User:Arthur Migliatti/Sandbox1

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<scene name='91/911850/Trx_cysteines_-_oxidized/1'>Catalytic site oxidized</scene>
<scene name='91/911850/Trx_cysteines_-_oxidized/1'>Catalytic site oxidized</scene>
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pmkml<Structure load='1trs' size='350' frame='true' align='right' caption='Insert caption here' scene='Insert optional scene name here' />
Trx and TrxR were first discovered in 1964 in a study realized in bacteria, and were described as necessary proteins to reduce '''[[Ribonucleotide Reductase]]'''(RNR), a protein that produces deoxyribonucleotides from ribonucleotides<ref>Laurent, T. C.; Moore, E. C.; Reichard, P. ENZYMATIC SYNTHESIS OF DEOXYRIBONUCLEOTIDES. IV. ISOLATION AND CHARACTERIZATION OF THIOREDOXIN, THE HYDROGEN DONOR FROM ESCHERICHIA COLI B. J Biol Chem 1964, 239, 3436–3444.</ref>. Since 1964, functions of Trx1 different than participating in cell division were discovered, as denitrosation, transnitrosation, deglutathionylation,
Trx and TrxR were first discovered in 1964 in a study realized in bacteria, and were described as necessary proteins to reduce '''[[Ribonucleotide Reductase]]'''(RNR), a protein that produces deoxyribonucleotides from ribonucleotides<ref>Laurent, T. C.; Moore, E. C.; Reichard, P. ENZYMATIC SYNTHESIS OF DEOXYRIBONUCLEOTIDES. IV. ISOLATION AND CHARACTERIZATION OF THIOREDOXIN, THE HYDROGEN DONOR FROM ESCHERICHIA COLI B. J Biol Chem 1964, 239, 3436–3444.</ref>. Since 1964, functions of Trx1 different than participating in cell division were discovered, as denitrosation, transnitrosation, deglutathionylation,

Revision as of 17:49, 13 June 2022

Introduction

This is a default text for your page Arthur Migliatti/Sandbox1. Click above on edit this page to modify. Be careful with the < and > signs. You may include any references to papers as in: the use of JSmol in Proteopedia [1] or to the article describing Jmol [2] to the rescue.

Human Thioredoxin 1

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References

  1. ↑ Hanson, R. M., Prilusky, J., Renjian, Z., Nakane, T. and Sussman, J. L. (2013), JSmol and the Next-Generation Web-Based Representation of 3D Molecular Structure as Applied to Proteopedia. Isr. J. Chem., 53:207-216. doi:http://dx.doi.org/10.1002/ijch.201300024
  2. ↑ Herraez A. Biomolecules in the computer: Jmol to the rescue. Biochem Mol Biol Educ. 2006 Jul;34(4):255-61. doi: 10.1002/bmb.2006.494034042644. PMID:21638687 doi:10.1002/bmb.2006.494034042644
  3. ↑ Lu, J.; Holmgren, A. The Thioredoxin Antioxidant System. Free Radical Biology and Medicine 2014, 66, 75–87. https://doi.org/10.1016/j.freeradbiomed.2013.07.036.
  4. ↑ Laurent, T. C.; Moore, E. C.; Reichard, P. ENZYMATIC SYNTHESIS OF DEOXYRIBONUCLEOTIDES. IV. ISOLATION AND CHARACTERIZATION OF THIOREDOXIN, THE HYDROGEN DONOR FROM ESCHERICHIA COLI B. J Biol Chem 1964, 239, 3436–3444.

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Arthur Migliatti

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