The allosteric ligand site in the Vmax-type cooperative enzyme phosphoglycerate dehydrogenase (Q27730185)

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English	The allosteric ligand site in the Vmax-type cooperative enzyme phosphoglycerate dehydrogenase	scientific article

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instance of

scholarly article

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title

The allosteric ligand site in the Vmax-type cooperative enzyme phosphoglycerate dehydrogenase (English)

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author name string

D J Schuller

series ordinal

1

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G A Grant

series ordinal

2

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L J Banaszak

series ordinal

3

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publication date

January 1995

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published in

Nature structural biology

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volume

2

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issue

1

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page(s)

69-76

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cites work

Crystal structure of a NAD-dependent D-glycerate dehydrogenase at 2.4 A resolution

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High resolution structures of holo and apo formate dehydrogenase

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22 April 2017

MOLSCRIPT: a program to produce both detailed and schematic plots of protein structures

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22 April 2017

SETOR: hardware-lighted three-dimensional solid model representations of macromolecules

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22 April 2017

Inhibition of 3-phosphoglycerate dehydrogenase by l-serine

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21 January 2018

Shared structural motif in proteins.

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21 January 2018

ON THE NATURE OF ALLOSTERIC TRANSITIONS: A PLAUSIBLE MODEL

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31 March 2020

A new family of 2-hydroxyacid dehydrogenases

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31 March 2020

Crystal structure of CTP-ligated T state aspartate transcarbamoylase at 2.5 A resolution: implications for ATCase mutants and the mechanism of negative cooperativity

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31 March 2020

Unbiased three-dimensional refinement of heavy-atom parameters by correlation of origin-removed Patterson functions

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31 March 2020

Generalized method of determining heavy-atom positions using the difference Patterson function

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31 March 2020

Crystallographic R factor refinement by molecular dynamics

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31 March 2020

The interpretation of protein structures: Estimation of static accessibility

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31 March 2020

Improved Fourier coefficients for maps using phases from partial structures with errors

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31 March 2020

The Protein Data Bank: a computer-based archival file for macromolecular structures

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31 March 2020

Diffraction methods for biological macromolecules. Interactive computer graphics: FRODO

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retrieved

7 January 2021

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Identifiers

DOI

10.1038/NSB0195-69

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Consolidated OpenCitations Corpus – April 2017

OpenCitations bibliographic resource ID

2461191

OpenCitations bibliographic resource ID

2461191

1 reference

stated in

Consolidated OpenCitations Corpus – April 2017

OpenCitations bibliographic resource ID

2461191

PubMed publication ID

7719856

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stated in

Consolidated OpenCitations Corpus – April 2017

OpenCitations bibliographic resource ID

2461191

ResearchGate publication ID

15479044

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