The genetic organization and protein crystallographic structure of human serine hydroxymethyltransferase-Reference-Cited by-同舟云学术

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The genetic organization and protein crystallographic structure of human serine hydroxymethyltransferase

Published:2000-06 Issue:1 Volume:40 Page:353-403
ISSN:0065-2571
Container-title:Advances in Enzyme Regulation
language:en
Short-container-title:Advances in Enzyme Regulation

Author:

Snell Keith,Baumann Ulrich,Byrne Paula C,Chave Karen J,Renwick Suzanne B,Sanders Peter G,Whitehouse Suzanna K

Publisher

Elsevier BV

Subject

Cancer Research,Genetics,Molecular Biology,Molecular Medicine

Reference90 articles.

1. Control analysis of mammalian serine biosynthesis: feedback inhibition on the final step;Fell;Biochem. J.,1988

2. Metabolic control analysis of mammalian serine metabolism;Snell;Advan. Enzyme Regul.,1989

3. Enzymes of serine metabolism in normal, developing and neoplastic rat tissues;Snell;Advan. Enzyme Regul.,1984

4. The modulation of serine metabolism in hepatoma 3924A during different phases of cellular proliferation in culture;Snell;Biochem. J.,1987

5. Serine metabolism in lectin-activated lymphocytes;Snell;Biochem. Soc. Trans.,1988

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2. Exploring the Cold-Adaptation Mechanism of Serine Hydroxymethyltransferase by Comparative Molecular Dynamics Simulations;International Journal of Molecular Sciences;2021-02-11

3. A flap motif in human serine hydroxymethyltransferase is important for structural stabilization, ligand binding, and control of product release;Journal of Biological Chemistry;2019-07

4. Association of Thymidylate Synthase 5'-UTR 28bp Tandem Repeat and Serine Hydroxymethyltransfarase C1420T Polymorphisms with Susceptibility to Acute Leukemia;Asian Pacific Journal of Cancer Prevention;2014-02-28

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