Structural basis for ordered substrate binding and cooperativity in aspartate transcarbamoylase.
about
From Genome to Structure and Back Again: A Family Portrait of the TranscarbamylasesThe first high pH structure ofEscherichia coliaspartate transcarbamoylaseThe Pathway of Product Release from the R State of Aspartate TranscarbamoylaseA Cooperative Escherichia coli Aspartate Transcarbamoylase without Regulatory Subunits,Crystallographic Snapshots of the Complete Catalytic Cycle of the Unregulated Aspartate Transcarbamoylase from Bacillus subtilisThe ygeW encoded protein from Escherichia coli is a knotted ancestral catabolic transcarbamylaseMetal Ion Involvement in the Allosteric Mechanism of Escherichia coli Aspartate TranscarbamoylaseStructure of the catalytic chain ofMethanococcus jannaschiiaspartate transcarbamoylase in a hexagonal crystal form: insights into the path of carbamoyl phosphate to the active site of the enzymeStructure and mechanisms of Escherichia coli aspartate transcarbamoylaseTime Evolution of the Quaternary Structure of Escherichia coli Aspartate Transcarbamoylase upon Reaction with the Natural Substrates and a Slow, Tight-Binding InhibitorX-ray Scattering Studies of Protein Structural Dynamics.Statistical Mechanics of Allosteric Enzymes.Asymmetric allosteric signaling in aspartate transcarbamoylase.Specific non-local interactions are not necessary for recovering native protein dynamics.Direct observation in solution of a preexisting structural equilibrium for a mutant of the allosteric aspartate transcarbamoylase.Allostery and cooperativity in Escherichia coli aspartate transcarbamoylaseN-phosphonacetyl-L-isoasparagine a potent and specific inhibitor of Escherichia coli aspartate transcarbamoylase.Mechanism of thermal decomposition of carbamoyl phosphate and its stabilization by aspartate and ornithine transcarbamoylasesSolution NMR Spectroscopy for the Study of Enzyme Allostery.Structural model of the R state of Escherichia coli aspartate transcarbamoylase with substrates bound.Conformational selection or induced fit? 50 years of debate resolved.Interpretation of solution x-ray scattering by explicit-solvent molecular dynamics.Dissecting enzyme regulation by multiple allosteric effectors: nucleotide regulation of aspartate transcarbamoylase.Allosteric transition and binding of small molecule effectors causes curvature change in central β-sheets of selected enzymes.
P2860
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P2860
Structural basis for ordered substrate binding and cooperativity in aspartate transcarbamoylase.
description
2005 nî lūn-bûn
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2005 թուականի Յունիսին հրատարակուած գիտական յօդուած
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2005 թվականի հունիսին հրատարակված գիտական հոդված
@hy
2005年の論文
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2005年論文
@yue
2005年論文
@zh-hant
2005年論文
@zh-hk
2005年論文
@zh-mo
2005年論文
@zh-tw
2005年论文
@wuu
name
Structural basis for ordered s ...... in aspartate transcarbamoylase
@nl
Structural basis for ordered s ...... n aspartate transcarbamoylase.
@ast
Structural basis for ordered s ...... n aspartate transcarbamoylase.
@en
Structural basis for ordered s ...... n aspartate transcarbamoylase.
@en-gb
type
label
Structural basis for ordered s ...... in aspartate transcarbamoylase
@nl
Structural basis for ordered s ...... n aspartate transcarbamoylase.
@ast
Structural basis for ordered s ...... n aspartate transcarbamoylase.
@en
Structural basis for ordered s ...... n aspartate transcarbamoylase.
@en-gb
prefLabel
Structural basis for ordered s ...... in aspartate transcarbamoylase
@nl
Structural basis for ordered s ...... n aspartate transcarbamoylase.
@ast
Structural basis for ordered s ...... n aspartate transcarbamoylase.
@en
Structural basis for ordered s ...... n aspartate transcarbamoylase.
@en-gb
P2093
P2860
P356
P1476
Structural basis for ordered s ...... n aspartate transcarbamoylase.
@en
P2093
Evan R Kantrowitz
James P Cardia
Kimberly A Stieglitz
P2860
P304
P356
10.1073/PNAS.0503742102
P407
P577
2005-06-10T00:00:00Z