Engineering a trifunctional proline utilization A chimaera by fusing a DNA-binding domain to a bifunctional PutA. - Wikidata - wikimedia - TriplyDB

Engineering a trifunctional proline utilization A chimaera by fusing a DNA-binding domain to a bifunctional PutA.

Engineering a trifunctional proline utilization A chimaera by fusing a DNA-binding domain to a bifunctional PutA.

http://www.wikidata.org/entity/Q37626806

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Structure, function, and mechanism of proline utilization A (PutA).Discovery of the Membrane Binding Domain in Trifunctional Proline Utilization A.Structure and characterization of a class 3B proline utilization A: Ligand-induced dimerization and importance of the C-terminal domain for catalysis.

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Engineering a trifunctional proline utilization A chimaera by fusing a DNA-binding domain to a bifunctional PutA.

http://www.wikidata.org/entity/Q37626806

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article científic

@ca

article scientifique

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articolo scientifico

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artigo científico

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bilimsel makale

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scientific article published on 14 October 2016

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vedecký článok

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vetenskaplig artikel

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videnskabelig artikel

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vědecký článek

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Engineering a trifunctional pr ...... domain to a bifunctional PutA.

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Engineering a trifunctional pr ...... domain to a bifunctional PutA.

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Engineering a trifunctional pr ...... domain to a bifunctional PutA.

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Engineering a trifunctional pr ...... domain to a bifunctional PutA.

@nl

prefLabel

Engineering a trifunctional pr ...... domain to a bifunctional PutA.

@en

Engineering a trifunctional pr ...... domain to a bifunctional PutA.

@nl

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Bioscience Reports

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Engineering a trifunctional pr ...... domain to a bifunctional PutA

@en

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Benjamin W Arentson

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

Donald F Becker

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

Erin L Hayes

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

Harkewal Singh

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

Weidong Zhu

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P2860

A compelling genetic hypothesis for a complex disease: PRODH2/DGCR6 variation leads to schizophrenia susceptibility.

Redox-Induced Changes in Flavin Structure and Roles of Flavin N(5) and the Ribityl 2‘-OH Group in Regulating PutA−Membrane Binding † , ‡

Structural Basis of the Transcriptional Regulation of the Proline Utilization Regulon by Multifunctional PutA

The Structure of the Proline Utilization A Proline Dehydrogenase Domain Inactivated by N -Propargylglycine Provides Insight into Conformational Changes Induced by Substrate Binding and Flavin Reduction ,

Crystal structure of the bifunctional proline utilization A flavoenzyme from Bradyrhizobium japonicum

Crystal Structures and Kinetics of Monofunctional Proline Dehydrogenase Provide Insight into Substrate Recognition and Conformational Changes Associated with Flavin Reduction and Product Release

Involvement of the β3-α3 Loop of the Proline Dehydrogenase Domain in Allosteric Regulation of Membrane Association of Proline Utilization A

Structural Determinants of Oligomerization of Δ1-Pyrroline-5-Carboxylate Dehydrogenase: Identification of a Hexamerization Hot Spot

Structures of the PutA peripheral membrane flavoenzyme reveal a dynamic substrate-channeling tunnel and the quinone-binding site

UCSF Chimera--a visualization system for exploratory research and analysis

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scholarly article

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10.1042/BSR20160435

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6

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36

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2016-11-22T00:00:00Z

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27742866

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5293562

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