombin that contained 10 glutamate (Glu) amino acid residues near the amino terminus of this protein, the normal (untreated) cows contained 10 unusual residues that were chemically identified as γ-carboxyglutamate (Gla)  The extra carboxyl group in Gla made clear that vitamin K plays a role in a carboxylation reaction during which Glu is converted into Gla 
The biochemistry of how vitamin K is used to convert Glu to Gla has been elucidated over the past thirty years in academic laboratories throughout the world 
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^ "Important information to know when you are taking: Warfarin (Coumadin) and Vitamin K" (PDF)  National Institutes of Health Clinical Center  ^ "Nutrition Facts and Information for Parsley, raw"  Nutritiondata com  Retrieved 21 Apr 2013  ^ "Nutrition facts, calories in food, labels, nutritional information and analysis"  Nutritiondata com  13 Feb 2008  Retrieved 21 Apr 2013  ^ "Vitamin K"  Vivo colostate edu  2 Jul 1999  Retrieved 21 Apr 2013  ^ "Vitamin K"  Micronutrient Data Centre  ^ Ikeda, Y ; Iki, M ; Morita, A ; Kajita, E ; Kagamimori, S ; Kagawa, Y ; Yoneshima, H  (May 2006)  "Intake of fermented soybeans, natto, is associated with reduced bone loss in postmenopausal women: Japanese Population-Based Osteoporosis (JPOS) Study"  Journal of Nutrition  136 (5): 1323–1328  PMID 16614424  ^ Katsuyama, H ; Ideguchi, S ; Fukunaga, M ; Saijoh, K ; Sunami, S  (Jun 2002)  "Usual dietary intake of fermented soybeans (Natto) is associated with bone mineral density in premenopausal women"  Journal of Nutritional Science and Vitaminology  48 (3): 207–215  doi:10 3177/jnsv 48 207  PMID 12350079  ^ Sano, M ; Fujita, H ; Morita, I ; Uematsu, H ; Murota, S  (Dec 1999)  "Vitamin K2 (menatetrenone) induces iNOS in bovine vascular smooth muscle cells: no relationship between nitric oxide production and gamma-carboxylation"  Journal of Nutritional Science and Vitaminology  45 (6): 711–723  doi:10 3177/jnsv 45 711  PMID 10737225  ^ Gast, G  C ; de Roos, N  M ; Sluijs, I ; Bots, M  L ; Beulens, J  W ; Geleijnse, J  M ; Witteman, J  C ; Grobbee, D  E ; Peeters, P  H ; van der Schouw, Y  T  (Sep 2009)  "A high menaquinone intake reduces the incidence of coronary heart disease"  Nutrition, Metabolism, and Cardiovascular Diseases  19 (7): 504–510  doi:10 1016/j numecd 2008 10 004  PMID 19179058  ^ Oldenburg, J ; Bevans, C  G ; Müller, C  R ; Watzka, M  (2006)  "Vitamin K epoxide reductase complex subunit 1 (VKORC1): the key protein of the vitamin K cycle"  Antioxidants & Redox Signaling  8 (3–4): 347–353  doi:10 1089/ars 2006 8 347  PMID 16677080  ^ Suttie, J  W  (1985)  "Vitamin K-dependent carboxylase"  Annual Review of Biochemistry  54: 459–477  doi:10 1146/annurev bi 54 070185 002331  PMID 3896125  ^ Presnell, S  R ; Stafford, D  W  (Jun 2002)  "The vitamin K-dependent carboxylase"  Thrombosis and Haemostasis  87 (6): 937–946  PMID 12083499  ^ Stafford, D  W  (Aug 2005)  "The vitamin K cycle"  Journal of Thrombosis and Haemostasis  3 (8): 1873–1878  doi:10 1111/j 1538-7836 2005 01419 x  PMID 16102054  ^ Rhéaume-Bleue, p  79 
^ Whitlon, D  S ; Sadowski, J  A ; Suttie, J  W  (Apr 1978)  "Mechanism of coumarin action: significance of vitamin K epoxide reductase inhibition"  Biochemistry  17 (8): 1371–1377  doi:10 1021/bi00601a003  PMID 646989  ^ Terlau, H ; Olivera, B  M  (Jan 2004)  "Conus venoms: a rich source of novel ion channel-targeted peptides"  Physiological Reviews  84 (1): 41–68  doi:10 1152/physrev 00020 2003  PMID 14715910  ^ Buczek, O ; Bulaj, G ; Olivera, BM (Dec 2005)  "Conotoxins and the posttranslational modification of secreted gene products"  Cellular and Molecular Life Sciences  62 (24): 3067–3079  doi:10 1007/s00018-005-5283-0  PMID 16314929  ^ "Prothrombin Time"  WebMD  ^ Dituri, F ; Buonocore, G ; Pietravalle, A ; Naddeo, F ; Cortesi, M; Pasqualetti, P; Tataranno M  L ; R , Agostino (Sep 2012)  "PIVKA-II plasma levels as markers of subclinical vitamin K deficiency in term infants"  Journal of Maternal, Fetal & Neonatal Medicine  25 (9): 1660–1663  doi:10 3109/14767058 2012 657273  PMID 22280352  ^ Thane, C  W ; Bates, C  J ; Shearer, M  J ; Unadkat, N; Harrington, D  J ; Paul, A  A ; Prentice, A ; Bolton-Smith, C  (Jun 2002)  "Plasma phylloquinone (vitamin K1) concentration and its relationship to intake in a national sample of British elderly people"  British Journal of Nutrition  87 (6): 615–622  doi:10 1079/BJNBJN2002582  PMID 12067432  ^ McKeown, N  M ; Jacques, P  F ; Gundberg, C  M ; Peterson, J  W ; Tucker, K  L ; Kiel, D  P ; Wilson, P  W ; Booth, SL (Jun 2002)  "Dietary and nondietary determinants of vitamin K biochemical measures in men and women" (PDF)  Journal of Nutrition  132 (6): 1329–1334  PMID 12042454  ^ Yamano, M ; Yamanaka, Y ; Yasunaga, K ; Uchida, K  (Sep 1989)  "Effect of vitamin K deficiency on urinary gamma-carboxyglutamic acid excretion in rats"  Nihon Ketsueki Gakkai Zasshi  52 (6): 1078–1086  PMID 2588957  ^ Matsumoto, T ; Miyakawa, T ; Yamamoto, D  (Mar 2012)  "Effects of vitamin K on the morphometric and material properties of bone in the tibiae of growing rats"  Metabolism  61 (3): 407–414  doi:10 1016/j metabol 2011 07 018  PMID 21944271  ^ Je, S -H ; Joo, N -S ; Choi, B -H ; Kim, K -M ; Kim, B -T ; Park, S -B ; Cho, D -Y ; Kim, K -N ; Lee, D -J  (Aug 2011)  "Vitamin K supplement along with vitamin D and calcium reduced serum concentration of undercarboxylated osteocalcin while increasing bone mineral density in Korean postmenopausal women over sixty-years-old"  Journal of Korean Medical Science  26 (8): 1093–1098  doi:10 3346/jkms 2011 26 8 1093  PMC 3154347  PMID 21860562  ^ Bentley, R ; Meganathan, R  (Sep 1982)  "Biosynthesis of vitamin K (menaquinone) in bacteria" (PDF)  Microbiological Reviews  46 (3): 241–280  PMC 281544  PMID 6127606  ^ Haddock, B  A ; Jones, C  W  (Mar 1977)  "Bacterial respiration" (PDF)  Bacteriological Reviews  41 (1): 47–99  PMC 413996  PMID 140652  ^ Shearer, M  J  (Jan 1995)  "Vitamin K"  Lancet  345 (8944): 229–234  doi:10 1016/S0140-6736(95)90227-9  PMID 7823718  ^ Greer, J  P ; Foerster, J ; Lukens, J  N ; Rodgers, G  M ; Paraskevas, F ; Glader, B  (eds )  Wintrobe's Clinical Hematology (11th ed )  Philadelphia, Pennsylvania: Lippincott, Williams and Wilkens  ^ a b American Academy of Pediatrics Committee on Fetus Newborn  (Jul 2003)  "Controversies concerning vitamin K and the newborn  American Academy of Pediatrics Committee on Fetus and Newborn" (PDF)  Pediatrics  112 (1 1): 191–192  doi:10 1542/peds 112 1 191  PMID 12837888  ^ Logan, S ; Gilbert, R  (1998)  "Vitamin K For Newborn Babies" (PDF)  Department of Health  Retrieved 12 Oct 2014  ^ "Postnatal care: Routine postnatal care of women and their babies [CG37]"  www nice org uk  NICE  Jul 2006  Retrieved 12 Oct 2014  ^ Parker, L ; Cole, M ; Craft, A  W ; Hey, E  N  (1998)  "Neonatal vitamin K administration and childhood cancer in the north of England: retrospective case-control study"  BMJ (Clinical Research Edition)  316 (7126): 189–193  doi:10 1136/bmj 316 7126 189  PMC 2665412  PMID 9468683  ^ McMillan, D  D  (1997)  "Routine administration of vitamin K to newborns"  Paediatric Child Health  2 (6): 429–431  ^ "Newborns get rare disorder after parents refused shots"  Having four cases since February just at Vanderbilt was a little bit concerning to me ^ Dam, C  P  H  (1935)  "The Antihaemorrhagic Vitamin of the Chick: Occurrence And Chemical Nature"  Nature  135 (3417): 652–653  doi:10 1038/135652b0  ^ Dam, C  P  H  (1941)  "The discovery of vitamin K, its biological functions and therapeutical application" (PDF)  Nobel Prize Laureate Lecture  ^ McAlister, V  C  (2006)  "Control of coagulation: a gift of Canadian agriculture" (PDF)  Clinical and Investigative Medicine  29 (6): 373–377  ^ MacCorquodale, D  W ; Binkley, S  B ; Thayer, S  A ; Doisy, E  A  (1939)  "On the constitution of Vitamin K1"  Journal of the American Chemical Society  61 (7): 1928–1929  doi:10 1021/ja01876a510  ^ Fieser, L  F  (1939)  "Synthesis of Vitamin K1"  Journal of the American Chemical Society  61 (12): 3467–3475  doi:10 1021/ja01267a072  ^ Dam, C  P  H  (12 Dec 1946)  "The discovery of vitamin K, its biological functions and therapeutical application" (PDF)  Nobel Prize lecture  ^ Warner, E  D ; Brinkhous, K  M ; Smith, H  P  (1938)  "Bleeding Tendency of Obstructive Jaundice"  Proceedings of the Society of Experimental Biology and Medicine  37 (4): 628–630  doi:10 3181/00379727-37-9668P  ^ Stenflo, J; Fernlund, P ; Egan, W ; Roepstorff, P  (Jul 1974)  "Vitamin K dependent modifications of glutamic acid residues in prothrombin"  Proceedings of the National Academy of Sciences of the United States of America  71 (7): 2730–2733  doi:10 1073/pnas 71 7 2730  PMC 388542  PMID 4528109  ^ Nelsestuen, G  L ; Zytkovicz, T  H ; Howard, J  B  (Oct 1974)  "The mode of action of vitamin K  Identification of gamma-carboxyglutamic acid as a component of prothrombin" (PDF)  Journal of Biological Chemistry  249 (19): 6347–6350  PMID 4214105  ^ Magnusson, S ; Sottrup-Jensen, L ; Petersen, T  E ; Morris, H  R ; Dell, A  (Aug 1974)  "Primary structure of the vitamin K-dependent part of prothrombin"  FEBS Letters  44 (2): 189–193  doi:10 1016/0014-5793(74)80723-4  PMID 4472513  Bibliography[edit]
Rhéaume-Bleue, Kate (2012)  Vitamin K2 and the Calcium Paradox  John Wiley & Sons, Canada  ISBN 1-118-06572-7  External links[edit]
"Vitamin K: Another Reason to Eat Your Greens"  v
TPP / ThDP (B1)
FMN, FAD (B2)
NAD+, NADH, NADP+, NADPH (B3)
Coenzyme A (B5)
PLP / P5P (B6)
THFA / H4FA, DHFA / H2FA, MTHF (B9)
AdoCbl, MeCbl (B12)
Phylloquinone (K1), Menaquinone (K2)
non-vitamins
Coenzyme B
Heme / Haem (A, B, C, O)
Molybdopterin/Molybdenum cofactor
THMPT / H4MPT
Fe2+, Fe3+
vitamins: see vitamins
Antihemorrhagics (B02)
(coagulation)
Phytomenadione (K1)
Menadione (K3)
intrinsic: IX/Nonacog alfa
VIII/Moroctocog alfa/Turoctocog alfa
extrinsic: VII/Eptacog alfa
common: X
II/Thrombin
I/Fibrinogen
XIII/Catridecacog
combinations: Prothrombin complex concentrate (II, VII, IX, X, protein C and S)
Carbazochrome
thrombopoietin receptor agonist (Romiplostim
Eltrombopag)
Tetragalacturonic acid hydroxymethylester
Epinephrine/Adrenalone
amino acids (Aminocaproic acid
Aminomethylbenzoic acid)
serpins (Aprotinin
Alfa1 antitrypsin
Camostat) 
Context 3: Publications of Kam W  Leong
Publications of Kam W  Leong :chronological alphabetical combined bibtex listing:
K W  Leong, Synthetic mast-cell granules as adjuvants to promote and polarize immunity in lymph nodes (2013) [PDF]
K W  Leong, Tuning Physical Properties of Nanocomplexes through Microfluidics-Assisted Confinement (2013) [PDF]
K W  Leong, Nucleic acid scavengers inhibit thrombosis without increasing bleeding (2013) [PDF]
K W  Leong, Nanotopography as modulator of human mesenchymal stem cell function (2013) [PDF]
K W  Leong, Efficacy of engineered FVIII-producing skeletal muscle enhanced by growth factor-releasing co-axial electrospun fibers (2013) [PDF]
Zhao, F  and Veldhuis, J  J  and Duan, Y  J  and Yang, Y  and Christoforou, N  and Ma, T  and Leong, K  W , Low Oxygen Tension and Synthetic Nanogratings Improve the Uniformity and Stemness of Human Mesenchymal Stem Cell Layer, Molecular Therapy, vol  18 no  5 (2010), pp  1010-1018 [abs]
Kadiyala, I  and Loo, Y  H  and Roy, K  and Rice, J  and Leong, K  W , Transport of chitosan-DNA nanoparticles in human intestinal M-cell model versus normal intestinal enterocytes, European Journal of Pharmaceutical Sciences, vol  39 no  1-3 (2010), pp  103-109 [abs]
Wang, Y  and Quek, C  H  and Leong, K W  and Fang, J , Synthesis and Cytotoxity of Luminescent InP Quantum Dots, MRS Symposium Proceeding, vol  1241E (2010)
Jiang, X  and Zheng, Y  and Chen, H  H  and Leong, K  W  and Wang, T  H  and Mao, H  Q , Dual-Sensitive Micellar Nanoparticles Regulate DNA Unpacking and Enhance Gene-Delivery Efficiency, Adv Mater (2010)
Ho, Y  P  and Leong, K  W , Quantum dot-based theranostics, Nanoscale, vol  2 no  1 (2010), pp  60-68 [PDF] [abs]
Phua, K  and Leong, K  W , Microscale oral delivery devices incorporating nanoparticles, Nanomedicine, vol  5 no  2 (2010), pp  161-163
Grigsby, C  L  and Leong, K  W , Balancing protection and release of DNA: tools to address a bottleneck of non-viral gene delivery, Journal of the Royal Society Interface, vol  7 (2010), pp  S67-S82 [abs]
Chalut, K  J  and Kulangara, K  and Giacomelli, M  G  and Wax, A  and Leong, K  W , Deformation of stem cell nuclei by nanotopographical cues, Soft Matter, vol  6 no  8 (2010), pp  1675-1681 [abs]
Chen, S  and Jones, J  A  and Xu, Y  and Low, H  Y  and Anderson, J  M  and Leong, K  W , Characterization of topographical effects on macrophage behavior in a foreign body response model, Biomaterials, vol  31 no  13 (2010), pp  3479-91 [PDF] [abs]
Yim, E  K  F  and Darling, E  M  and Kulangara, K  and Guilak, F  and Leong, K  W , Nanotopography-induced changes in focal adhesions, cytoskeletal organization, and mechanical properties of human mesenchymal stem cells, Biomaterials, vol  31 no  6 (2010), pp  1299-1306 [PDF] [abs]
Yow, S  Z  and Quek, C  H  and Yim, E  K  F  and Lim, C  T  and Leong, K  W , Collagen-based fibrous scaffold for spatial organization of encapsulated and seeded human mesenchymal stem cells, Biomaterials, vol  30 no  6 (2009), pp  1133-1142 [abs]
Kunder, C  A  and John, A  L  S  and Li, G  J  and Leong, K  W  and Berwin, B  and Staats, H  F  and Abraham, S  N , Mast cell-derived particles deliver peripheral signals to remote lymph nodes, Journal of Experimental Medicine, vol  206 no  11 (2009), pp  2455-2467 [abs]
Ho, Y P  and Chen, H H  and Leong, K W  and Wang, T H , Combining QD-FRET and microfluidics to monitor DNA nanocomplex self-assembly in real-time, J Vis Exp (2009), pp  1432
Kulangara, K  and Leong, K  W , Substrate topography shapes cell function, Soft Matter, vol  5 no  21 (2009), pp  4072-4076 [abs]
Chakraborty, S  and Liao, I  C  and Adler, A  and Leong, K  W , Electrohydrodynamics: A facile technique to fabricate drug delivery systems, Advanced Drug Delivery Reviews, vol  61 no  12 (2009), pp  1043-1054 [abs]
Oney, S  and Lam, R  T  S  and Bompiani, K  M  and Blake, C  M  and Quick, G  and Heidel, J  D  and Liu, J  Y  C  and Mack, B  C  and Davis, M  E  and Leong, K  W  and Sullenger, B  A , Development of universal antidotes to control aptamer activity, Nature Medicine, vol  15 no  10 (2009), pp  1224-1228 [PDF] [abs]
Chen, H  H  and Ho, Y  P  and Jiang, X  and Mao, H  Q  and Wang, T  H  and Leong, K  W , Simultaneous non-invasive analysis of DNA condensation and stability by two-step QD-FRET, Nano Today, vol  4 no  2 (2009), pp  125-134 [PDF] [abs]
Ho, Y  P  and Chen, H  H  and Leong, K  W  and Wang, T  H , The convergence of quantum-dot-mediated fluorescence resonance energy transfer and microfluidics for monitoring DNA polyplex self-assembly in real time, Nanotechnology, vol  20 no  9 (2009), pp  - [abs]
Liao, I  C  and Chen, S  L  and Liu, J  B  and Leong, K  W , Sustained viral gene delivery through core-shell fibers, Journal of Controlled Release, vol  139 no  1 (2009), pp  48-55 [abs]
Lou, Y  L  and Peng, Y  S  and Chen, B  H  and Wang, L  F  and Leong, K  W , Poly(ethylene imine)-g-chitosan using EX-810 as a spacer for nonviral gene delivery vectors, Journal of Biomedical Materials Research Part A, vol  88A no  4 (2009), pp  1058-1068 [abs]
Chew, S  Y  and Mi, R  and Hoke, A  and Leong, K  W , The effect of the alignment of electrospun fibrous scaffolds on Schwann cell maturation, Biomaterials, vol  29 no  6 (2008), pp  653-61 [abs]
Chen, H  H  and Ho, Y  P  and Jiang, X  and Mao, H  Q  and Wang, T  H  and Leong, K  W , Quantitative comparison of intracellular unpacking kinetics of polyplexes by a model constructed from quantum Dot-FRET, Molecular Therapy, vol  16 no  2 (2008), pp  324-332 [abs]
Chan, B  P  and Leong, K  W , Scaffolding in tissue engineering: general approaches and tissue-specific considerations, European Spine Journal, vol  17 (2008), pp  S467-S479 [abs]
Tsurushima, H  and Yuan, X  and Dillehay, L  E  and Leong, K  W , Radiation-inducible caspase-8 gene therapy for malignant brain tumors, International Journal of Radiation Oncology Biology Physics, vol  71 no  2 (2008), pp  517-525 [abs]
Bowman, K  and Sarkar, R  and Raut, S  and Leong, K  W , Gene transfer to hemophilia A mice via oral delivery of FVIII-chitosan nanoparticles, Journal of Controlled Release, vol  132 no  3 (2008), pp  252-259 [abs]
Choi, J  S  and Leong, K  W  and Yoo, H  S , In vivo wound healing of diabetic ulcers using electrospun nanofibers immobilized with human epidermal growth factor (EGF), Biomaterials, vol  29 no  5 (2008), pp  587-96 [abs]
Liao, I  C  and Liu, J  B  and Bursac, N  and Leong, K  W , Effect of Electromechanical Stimulation on the Maturation of Myotubes on Aligned Electrospun Fibers, Cellular and Molecular Bioengineering, vol  1 no  2-3 (2008), pp  133-145 [abs]
Prow, T  W  and Bhutto, I  and Kim, S  Y  and Grebe, R  and Merges, C  and McLeod, D  S  and Uno, K  and Mennon, M  and Rodriguez, L  and Leong, K  and Lutty, G  A , Ocular nanoparticle toxicity and transfection of the retina and retinal pigment epithelium, Nanomedicine-Nanotechnology Biology and Medicine, vol



ground_truth: Vitamins K3, K4, and K5.

prompt_front: Now, answer the following question based on the text below, only give me the answer and do not output any other words.

Question: What are the titles of one of Kam W. Leong's publications in Journal of Controlled Release?

Read the following text and answer briefly.

Context 3:  4 no  4 (2008), pp  340-349 [abs]
Tan, S  C  W  and Pan, W  X  and Ma, G  and Cai, N  and Leong, K  W  and Liao, K , Viscoelastic behaviour of human mesenchymal stem cells, Bmc Cell Biology, vol  9 (2008), pp  - [abs]
Chalut, K  J  and Chen, S  and Finan, J  D  and Giacomelli, M  G  and Guilak, F  and Leong, K  W  and Wax, A , Label-free, high-throughput measurements of dynamic changes in cell nuclei using angle-resolved low coherence interferometry, Biophysical Journal, vol  94 no  12 (2008), pp  4948-4956 [abs]
Haider, M  and Cappello, J  and Ghandehari, H  and Leong, K  W , In vitro chondrogenesis of mesenchymal stem cells in recombinant silk-elastinlike hydrogels, Pharmaceutical Research, vol  25 no  3 (2008), pp  692-699 [abs]
N  Bursac and Y  H  Loo and K  Leong and L  Tung, Novel anisotropic engineered cardiac tissues: Studies of electrical propagation, Biochemical And Biophysical Research Communications, vol  361 no  4 (October, 2007), pp  847 -- 853, ISSN 0006-291X [abs]
Chen, Beiyi and Dang, Jiyoung and Tan, Tuan Lin and Fang, Ning and Chen, Wei Ning and Leong, Kam W  and Chan, Vincent, Dynamics of smooth muscle cell deadhesion from thermosensitive hydroxybutyl chitosan, Biomaterials, vol  28 no  8 (2007), pp  1503 - 1514 [027] [abs]
Chen, B  and Dang, J  and Tan, T  L  and Fang, N  and Chen, W  N  and Leong, K  W  and Chan, V , Dynamics of smooth muscle cell deadhesion from thermosensitive hydroxybutyl chitosan, Biomaterials, vol  28 no  8 (2007), pp  1503-14 [abs]
Park, D  J  and Choi, J  H  and Leong, K  W  and Kwon, J  W  and Eun, H  S , Tissue-engineered bone formation with gene transfer and mesenchymal stem cells in a minimally invasive technique, Laryngoscope, vol  117 no  7 (2007), pp  1267-71 [abs]
Tsurushima, H  and Yuan, X  and Dillehay, L  E  and Leong, K  W , Radioresponsive tumor necrosis factor-related apoptosisinducing ligand (TRAIL) gene therapy for malignant brain tumors, Cancer Gene Therapy, vol  14 no  8 (2007), pp  706-716 [abs]
Chai, C  and Leong, K  W , Biomaterials approach to expand and direct differentiation of stem cells, Molecular Therapy, vol  15 no  3 (2007), pp  467-480 [abs]
Zhang, Y  and Chai, C  and Jiang, X  S  and Teoh, S  H  and Leong, K  W , Fibronectin immobilized by covalent conjugation or physical adsorption shows different bioactivity on aminated-PET, Materials Science & Engineering C-Biomimetic and Supramolecular Systems, vol  27 no  2 (2007), pp  213-219 [abs]
Song, R  J  and Liu, S  Q  and Leong, K  W , Effects of MIP-1 alpha, MIP-3 alpha, and MIP-3 beta on the induction of HIV Gag-specific immune response with DNA vaccines, Molecular Therapy, vol  15 no  5 (2007), pp  1007-1015 [abs]
Yim, E  K  F  and Liao, I  C  and Leong, K  W , Tissue compatibility of interfacial polyelectrolyte complexation fibrous scaffold: Evaluation of blood compatibility and biocompatibility, Tissue Engineering, vol  13 no  2 (2007), pp  423-433 [abs]
Sharma, B  and Williams, C  G  and Kim, T  K  and Sun, D  N  and Malik, A  and Khan, M  and Leong, K  and Elisseeff, J  H , Designing zonal organization into tissue-engineered cartilage, Tissue Engineering, vol  13 no  2 (2007), pp  405-414 [abs]
Chua, K  N  and Tang, Y  N  and Quek, C  H  and Ramakrishna, S  and Leong, K  W  and Mao, H  Q , A dual-functional fibrous scaffold enhances P450 activity of cultured primary rat hepatocytes, Acta Biomaterialia, vol  3 no  5 (2007), pp  643-650 [abs]
Chua, K  N  and Chai, C  and Lee, P  C  and Ramakrishna, S  and Leong, K  W  and Mao, H  Q , Functional nanofiber scaffolds with different spacers modulate adhesion and expansion of cryopreserved umbilical cord blood hematopoietic stem/progenitor cells, Experimental Hematology, vol  35 no  5 (2007), pp  771-781 [abs]
Yim, E  K  F  and Pang, S  W  and Leong, K  W , Synthetic nanostructures inducing differentiation of human mesenchymal stem cells into neuronal lineage, Experimental Cell Research, vol  313 no  9 (2007), pp  1820-1829 [abs]
Chew, S  Y  and Mi, R  F  and Hoke, A  and Leong, K  W , Aligned protein-polymer composite fibers enhance nerve regeneration: A potential tissue-engineering platform, Advanced Functional Materials, vol  17 no  8 (2007), pp  1288-1296 [abs]
Tsurushima, H  and Yuan, X  and Dillehay, L  E  and Leong, K  W , Radio-responsive gene therapy for malignant glioma cells without the radiosensitive promoter: Caspase-3 gene therapy combined with radiation, Cancer Letters, vol  246 no  1-2 (2007), pp  318-323 [abs]
Dang, J M  and Leong, K  W , Myogenic induction of aligned mesenchymal stem cell sheets by culture on thermally responsive electrospun nanofibers, Advanced Materials, vol  19 no  19 (2007), pp  2775-2779
Dai, H  and Jiang, X  and Tan, G  C  and Chen, Y  and Torbenson, M  and Leong, K  W  and Mao, H  Q , Chitosan-DNA nanoparticles delivered by intrabiliary infusion enhance liver-targeted gene delivery, International Journal of Nanomedicine, vol  1 no  4 (2006), pp  507-522 [abs]
Le Visage, C  and Kim, S  W  and Tateno, K  and Sieber, A  N  and Kostuik, J  P  and Leong, K  W , Interaction of human mesenchymal stem cells with disc cells - Changes in extracellular matrix biosynthesis, Spine, vol  31 no  18 (2006), pp  2036-2042
Ong, S  Y  and Dai, H  and Leong, K  W , Inducing hepatic differentiation of human mesenchymal stem cells in pellet culture, Biomaterials, vol  27 no  22 (2006), pp  4087-4097
Bright, C  and Park, Y  S  and Sieber, A  N  and Kostuik, J  P  and Leong, K  W , In vivo evaluation of plasmid DNA encoding OP-1 protein for spine fusion, Spine, vol  31 no  19 (2006), pp  2163-2172
Yim, E  K  and Wan, A  C  and Le Visage, C  and Liao, I  C  and Leong, K  W , Proliferation and differentiation of human mesenchymal stem cell encapsulated in polyelectrolyte complexation fibrous scaffold, Biomaterials, vol  27 no  36 (2006), pp  6111-22 [abs]
Luong-Van, E  and Grondahl, L  and Chua, K  N  and Leong, K  W  and Nurcombe, V  and Cool, S  M , Controlled release of heparin from poly(epsilon-caprolactone) electrospun fibers, Biomaterials, vol  27 no  9 (2006), pp  2042-2050
Dang, J  M  and Leong, K  W , Natural polymers for gene delivery and tissue engineering, Advanced Drug Delivery Reviews, vol  58 no  4 (2006), pp  487-499
Li, J  and Li, X  and Ni, X  P  and Wang, X  and Li, H  Z  and Leong, K  W , Self-assembled supramolecular hydrogels formed by biodegradable PEO-PHB-PEO triblock copolymers and alpha-cyclodextrin for controlled drug delivery, Biomaterials, vol  27 no  22 (2006), pp  4132-4140
Yim, E  K  F  and Wen, J  and Leong, K  W , Enhanced extracellular matrix production and differentiation of human embryonic germ cell derivatives in biodegradable poly(epsilon-caprolactone-co-ethyl ethylene phosphate) scaffold, Acta Biomaterialia, vol  2 no  4 (2006), pp  365-376
Chew, S  Y  and Hufnagel, T  C  and Lim, C  T  and Leong, K  W , Mechanical properties of single electrospun drug-encapsulated nanofibres, Nanotechnology, vol  17 no  15 (2006), pp  3880-3891
Zhang, Y  and Chai, C  and Jiang, X  S  and Teoh, S  H  and Leong, K  W , Co-culture of umbilical cord blood CD34(+) cells with human mesenchymal stem cells, Tissue Engineering, vol  12 no  8



ground_truth: Sustained viral gene delivery through core-shell fibers and Gene transfer to hemophilia A mice via oral delivery of FVIII-chitosan nanoparticles.