Bacillus anthracis Prolyl 4-Hydroxylase Interacts with and Modifies Elongation Factor Tu.

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Bacillus anthracis Prolyl 4-Hydroxylase Interacts with and Modifies Elongation Factor Tu.

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2017 nî lūn-bûn

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2017年論文

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Bacillus anthracis Prolyl 4-Hydroxylase Interacts with and Modifies Elongation Factor Tu.

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Bacillus anthracis Prolyl 4-Hydroxylase Interacts with and Modifies Elongation Factor Tu.

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Bacillus anthracis Prolyl 4-Hydroxylase Interacts with and Modifies Elongation Factor Tu.

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P1476

Bacillus anthracis Prolyl 4-Hydroxylase Interacts with and Modifies Elongation Factor Tu.

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P2093

Mortezaali Razzaghi

http://www.w3.org/2001/XMLSchema#string

Sanjukta Guha Thakurta

http://www.w3.org/2001/XMLSchema#string

Srinivas Chakravarthy

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P2860

I-TASSER: a unified platform for automated protein structure and function prediction

Prolyl 4-hydroxylase

Whole proteome analysis of post-translational modifications: applications of mass-spectrometry for proteogenomic annotation

Post-translational hydroxylation by 2OG/Fe(II)-dependent oxygenases as a novel regulatory mechanism in bacteria

Structural bases of collagen stabilization induced by proline hydroxylation

The Crystal Structure of an Algal Prolyl 4-Hydroxylase Complexed with a Proline-rich Peptide Reveals a Novel Buried Tripeptide Binding Motif

Structural basis for binding of hypoxia-inducible factor to the oxygen-sensing prolyl hydroxylases

Crystal Structure of Prolyl 4-Hydroxylase from Bacillus anthracis

Structural Basis of Regiospecificity of a Mononuclear Iron Enzyme in Antibiotic Fosfomycin Biosynthesis

The structural motifs for substrate binding and dimerization of the α subunit of collagen prolyl 4-hydroxylase

P304

5771-5785

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P31

scholarly article

P356

10.1021/ACS.BIOCHEM.7B00601

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P407

English

P433

http://www.w3.org/2001/XMLSchema#string

P478

http://www.w3.org/2001/XMLSchema#string

P50

Mishtu Dey

Nicholas J Schnicker

P577

2017-10-05T00:00:00Z

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P698

28981257

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P932

5735995

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