Influence of key residues on the reaction mechanism of the cAMP-dependent protein kinase. - Wikidata - wikimedia - TriplyDB

Influence of key residues on the reaction mechanism of the cAMP-dependent protein kinase.

Influence of key residues on the reaction mechanism of the cAMP-dependent protein kinase.

http://www.wikidata.org/entity/Q41954017

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Low- and room-temperature X-ray structures of protein kinase A ternary complexes shed new light on its activity STRUBBELIG defines a receptor kinase-mediated signaling pathway regulating organ development in Arabidopsis.Unique kinase catalytic mechanism of AceK with a single magnesium ion.Elucidation of human choline kinase crystal structures in complex with the products ADP or phosphocholine.Cyclin-dependent kinases: bridging their structure and function through computations.Phosphoryl transfer by a concerted reaction mechanism in UMP/CMP-kinase.The mechanism of phosphorylation of natural nucleosides and anti-HIV analogues by nucleoside diphosphate kinase is independent of their sugar substituents.Theoretical studies of cyclic adenosine monophosphate dependent protein kinase: native enzyme and ground-state and transition-state analogues.Fragment molecular orbital study of the cAMP-dependent protein kinase catalyzed phosphoryl transfer: a comparison with the differential transition state stabilization method.

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P2860

Influence of key residues on the reaction mechanism of the cAMP-dependent protein kinase.

http://www.wikidata.org/entity/Q41954017

description

1999 nî lūn-bûn

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1999年の論文

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1999年論文

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1999年論文

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1999年論文

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1999年論文

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1999年論文

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1999年论文

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1999年论文

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1999年论文

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name

Influence of key residues on the reaction mechanism of the cAMP-dependent protein kinase.

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type

label

Influence of key residues on the reaction mechanism of the cAMP-dependent protein kinase.

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prefLabel

Influence of key residues on the reaction mechanism of the cAMP-dependent protein kinase.

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Protein Science

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Influence of key residues on the reaction mechanism of the cAMP-dependent protein kinase.

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Hutter MC

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P2860

Two structures of the catalytic domain of phosphorylase kinase: an active protein kinase complexed with substrate analogue and product

The protein kinase family: conserved features and deduced phylogeny of the catalytic domains

Active and inactive protein kinases: structural basis for regulation

Conserved water molecules contribute to the extensive network of interactions at the active site of protein kinase A

Electrostatic energy and macromolecular function.

Protein kinases--structure and function.

cAMP-dependent protein kinase: crystallographic insights into substrate recognition and phosphotransfer

Why have mutagenesis studies not located the general base in ras p21.

Rational scanning mutagenesis of a protein kinase identifies functional regions involved in catalysis and substrate interactions.

Is there a catalytic base in the active site of cAMP-dependent protein kinase?

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2728-2733

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10.1110/PS.8.12.2728

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12

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10631989

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2144238

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