The structure of apo human glutamate dehydrogenase details subunit communication and allostery (Q27639129)

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English	The structure of apo human glutamate dehydrogenase details subunit communication and allostery	scientific article

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title

The structure of apo human glutamate dehydrogenase details subunit communication and allostery (English)

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author

Thomas J. Smith

object named as

Thomas J Smith

series ordinal

1

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Gary Siuzdak

object named as

Gary Siuzdak

series ordinal

5

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Charles A Stanley

object named as

Charles A Stanley

series ordinal

6

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author name string

Timothy Schmidt

series ordinal

2

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Jie Fang

series ordinal

3

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Jane Wu

series ordinal

4

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language of work or name

English

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publication date

3 May 2002

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published in

Journal of Molecular Biology

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volume

318

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issue

3

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page(s)

765-77

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cites work

The structure of bovine glutamate dehydrogenase provides insights into the mechanism of allostery

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Structures of bovine glutamate dehydrogenase complexes elucidate the mechanism of purine regulation

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Effects of adenosine 5'-diphosphate on bovine glutamate dehydrogenase: diethyl pyrocarbonate modification

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Studies of glutamate dehydrogenase. The influence of ADP, GTP, and L-glutamate on the binding of the reduced coenzyme to beef-liver glutamate dehydrogenase

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Expression, purification and characterization of human glutamate dehydrogenase (GDH) allosteric regulatory mutations

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Negative co-operativity in glutamate dehydrogenase. Involvement of the 2-position in glutamate in the induction of conformational changes

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A syndrome of congenital hyperinsulinism and hyperammonemia

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Linkage-disequilibrium mapping without genotyping

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Probing Protein/Protein Interactions with Mass Spectrometry and Isotopic Labeling: Analysis of the p21/Cdk2 Complex

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Probing protein structure using biochemical and biophysical methods. Proteolysis, matrix-assisted laser desorption/ionization mass spectrometry, high-performance liquid chromatography and size-exclusion chromatography of p21Waf1/Cip1/Sdi1.

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Evidence of Viral Capsid Dynamics Using Limited Proteolysis and Mass Spectrometry

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Crystallographically identical virus capsids display different properties in solution.

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Mass spectrometry in viral proteomics.

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Viral capsid mobility: a dynamic conduit for inactivation.

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Conformational flexibility in glutamate dehydrogenase. Role of water in substrate recognition and catalysis

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Mechanism of hysteresis in bovine glutamate dehydrogenase: role of subunit interactions

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Transduction of enzyme-ligand binding energy into catalytic driving force

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MOLView: A program for analyzing and displaying atomic structures on the Macintosh personal computer

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Subunit assembly and active site location in the structure of glutamate dehydrogenase

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PROCHECK: a program to check the stereochemical quality of protein structures

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7 January 2021

Identifiers

DOI

10.1016/S0022-2836(02)00161-4

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PubMed publication ID

12054821

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