Structural biology of S-adenosylmethionine decarboxylase. - Wikidata - wikimedia - TriplyDB

Structural biology of S-adenosylmethionine decarboxylase.

Structural biology of S-adenosylmethionine decarboxylase.

http://www.wikidata.org/entity/Q33761173

about

Polyamine homoeostasis as a drug target in pathogenic protozoa: peculiarities and possibilities The Concise Guide to PHARMACOLOGY 2013/14: enzymes.S-adenosylmethionine inhibits the growth of cancer cells by reversing the hypomethylation status of c-myc and H-ras in human gastric cancer and colon cancer.DNA methylation regulates expression of VEGF-C, and S-adenosylmethionine is effective for VEGF-C methylation and for inhibiting cancer growth.Prediction and Analysis of Post-Translational Pyruvoyl Residue Modification Sites from Internal Serines in Proteins.Independent evolutionary origins of functional polyamine biosynthetic enzyme fusions catalysing de novo diamine to triamine formation.From Protease to Decarboxylase: THE MOLECULAR METAMORPHOSIS OF PHOSPHATIDYLSERINE DECARBOXYLASE.Discovery of novel inhibitors of human S-adenosylmethionine decarboxylase based on in silico high-throughput screening and a non-radioactive enzymatic assay.Extending enzyme molecular recognition with an expanded amino acid alphabet.Trypanosoma brucei S-adenosylmethionine decarboxylase N terminus is essential for allosteric activation by the regulatory subunit prozyme Current status of the polyamine research field Relief of autoinhibition by conformational switch explains enzyme activation by a catalytically dead paralog Potential role of S-adenosylmethionine in osteosarcoma development.Different polyamine pathways from bacteria have replaced eukaryotic spermidine biosynthesis in ciliates Tetrahymena thermophila and Paramecium tetaurelia.A surprising range of modified-methionyl S-adenosylmethionine analogues support bacterial growth.mTORC1-dependent AMD1 regulation sustains polyamine metabolism in prostate cancer.Unusual post-translational protein modifications: the benefits of sophistication

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P2860

Structural biology of S-adenosylmethionine decarboxylase.

http://www.wikidata.org/entity/Q33761173

description

2009 nî lūn-bûn

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2009 թուականի Դեկտեմբերին հրատարակուած գիտական յօդուած

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2009 թվականի դեկտեմբերին հրատարակված գիտական հոդված

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2009年の論文

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2009年論文

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2009年論文

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2009年論文

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2009年論文

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2009年論文

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2009年论文

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Structural biology of S-adenosylmethionine decarboxylase.

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Structural biology of S-adenosylmethionine decarboxylase.

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Structural biology of S-adenosylmethionine decarboxylase.

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Structural biology of S-adenosylmethionine decarboxylase.

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Structural biology of S-adenosylmethionine decarboxylase.

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Structural biology of S-adenosylmethionine decarboxylase.

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Structural biology of S-adenosylmethionine decarboxylase.

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P2860

The crystal structure of human S-adenosylmethionine decarboxylase at 2.25 A resolution reveals a novel fold

The structural basis for substrate specificity and inhibition of human S-adenosylmethionine decarboxylase

Structure of a human S-adenosylmethionine decarboxylase self-processing ester intermediate and mechanism of putrescine stimulation of processing as revealed by the H243A mutant

Monomeric S-adenosylmethionine decarboxylase from plants provides an alternative to putrescine stimulation

Mechanism of human S-adenosylmethionine decarboxylase proenzyme processing as revealed by the structure of the S68A mutant

Pyruvoyl-dependent arginine decarboxylase from Methanococcus jannaschii: crystal structures of the self-cleaved and S53A proenzyme forms

Structural constraints on protein self-processing in L-aspartate- -decarboxylase

Structures of the N47A and E109Q mutant proteins of pyruvoyl-dependent arginine decarboxylase fromMethanococcus jannaschii

Structural Basis for Putrescine Activation of Human S -Adenosylmethionine Decarboxylase † ‡

New Insights into the Design of Inhibitors of Human S -Adenosylmethionine Decarboxylase: Studies of Adenine C 8 Substitution in Structural Analogues of S -Adenosylmethionine †

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10.1007/S00726-009-0404-Y

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38

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Steven E Ealick

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