OpenLLM-France/wikimedia huggingface dataset:
# SAASTE Technology/Key Concepts/Grade 9

KEY
CONCEPTS, KEY FOCUS and IMPLICATIONS for TEACHING & LEARNING
of Technology through the RNCS :
| Grade 9 |||
| Investigates: identify & explain problem, need or opportunity in context Existing products - analyses - (relevant to problem and based on specified design aspects) Practical tests / testing Data handling (Locate, collect, compare, sort, verify, evaluate, store, presents and uses the information to justify and support decisions) | Systems & Control: Analyse systems and sub- systems Drawing systems diagrams Combining different sub- systems to create systems. Input - Process and Output Components of electronic circuits. Reading, Drawing & Building electronic circuits. Input - Process and Output Drawing system diagrams | Impacts: technological developments (Recognise & identify impacts on society/ environment and suggest strategies to reduce any negative impacts) |
| Designs: Design brief Lists specifications and constraints based on specified design aspects. possible solutions- significantly different- (linked to design brief & specifications and/or constraints.) choice of solution with reasons chosen solution developed further -(graphics) | Processing: Preservation of materials (galvanised, frozen, dried, painted, varnished, electroplated) Manufacture of products from recyclable materials. | Biases: Human rights (Opinions backed by factual evidence on technological decisions and suggest strategies for redress) |
| Makes: Planning Materials list Tools list Construction techniques Design adaption Safety, efficient material and tools use | Structures : Effect in performance of materials based on their properties Analysis of the effect of loads. | Indigenous Technology: Cultures (Compare and explain global (world) adaptation of technological solutions for optimal benefit) |
| Evaluates: identifying strengths and weaknesses of: Product, System and of plan of action Generating and using (own) objective criteria suggestions for improvement / modification | | |
| Communicates: 2D (1st / 3rd angle) or 3D (isometric, perspective, oblique) enhanced sketches / drawings (colour/ shading/ rendering) circuit diagrams (circuit symbols) systems diagrams (input, process, output) notes, labels, dimensions, list of quantities. SA drawing conventions (for above) Appropriate use of Technology to present information for particular target audience | | |
# SAP ERP/Accounts Receivable
## Financial Accounting in one of the important part is Account receivable which very important process.
###### In this world paper work is very old dated because of computers developments, its grown so much were can't see the end point of its way.

Account receivable is changed from oldschool to new age(next generation) of electrical storage and digitalised. In digitalised system were
we can store any number of datas can store this storeage is also being as big commercial business today life even future too.
Account receivable is one of important part of financial accounting which is help to consolidate and digitalised journal entries can be
processed between customer to bank so receiving payments was noted by systematically which takes help form humans in priority mannar.
which easly to approach and it has good clearity of view and storing datas.
This process is hlep to pass the journals then taking to the next level of process in a easy way. Other process can be done followed by
as per their requirements. which we can track for future purpose also.
Account receivable is a gateway of income for all scenarios.
# SAASTE Technology/Modules

Our modules are complete units of work that contain a series of enabling activities / tasks and a challenge.
Each of these modules is designed to provide the learner with an opportunity to apply knowledge and skills in an authentic situation.
* Processing Grade 8/9
* Mechanical Systems Grade 9
* Structures Grade 5
* Structures Grade 8
# Radiation Oncology/Toxicity grading/CTCAE

* Front Page: Radiation Oncology | RTOG Trials | Randomized Trials
NCI Common Terminology Criteria for Adverse Events (CTCAE)
# Radiation Oncology/Treatment planning/NTCP

* Front Page: Radiation Oncology | RTOG Trials | Randomized Trials
This page deals with concepts of Normal tissue complication probability, or NTCP.
    See also: Radiation_Oncology/Normal_tissue_tolerance
* Full text No PMID — "Use of normal tissue tolerance doses into linear quadratic equation to estimate normal tissue complicatio probability." T. S. Kehwar, Ph.D., D.Sc. and S. C. Sharma, M.D. Radiation Oncology Online Journal (www.rooj.com).
** Tables 3 and 4 are most helpful.
* Full text PMID 17998649 — "Analytical approach to estimate normal tissue complication probability using best fit of normal tissue tolerance doses into the NTCP equation of the linear quadratic model." T. S. Kehwar, D.Sc., DABR. Journal of Cancer Research and Therapeutics.
** See especially Table 4
# Radiation Oncology/Treatment time

* Front Page: Radiation Oncology | RTOG Trials | Randomized Trials
This page discusses how the time from surgery, overall treatment time, and time to deliver a fraction have an impact on the success of treatment.
    See also: the appropriate Radiobiology concepts.
The concept of surgery to radiotherapy interval (SRI):
* effect of boost dose
* sequencing of chemotherapy and radiotherapy (in particular for breast cancer)
* Radiation Oncology:H&N - see discussion for head and neck tumors
* Radiation Oncology:Breast overview - see discussion for breast cancer
The concept of overall treatment time:

## Head & Neck

* Aarhus, 2007 (Denmark) PMID 17493700 -- "Tumor progression in waiting time for radiotherapy in head and neck cancer." (Jensen AR, Radiother Oncol. 2007 Jul;84(1):5-10.)
** Retrospective. 61 patients with SCCHN, with diagnostic and treatment-planning CT scan. Median interval between scans 28 days (5-95)
** Outcome: 62% patients measurable increase in tumor volume; median increase 46% (6-495%). 20% new LN mets, 16% progression in T-stage
** Doubling time: median 99 days, but median for faster half was 30 days.
** Conclusion: Negative impact of waiting time; majority showed progression within 4 week waiting time
** Editorial PMID 17574695 -- "Killing time: The consequences of delays in radiotherapy." (Mackillop WJ, Radiother Oncol. 2007 Jul;84(1):1-4.)
* Wisconsin; 2007 PMID 17305251 -- "Is there an optimum overall time for head and neck radiotherapy? A review, with new modelling." (Fowler JF, Clin Oncol (R Coll Radiol). 2007 Feb;19(1):8-22.)
** LQ modelling for various schedules, calculated tumor log cell kill, with acute and late complications
** Conclusion: Schedules of 4-6 weeks give 11 log10 cell kill; most require two fractions/day
* Ontario, 1996 PMID 12118558 -- "The effect of delay in treatment on local control by radiotherapy." (Mackillop WJ, Int J Radiat Oncol Biol Phys. 1996 Jan 1;34(1):243-50.)
** Monte Carlo simulation, applied to tonsillar CA
** Outcome: at some point for every patient, probability of local control decreases sharply over a relatively short time period. LC rate decreases by ~10% per month for tonsillar CA
** Conclusion: Waiting times for RT should be As Short As Reasonably Achievable (ASARA)

## NSCLC

* Netherlands; 2003 PMID 14676792 -- "Accelerated regrowth of non-small-cell lung tumours after induction chemotherapy." (El Sharouni SY, Br J Cancer. 2003 Dec 15;89(12):2184-9.)
** Retrospective. 23 patients with NSCLC. Interval times between end of induction of start of RT evaluated. Mean time to RT 80 days
** Outcome: 41% potentially curable patients became incurable; tumor median doubling 29 days (8.3-171 days)
** Conclusion: Accelerated tumor cell proliferation, much shorter doubling time than for untreated tumors. Gain from chemo (tumor decrease) was lost with waiting for RT
# Radiation Oncology/Toxicity grading

* Front Page: Radiation Oncology | RTOG Trials | Randomized Trials
Toxicity Grading
* NCI Common Terminology Criteria for Adverse Events (CTCAE)
* RTOG/EORTC Toxicity Grading
* LENT SOMA Toxicity Grading
# Radiation Oncology/Toxicity grading/LENT SOMA

* Front Page: Radiation Oncology | RTOG Trials | Randomized Trials
LENT SOMA Toxicity Grading
From Late Effects of Normal Tissues (LENT) Consensus Conference
# Radiation Oncology/Treatment planning/Ergonomics

* The International Ergonomics Association defines ergonomics or human factors as follows:
** Ergonomics (or human factors) is the scientific discipline concerned with the understanding of interactions among humans and other elements of a system, and the profession that applies theory, principles, data and methods to design to optimize human well-being and overall system performance
* Alvita J Chan et al. Radiother Oncol. 2010 Dec. The use of human factors methods to identify and mitigate safety issues in radiation therapy (PMID: 21044802)
# Radiation Oncology/Treatment planning/Motion

* Front Page: Radiation Oncology | RTOG Trials | Randomized Trials
Tumor and Organ At Risk Motion

## Abdominal Tumors

* PMID 15817361, 2005 — "The correlation between internal and external markers for abdominal tumors: implications for respiratory gating." Gierga BP et al. Int J Radiat Oncol Biol Phys. 2005 Apr 1;61(5):1551-8.
** 4 pts. liver tumors.
* PMID 15050340, 2004 — "Quantification of respiration-induced abdominal tumor motion and its impact on IMRT dose distributions." Gierga BP et al. Int J Radiat Oncol Biol Phys. 2004 Apr 1;58(5):1584-95.
** Used surgical clips and fluroscopy. 7 pts (6 pancreas, 1 liver).
** Average peak-to-peak motion (i.e., twice the amplitude): LR < 2mm, CC 7.4mm, AP 3.8mm
** IMRT plan using PTV margin of 8 mm (accounting for tumor motion only, not setup inaccuracy)

## Abdominal Organs

* Pittsburgh; 2006 PMID 16690437 -- "Abdominal organ motion measured using 4D CT." (Brandner ED, Int J Radiat Oncol Biol Phys. 2006 Jun 1;65(2):554-60.)
** 4D CT scanning, 13 patients
** sup-inf organ motion: liver 1.3 cm, spleen 1.3 cm, left kidney 1.1 cm, right kidney 1.3 cm
** Conclusion: 4D CT can accurately measure abdominal organ motion throughout respiration
# Radiation Oncology/Treatment planning

* Front Page: Radiation Oncology | RTOG Trials | Randomized Trials
Radiation Therapy Treatment Planning
* Contraindications to radiotherapy
* Anatomy
* Contouring
* Bone marrow distribution
* Examples of treatment fields
* Motion
* IMRT
* Devices used in simulation
* Treatment of patients with pacemakers
* Fetal dose (TG 36) (see also: AAPM Reports page)
* Dose evaluation
* Radiomics
* Molecular Imaging
* Monte Carlo (MC) Method (PMID: 29945636)
* Artificial Intelligence (PMID: 31495281)
* Ergonomics (PMID: 22316817)
# Proteomics/Protein Separations - Chromatography/Hydrophobic Interaction Chromatography (HIC)

Chapter written by: Laura Grell and Alexander Butarbutar
Contact llg3875@rit.edu or nbb3924@rit.edu for contributions
Chapter modified by Kai Burnett and Dalia Ghoneim
Contact kab9783@rit.edu or dxg6098@rit.edu

## Hydrophobic Interaction Chromatography (HIC)

Hydrophobic Interaction Chromatography is a separation technique that uses the properties of hydrophobicity to separate proteins from one another. In this type of chromatography, hydrophobic groups such as phenyl, octyl, or butyl, are attached to the stationary column. Proteins that pass through the column that have hydrophobic amino acid side chains on their surfaces are able to interact with and bind to the hydrophobic groups on the column.
HIC separations are often designed using the opposite conditions of those used in ion exchange chromatography. In this separation, a buffer with a high ionic strength, usually ammonium sulfate, is initially applied to the column. The salt in the buffer reduces the solvation of sample solutes thus as solvation decreases, hydrophobic regions that become exposed are adsorbed by the medium.
(Res1). The more hydrophobic the molecule, the less salt needed to promote binding (Res1). To elute the proteins, the salt concentration is gradually decreased, eluting bound species in order of increasing hydrophobicity. Additionally, elution can also be achieved through the use of mild organic modifiers or detergent (Res1).
The stationary phase is designed to form hydrophobic interactions with other molecules. These interactions are too weak in water. However, addition of salts to the buffer result in hydrophobic interactions. The following is a list of salts that increase hydrophobic interactions in the order of their ability to enhance interactions:
* Na$_2$SO$_4$
* K$_2$SO$_4$
* (NH$_4$)$_2$SO$_4$
* NaCl
* NH$_4$Cl
* NaBr
* NaSCN
Although reversed phase chromatography and hydrophobic interaction chromatography are very similar, the ligands in reversed phase chromatography are much more hydrophobic than the ligands in hydrophobic interaction chromatography. This enables hydrophobic interaction chromatography to make use of more moderate elution conditions, which do not disrupt the sample nearly as much.
< Previous Page | Next Page >

## Resources

* Bio-Rad Hydrophobic Interaction & Products
* GE Healthcare Hydrophobic Interaction Chromatography Animation || Introduction to Hydrophobic Interaction & Products
# Proteomics/Protein Separations - Chromatography/Cation Exchangers
## Cation Exchangers

Cation exchangers are named for their ability to attract cations or positively charged particles. In this case, the resin of the chromatography system is negatively charged and proteins will bind if the buffer pH is less than the protein’s unique isoelcetric point.
Just as with anion exchangers, cation exchangers can be classified as either weak or strong. A weak cation exchanger is comprised of a weak acid that gradually loses its charge as the pH decreases, while a strong anion exchanger is comprised of a strong acid that is able to sustain its charge over a wide pH range. Carboxymethal groups are used commonly as weak cation exchangers, while sulfopropyl groups are widely used as strong cation exchangers (Res1)

## Designing a Cation Exchange Separation

Selecting the correct resin and buffer is critical as it determines the binding properties of proteins to the resin. In cation exchange, the protein of interests needs to be positively charge to bind to the negatively charged stationary phase. Suppose we have a mixture of the following protein :
| Protein | pI | pH 4.8 cm | pH 7.2 cm | pH 8 cm |
| Carbonic Anhydrase | 7.0 | +16.5 | -0.4 | -2.7 |
| Carboxypeptidase B | 6.2 | +12.0 | -3.3 | -6.3 |
| Chymotrypsin | 8.0 | +9.0 | +2.7 | 0.0 |
| Lysozyme | 9.8 | +14.1 | +7.9 | +6.9 |
* At pH 4.8 cm all protein will bind to the cation exchanger, with carbonic anhydrase binding the strongest to the stationary. If elution is performed at this pH, the protein will elute in the order of chymotrypsin, carboxypeptidase B, lysozyme, and carbonic anhydrase.
* At pH 7.2 cm, cm, carbonic anhydrase and carboxypeptidase B will elute in the wash (before the gradient is initiated), followed by chymotrypsin, then lysozyme during the salt gradient.
* AtpH 8 cm, only the lysozyme will bind to the stationary phase, the other three proteins will elute in the wash.
It is also possible to refine the salt concentration in solvents A and B so that the more weakly bound proteins will wash off the column in the wash, even if they are positively charged. For example, if you modify pH 4.8 cm to have 0.1 M NaCl in solvent A and 0.2 M NaCl in solvent B, you find that the most weakly bound protein (chymotrypsin) elutes in the wash, while the other three elute in the gradient.

## Resources

* Craig. P, Rochester Institute of Technology, Designing a Cation Exchange Separation
# Proteomics/Protein Separations - Chromatography/Chromatography Theory

Chapter written by: Laura Grell and Alexander Butarbutar
Contact llg3875@rit.edu or nbb3924@rit.edu for contributions
Chapter modified by Kai Burnett and Dalia Ghoneim
Contact kab9783@rit.edu or dxg6098@rit.edu

## Chromatography Theory

Chromatography is a method of separating molecule. The method takes advantage of differences between a mobile phase and a stationary phase to separate the different components in a mixture. The target molecules can interact with the stationary phase based on characteristics such as charge, size, and hydrophobicity.
There are two theories of Chromatography:
* Plate theory
* Rate theory

### Plate Theory of Chromatography

Archer John Porter Martin and Richard Laurence Millington Synge created the plate theory of chromatography. The plate theory describes the stationary phase and the mobile phase as being in equilibrium. The partition coefficient k between these two plates can be defined as:
    $K={\frac {Concentration\ of\ solute\ in\ stationary\ phase}{Concentration\ of\ solute\ in\ mobile\ phase}}$
As k increases, the time it takes for the solutes to separate increases. If chromatography is being performed in a column of fixed length and flow rate, the retention time $(t_{R})$ and retention volume $(V_{r})$ can be measured and used to determine the value of K.

### Rate Theory of Chromatography

Rate theory was introduced by van Deemter to account for chromatographic behavior that could not be explained by plate theory. Rate theory is based on three terms: path-dependent diffusion (A),longitudinal diffusion (B) and mass transfer (C).
A. Path-dependent diffusion occurs when the packing in a chromatography column is not uniform, so that two identical analytes may migrate differently because one had further to travel than the other.
B. Longitudinal diffusion is the result of materials moving from an area of high concentration (the center of a band on a chromatography column) to an area of low concentration (the outside edges of the same band). Longitudinal diffusion increases with increasing temperature.
C. Mass transfer effects result from the fact that materials take time to equilibrate between the stationary and mobile phases. While that time is elapsing, the mobile phase is still moving. This leads to band broadening.

## References

* Chromatography on Wikipedia
# Proteomics/Protein Separations - Centrifugation/Preparative Centrifugation vs. Analytical Centrifugation

Table of Contents: Protein Separations - Centrifugation
* History of the Centrifuge
* How the Centrifuge Works
* Density Gradient Centrifugation
* Differential Centrifugation
* Preparative Centrifugation vs. Analytical Centrifugation

## Two types of ultracentrifuges developed: analytical and preparative
### Analytical

· Uses small sample size (less than 1 ml)
· Built in optical system to analyze progress of molecules during centrifugation
· Uses relatively pure sample
· Used to precisely determine sedimentation coefficient and MW of molecules
· Beckman Model E is an example of centrifuge used for these purposes.

### Preparative

· Larger sample size can be used
· No optical read-out – collect fractions and analyze them after the run
· Less pure sample can be used
· Can be used to estimate sedimentation coefficient and MW
· Generally used to separate organelles and molecules. Most centrifugation work done using preparative ultracentrifuge
· Several models available, including L5-65 and L5-75 used for preparative purposes.
# Proteomics/Protein Separations - Chromatography/Immobilized Metal Ion Affinity Chromatography (IMAC)

Chapter written by: Laura Grell and Alexander Butarbutar
Contact llg3875@rit.edu or nbb3924@rit.edu for contributions
Chapter modified by Kai Burnett and Dalia Ghoneim
Contact kab9783@rit.edu or dxg6098@rit.edu

## Immobilized Metal Ion Affinity Chromatography (IMAC)

Immobilized metal ion/Metal Chelate affinity chromatography is a separation technique that is based on coordinate covalent binding between proteins and metal ions. Proteins have a wide variety of amino acids composition which, in effect, generates a range of different affinities towards metal ions. However, not many naturally occurring proteins have affinity for metal ions, so the technique is mainly used to purify recombinant proteins. For example, proteins can be engineered to contain a poly-histidine tail (histidine can generally act as a ligand towards divalent metal cations). If the stationary phase is immobilized with divalent metal cations, a mixture of proteins can be separated based on their ability to interact with the metal ions. Those proteins containing a higher number of histidine residues would be able to bind to the column more tightly than those with fewer histidine residues.
Several different types of immobilized metal ion column have been developed to separate various proteins (e.g. Fe, Co, Cd, Ni, or Zn). Protein separation in IMAC generally depends on the strength of the metal ion-protein bond. Thus, choosing the type of immobilized ion is crucial to successful protein separation. By far the most widely-used technique is to use an immobilized nickel column, and to engineer poly-histidine tags of six or more residues onto the recombinant proteins of interest. One thing to keep in mind is that the binding between metal ion and protein must be reversible, allowing elution of bounded protein at later steps. Three different elution strategies can be applied to IMAC competitive elution, stripping elution and pH Adjustment (Ref1).
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## Resources

* Affiland Immobilized metal ion affinity chromatography (IMAC)
* GE Healthcare Immobilized metal ion affinity chromatography products
* Merck Metal Chelate Affinity Chromatography Using Tentacle Gels
* Bio-Rad Profinity IMAC Resins

## References

* Paunovic. I, Schulin. R, Nowack, B. Evaluation of immobilized metal-ion affinity chromatography for the fractionation of natural Cu complexing ligands Journal of Chromatography A, 1100 (2005) 176–184. *
* Yip TT, Hutchens TW. Immobilized metal-ion affinity chromatography. Methods Mol Biol. 2004;244:179-90.
* Sun X, Chiu JF, He QY.Application of immobilized metal affinity chromatography in proteomics. Expert Rev Proteomics. 2005 Oct;2(5):649-57. *
* Zachariou M. Immobilized metal ion affinity chromatography of proteins. Methods Mol Biol. 2004;251:89-102.
* Belew M, Porath J. Immobilized metal ion affinity chromatography. Effect of solute structure, ligand density and salt concentration on the retention of peptides. J Chromatogr. 1990 Sep 21;516(2):333-54.
.* Denotes Free Article
# Proteomics/Protein Separations - Chromatography/Anion exchangers
## Anion Exchangers

While the resin involved with an anion exchanger is positively charged, anion exchangers are named so because of their affinity to anions. To effectively bind proteins, the pH of the buffer in the system must be greater than the isoelectric point of the protein of interest, as proteins are negatively charged above their isoelectric point.
Anion exchangers can be classified as either weak or strong. The charged group on a weak exchanger is a weak base that easily loses its charge at a high pH due to deprotonation. On the other hand, strong anion exchangers are comprised of a charged group that is a strong base. Strong anion exchangers are able to maintain their positive charges across a variable pH range while weak anion exchangers tend to lose their charge as the pH increases. Examples of anion exchangers include the strong anion exchanger Q (quaternary resin), and the weak anion exchanger DEAE (diethylaminoethane).
Typically, the chromatography is performed using buffers at pH's between 7 and 10 and running a gradient from a solution containing just this buffer to a solution containing this buffer with 1M NaCl (Res1). The salt (in solution) competes for binding to the stationary phase, thus releasing the protein from its bound state. Proteins separate because the amount of salt needed to compete varies with the external charge of the protein. Anion exchange chromatography have been successfully used to clean up of a crude slurry, separation of proteins from each other, concentrating a protein, and the removal of negatively charged endotoxin from protein preparations (Res1).

## Resources

* Proteinchemist.com Ion Exchange Chromatography (IEC)
* Whatman Advanced Ion Exchange Cellulose and Column Chromatography
# Pinyin/Steal

See also
# Pinyin/State-Run

Search Pinyin state
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# Pinyin/Statue

See also