OpenLLM-France/wikimedia huggingface dataset:
# The Voynich Manuscript/Wilfrid Michael Voynich

Wilfrid Michael Voynich (Telshi, Russian Empire, 31 October 1865 – New York City, United States, 19 March 1930), born Michał Habdank-Wojnicz, was a Polish revolutionary, British and American antiquarian and bibliophile, and the eponym of the Voynich manuscript.

## Biography

Michał Wojnicz was born in Telshi — a town in then Kovno Governorate, which was part of the Russian Empire, now it is Telšiai, a town in Lithuania — into a Polish-Lithuanian noble family. He was the son of a titular counsellor (described by Prinke as a "petty official").
He studied at the universities in Warsaw and St. Petersberg, and graduated from Moscow University in chemistry and pharmacy.
In 1885, in Warsaw, Wojnicz joined Ludwik Waryński's revolutionary organization, Proletarjat. He was vital for the organization as a stranger who spoke fluent Russian, so could gain favour of a renegade Pole, Lieut.-Col. Bielanowski of the gendarmerie, from whom he elicited the passwords for the planned escape of Piotr Bardowski (1846-1886) and Stanisław Kunicki (1861-1886), former members of Narodnaya Volia and both sentenced to death, from the Citadel. The attempt failed allegedly due to a traitor, and Bardowski and Kunicki were hanged on 28 January 1886, while Woynicz and others were arrested by the Tsarist police and, in 1887, he was sent to penal servitude at Tunka.
In 1890 he escaped from Siberia and arrived in London, adopting as his first name his nom de guerre, Wilfryd. In 1893 he married a fellow-revolutionary, Ethel Lilian Boole, daughter of the famous British mathematician, George Boole.
With Sergey Stepnyak-Kravchinsky, a fellow revolutionary, he founded the Society of Friends for a Free Russia in London.
After the 1895 death of Stepniak in a railway crossing accident, the Voyniches (as they had anglicized their surname) ceased revolutionary activity. In 1898 Voynich opened a bookshop in London, followed by another in 1914 in New York. He was much involved with the handling of early books and wrote a number of catalogues and other texts on the subject.
Voynich died in New York in 1930.

## References

* 1 2 Деятели революционного движения в России: Био-библиографический словарь: От предшественников декабристов до падения царизма: [В 5 т.]. - М.: Изд-во Всесоюзного общества политических каторжан и ссыльно-поселенцев, 1927-1934. Entry on Voynich
* ↑ Otto von Schleinitz, "Die Bibliophilen. W. M. Voynich" in Zeitschrift für Bücherfreunde, 10 (1906/7), p. 481-487
* ↑ E. Millicent Sowerby, Rare People & Rare Books, London 1967 [2nd ed. Williamsburg, Va. 1987]
* ↑ Lewis Bernhardt, "The Gadfly in Ruissia," The Princeton University Library Chronicle 28, no. 1 (Autumn 1966): 2.

## External links

* Biographical information on E. L. Voynich and W. M. Voynich by Rafał T. Prinke
# The Way of the Java
## Contents

* Introduction: The Way of the Java
* Variables and types
* Methods
* Conditionals, graphics, and recursion
* Fruitful methods
* Iteration
* Strings and things
* Interesting objects
* Create your own objects
* Arrays
* Arrays of Objects
* Objects of Arrays
* Object-oriented programming
* Linked lists
* Stacks
* Queues and Priority Queues
* Trees
* Heap
* Table
* Wrapper classes
* Input and Output in Java
* The Slate Class
* Debugging
# The Voynich Manuscript/Leo Levitov

Levitov's claim of decipherment has been thoroughly discredited.
For a critique by linguistic science, by Jacques B.-M. Guy, see http://www.voynich.net/reeds/gillogly/levitov
For a critique by historical analysis, by Dennis J. Stallings, see http://web.archive.org/web/20010410030648/http://www.geocities.com/ctesibos/voynich/levitov2.htm
# The Voynich Manuscript/Page-by-page commentary
## Quire 1

Structurally, the Voynich Manuscript is divided into quires - each quire comprises a set of about four bifolios folded down the middle, stitched along the gutter.
Here, then, is a schematic diagram of Quire 1, with clickable links to each of its 16 pages:-

## Quire 2

Here is a schematic diagram of Quire 2, with clickable links to each of its 16 (original) pages:-

## Quire 3

Here is a schematic diagram of Quire 3, with clickable links to each of its 16 pages:-

## Quire 4

Here is a schematic diagram of Quire 4, with clickable links to each of its 16 pages:-

## Quire 5

Here is a schematic diagram of Quire 5, with clickable links to each of its 16 pages:-

## Quire 6

Here is a schematic diagram of Quire 6, with clickable links to each of its 16 pages:-

## Quire 7

Here is a schematic diagram of Quire 7, with clickable links to each of its 16 pages:-

## Quire 8

Here is a schematic diagram of Quire 8, with clickable links to each of its 8 remaining pages (originally probably 20):-

## Quire 9

Here is a schematic diagram of Quire 9, with clickable links to each of its pages. The two folios fold out to 10 pages altogether:-

## Quire 10

Here is a schematic diagram of Quire 10, with clickable links to each of its pages. The two folios fold out to 6 pages altogether:-

## Quire 11

Here is a schematic diagram of Quire 11, with clickable links to each of its pages. The two folios fold out to 8 pages altogether:-

## Quire 12

Here is a schematic diagram of Quire 12, with clickable links to its 2 remaining pages:-

## Quire 13

Here is a schematic diagram of Quire 13, with clickable links to each of its 20 pages:-

## Quire 14

Here is a schematic diagram of Quire 14, with clickable links to its pages. It consists of a single multiple-folded leaf consisting of a complicated 9-rosettes drawing on one side, and 6 individual pages on the other:-

## Quire 15

Here is a schematic diagram of Quire 15, with clickable links to each of its pages. The four folios fold out to 12 pages altogether:-

## Quire 16

Despite this quire's absence, it almost certainly contains (if the folio numbering system is consistent with the quire numbering system) folios 91 and 92 (i.e. probably a single bifolio).

## Quire 17

Here is a schematic diagram of Quire 17, with clickable links to each of its pages. The four folios fold out to 10 pages altogether:-

## Quire 18

Despite this quire's absence, it almost certainly contains (if the folio numbering system is consistent with the quire numbering system) folios 97 and 98 (i.e. probably a single bifolio).

## Quire 19

Here is a schematic diagram of Quire 19, with clickable links to each of its pages. The four folios fold out to 12 pages altogether:-

## Quire 20

Here is a schematic diagram of Quire 20, with clickable links to each of its remaining 24 pages:-
# Structural Biochemistry/Catalytic Strategies/Covalent Catalysis

[[:Image:]][[:Image:]]

## Covalent Catalysis: A Definition

Covalent Catalysis one of the four strategies that an enzyme will employ to catalyze a specific reaction. In this reaction the enzyme contains a reactive group, usually a nucleophilic residue which reacts with the substrate through a nucleophilic attack. This is usually carried out by pyridine, which is a better nucleophile than water that has a pKa of 5.5. The charge loss in the reaction during transitional state will then cause hydrolysis to accelerate. The residue becomes covalently attached to the substrate throughout the catalytic reaction adding an additional intermediate which helps stabilize later transition states by lowering the activation energy. The covalent bond is then broken to regenerate enzymes.

## Examples of Enzymes that Participate in Covalent Catalysis

Examples of enzymes that participate in covalent catalysis include the proteolytic enzyme chymotrypsin and trypsin in which the nucleophile is the hydroxyl group on the serine. Chymotrypsin is a degradative protease of the digestive system. It catalyzes the cleavage of peptide bonds that are adjacent to large aromatic or nonpolar residues. It cleaves the peptide bond on the carboxyl terminus side of the protein. The chymotrypsin has three main catalytic residues termed as the catalytic triad. These are His 57, Asp 102 and Ser 195. Upon deprotonation the serine residue becomes a powerful nucleophile due to its alkoxide that will attack the relatively unreactive carbon of the carbonyl in the protein. The figure shows the catalytic triads in neutral and deprotonated form. Courtesy of Kiongho; www.nsm.buffalo.edu/~kiongho/
Typical residues used in covalent catalysis are Lys, His, Cys, Asp, Glu, and Ser and some other coenzymes.
An example of covalent catalysis is shown below:
# Structural Biochemistry/Catalytic Mechanisms/Catalysis by Approximation
## Catalysis by Approximation

Substrates that happen to come together through random collisions have an even smaller possibility of contact with the reactive portions of the substrate. Thus, enzymes can employ a strategy known as catalysis by approximation by which the enzyme brings together two substrates in order to increase the rate of reaction. This strategy takes advantage of binding energy and positions the substrates in the correct orientation for the reaction to proceed. Usually in a reaction, there will be a loss in translational entropy and rotational entropy. In the reaction, the transition state is much more ordered than it is at ground state, making delta S negative. This reaction takes place in the active site of an enzyme and the substrate and the catalytic group will than act as one molecule, preventing the loss of translational and rotational energy. The reaction first begins with two molecules that are able to find each other, which makes the rate of reaction dependent on the concentrations of the reactants. This is due to the higher probability of molecules to find each other.

## Some Examples

An example of catalysis by approximation is when NMP kinases bring two nucleotides together to facilitate the transfer of a phosphoryl group from one nucleotide to the other. With the addition of adenosine triphosphate (ATP), a phosphate group is placed adjacently to the phosphate group of the NMP kinase. This facilitates in the transfer of the phosphate between the two molecules.
# Structural Biochemistry/Catalytic Strategies/General Acid-Base Catalysis

General acid-base catalysis involves a molecule besides water that acts as a proton donor or acceptor during the enzymatic reaction. In order to avoid having an unstable charged intermediates in the reaction, an enzyme has appropriately located functional groups readily to donate a proton or accept a proton to stabilize the transition state. When a functional group accepts a proton, it will release or donate a proton by the end of the catalytic cycle, and vice versa. Functional groups that participate in reaction are His imidazole, alpha-amino group, alpha-carboxyl group, thiol of Cys, R group of carboxyls of Glu and Asp, aromatic OH of Tyr, and guanidino group of ARG. The protonation of these functional groups are dependent on the pH, therefore the enzymatic catalytic activity is sensitive to the pH level.
General acid-base catalysis is involved in a majority of enzymatic reactions, wherein the side chains of various amino acids act as general acids or general basis. General acid–base catalysis needs to be distinguished from specific acid–base catalysis.
* Specific acid–base catalysis means specifically, –OH or H+ accelerates the reaction. The reaction rate is dependent on pH only (which of course is a function of –OH and H+ concentrations), and not on buffer concentration.
* In General acid–base catalysis, the buffer aids in stabilizing the transition state via donation or removal of a proton. Therefore, the rate of the reaction is dependent on the buffer concentration, as well as the appropriate protonation state.

## Example

The pKa of Histidine is close to neutral thus making it the most effective candidate for general acid or base because it can either donate or accept protons. His 119 plays the role of a general acid that donates a proton to 5'-hydroxyl of nucleoside. On the other hand, His 12 acts as a general base which accepting a proton from the 2'-hydroxyl of 3'-nucleotide. As a result, a 2’-3’ cyclic phosphate intermediate is formed. When water replaces the nucleoside, the roles of His 119 and His 12 are reversed. In the end, the original Histidine protonation states are restored.
File:ProtonAcceptingDonating.png His 119 is the acid and His 12 is the base. File:2’-3’ cyclic phosphate intermediate .png A 2'-3' cyclic phosphate intermediate is formed. File:ProtonAcceptingDonatingReversed.png Reversely, His 119 is the base and His 12 is the acid. File:OriginalStateofHis.png His 119 and His 12 return to their initial states.
# Structural Biochemistry/Cell Signaling Pathways/Adenylate Cyclase and cAMP Signaling
## Adenylate Cyclase and cAMP Signaling

Cyclic adenine monophosphate (cAMP) is a secondary messenger used in intercellular signal transduction. The synthesis of cAMP from ATP is done by adenylyl cyclases located in the plasma membrane. The understanding of this signaling mechanism is attributed to Earl W. Sutherland whose work won him the Nobel Prize in 1971.
cAMP is used for intracellular signal transduction and affects a number of cellular processes. For example, cAMP stimulates the production of ATP for muscle contraction. In other cells, cAMP enhances the degradation of storage fuels, increases the secretion of acid by the gastric mucosa, leads to the dispersion of melanin pigment gradules, and diminishes the aggregation of blood platelets. It is also involved in the activation of protein kinases and regulates the effects of adrenaline and glucagon. In addition, cAMP regulates the passage of metal ions, like Ca2+, through ion channels.
cAMP works by activating protein kinase A (PKA). PKA is a normally inactive tetrameric holoenzyme, consisting of two catalytic and two regulatory units (C2R2), with the regulatory units blocking the catalytic centers of the catalytic units. cAMP binds to specific locations on the regulatory units of the protein kinase, and causes dissociation between the regulatory and catalytic subunits, thus activating the catalytic units and enabling them to phosphorylate substrate proteins. Binding of four cAMP molecules causes the release of free and active catalytic subunits, which may phosphorylate serine and threonine residues on target proteins. The figure below shows a cAMP/PKA signaling pathway:
A cAMP/PKA signaling pathway
The active subunits catalyze the transfer of phosphate from ATP to specific serine or threonine residues of protein substrates. The phosphorylated proteins may act directly on the cell's ion channels, or may become activated or inhibited enzymes. PKA can also phosphorylate specific proteins that bind to promoter regions of DNA, causing increased expression of specific genes.

## Mechanism

When a signal is first transducted inside the cell, an enzyme called adenylyl cyclase is activated which converts ATP to cAMP. Then the cAMP activates protein kinase A by binding to the regulatory units in protein kinase A, thereby allowing the disassociation between the catalytic and regulatory subunits in protein kinase A. The newly activated protein kinase A allows for the phosphorylation of serine and threonine from ATP which generates cellular response. This secondary messenger amplifies the signal many times over through the synthesis of many molecules of cAMP by adenylyl cyclase. However, the cAMP molecules do not last long as another enzyme, phosphodiesterase, converts cAMP to AMP which means another signal is necessary in order for another response to occur.
# Structural Biochemistry/Cell Signaling Pathways/Circulatory Systems

The circulatory system is made up of the vessels and the muscles which help and control the flow of the blood around the body. The main components of the circulatory system are the heart, the blood and the blood vessles. It also includes the pulmonary circulation, a loop through the lungs for the blood to be oxygenated and the systemic circulation.
It serves to move blood to a site or sites where it can be oxygenated, and where wastes can be disposed. Circulation then serves to bring newly oxygenated blood to the tissues of the body. The waste produces diffuse into the blood cells to be carried away, when oxygen and other chemicals spread out of the blood cells and into the fluid surrounding the cells of the body's tissues. Blood circulates through organs where wastes are removed, and back to the lungs for a fresh dose of oxygen, and then the process repeats itself.
Open Circulatory Systems In higher animals, there are two primary types of circulatory systems -- open and closed. In an open circulatory system, blood leaves the blood and flows freely within the tissues. There is neither a true heart nor capillaries as are found in humans. Instead, there are blood vessels that act as pumps to force the blood along. Instead of capillaries, blood vessels join directly with open sinuses. A fluid called hemolymph, is forced from the blood vessels into large sinuses, where it actually baths the internal organs. Other vessels receive blood forced from these sinuses and conduct it back to the pumping vessels. This is a very inefficient system. Insects can get by with this type system because they have numerous openings in their bodies that allow the "blood" to come into contact with air. Closed Circulatory Systems The closed circulatory system separates the tissue fluid from blood. The blood is pumped through a closed system of arteries, veins, and capillaries. Capillaries surround the organs, making sure that all cells have an equal opportunity for nourishment and removal of their waste products.
The simplest type of closed circulatory systems is an earthworm. Earthworms have two main blood vessels, a dorsal and a ventral vessel, which carry blood towards the head or the tail. Blood is moved along the dorsal vessel by waves of contraction in the wall of the vessel. In the anterior region of the worm, there are five pairs of vessels, that connect the dorsal and the ventral vessels. These connecting vessels function as basic hearts and force the blood into the ventral vessel. There are also special organs in the earthworm for the removal of nitrogenous wastes. Still, blood can flow backward and the system is only slightly more efficient than the open system of insects.
The closed circulatory system has more advantages over the open circulatory system.
1. The blood transfers faster in the closed system, thus oxygen, nutritients, and wastes transport fast also.
2. Specialized cells help carry nutrients.
3. The blood and the tissue fluid are distinguished easily.
# World Stamp Catalogue/South America
## List of stamp-issuing entities in South America

* Argentina – ARG
** Buenos Aires
** Cordoba
** Corrientes
* Bolivia – BOL
* Brasil – BRA
* Chile – CHL
* Colombia – COL
** Antioquia
** Bolivar
** Boyaca
** Cauca
** Cundinamarca
** Magdalena
** Panama
** Tolima
** Corrientes
* Ecuador – ECU
* Guyana – GUY
* Paraguay – PRY
* Peru – PER
* Surinam – SUR
* Trinidad and Tobago – TRI
* Uruguay – URY
* Venezuela – VEN
# World Stamp Catalogue/S
### S

* Saar
* Sabah
* Saint Christopher Nevis & Anguilla
* Saint Helena
* Saint Kitts-Nevis
* Saint Lucia
* Saint Pierre et Miquelon
* Saint Thomas & Prince Islands
* Saint Vincent
* Samoa
* San Marino
* Sao Tome e Principe
* Sarawak
* Sardinia
* Saudi Arabia
* Saxony
* Senegal
* Serbia
* Serbian Post Abroad
* Seychelles
* Shanghai
* Sharjah
* Siberia
* Sicily
* Sierra Leone
* Singapore
* Slovakia
* Slovenia
* Solomon Islands
* Somalia
* Somaliland Protectorate
* South Africa
* South African Territories
* South Australia
* South Georgia and South Sandwich Islands
* South Korea (Korea)
* South Russia
* South west Africa
* Southern Nigeria
* Southern Rhodesia
* Sovereign Military Order of Malta
* Soviet Union (USSR)
* Spain
* Spanish Colonies
* Spanish Morocco
* Spanish Post Abroad
* Sri Lanka
* Stellaland
* Straits Settlements
* Sudan
* Suriname
* Swaziland
* Sweden
* Swiss Cantonal Issues
* Switzerland
* Syria
# World Stamp Catalogue/Saint Vincent and the Grenadines
## Saint Vincent and the Grenadines

* Postage stamps and postal history of Saint Vincent and the Grenadines
# Trainz/AM&C/Cross-loading JA and libraries

Back to the Top
* Trainz Asset Maintenance and Creation
* TOC | Beginnings | Fun | AM&C | Creation | InBook Refs | ORP Refs:  • Index • Containers • Kinds • Tags | Appendixes  • Vers
Glossary :
HKeys-CM :
HKeys-DVR :
HKeys-SUR :
HKeys-WIN :
Mouse use :
Notations :
Trainz pre-compiled asset Libraries, *.JA files can be uploaded into the next generation Trainz in most cases, and with some limitations. In point of fact, cross loading assets sometimes runs afoul of a incompatibility of scripts in *.gs files when doing so, and correcting these issues can be vexing, as where what changed, and which asset needs which change to work with the newer more modern *.gs files is not always immediately obvious.
It takes a little sleuthing and trial and error, advice seeking on the forums, and is just a spot of bother when an older asset runs afoul of a new system. The problem is rarely serious, though it may block running a particular route for a few days whilst the matter is resolved. Normally, this sort of hidden fault will show as a faulty asset, normally with a KIND and Class message in the Content Manager.
Tip: Remember - The new Trainzer is very unlikely to ever first discover a problem before a ten year veteran Trainzer! Use the information resource of the Auran forums!
To be continued from that start