Allostery and cooperativity in Escherichia coli aspartate transcarbamoylase - Wikidata - awgldk - TriplyDB

Allostery and cooperativity in Escherichia coli aspartate transcarbamoylase

Allostery and cooperativity in Escherichia coli aspartate transcarbamoylase

http://www.wikidata.org/entity/Q36085714

about

From Genome to Structure and Back Again: A Family Portrait of the Transcarbamylases A Second Allosteric Site in Escherichia coli Aspartate Transcarbamoylase Allostery and Substrate Channeling in the Tryptophan Synthase Bienzyme Complex: Evidence for Two Subunit Conformations and Four Quaternary States Rigid Residue Scan Simulations Systematically Reveal Residue Entropic Roles in Protein Allostery X-ray Scattering Studies of Protein Structural Dynamics.Insight into the allosteric mechanism of Scapharca dimeric hemoglobin The CJIE1 prophage of Campylobacter jejuni affects protein expression in growth media with and without bile salts.Pyrimidine homeostasis is accomplished by directed overflow metabolism.ViewMotions Rainbow: a new method to illustrate molecular motions in proteins Solution NMR Spectroscopy for the Study of Enzyme Allostery.General base-general acid catalysis by terpenoid cyclases.Expression, purification, crystallization and preliminary X-ray diffraction analysis of the aspartate transcarbamoylase domain of human CAD.Understanding allosteric and cooperative interactions in enzymes.From feedback inhibition to allostery: the enduring example of aspartate transcarbamoylase.The role of strong electrostatic interactions at the dimer interface of human glutathione synthetase.50 years of allosteric interactions: the twists and turns of the models.Interfacial water effect on cooperativity and signal communication in Scapharca dimeric hemoglobin.

P2860

Q26798133-C28BF8EF-0807-42A1-8AD1-DCD280BA838E Q27679509-6014332F-7FF7-4ADB-A394-A052D252115D Q27679702-3D60438E-F254-4E55-8CD2-69386FD70802 Q28551601-B5090D0B-CBAD-463D-972E-8365405F6C4A Q30101114-EA31A751-1ED9-473D-8466-72E39BA07E8E Q30865627-EFE7658C-319A-4C3C-98A5-BB9751686E68 Q35123510-E2610E0F-86D0-4B47-B27F-1F690FD75A47 Q35751186-F98BB62D-9362-4D06-8932-AFAE1EB6A0E9 Q36895028-A6D7EFC1-A988-4C76-AF1D-19BC3476CFBC Q37076848-9FC6D09C-9306-42FD-A1FB-EE48FD272080 Q37131551-D1C6D70D-5AC5-4DCA-95B3-45AFDC7BECB1 Q37374716-3B6B07EE-5460-4402-AFCC-F9D1ACCBAFC3 Q38126216-54EAFA46-796A-439E-AE02-53EE27433637 Q38129478-A1068CAD-C2CD-4614-9529-C7C6AA9E093E Q42921549-097D1478-7BC1-4BCE-8FF9-7E40226F1AA9 Q46140335-47B03D97-AAC7-4934-90BB-1959BB342457 Q48187925-0633143B-5C9F-4284-A685-69CE14802C79

P2860

Allostery and cooperativity in Escherichia coli aspartate transcarbamoylase

http://www.wikidata.org/entity/Q36085714

description

2011 nî lūn-bûn

@nan

2011年の論文

@ja

2011年論文

@yue

2011年論文

@zh-hant

2011年論文

@zh-hk

2011年論文

@zh-mo

2011年論文

@zh-tw

2011年论文

@wuu

2011年论文

@zh

2011年论文

@zh-cn

name

Allostery and cooperativity in Escherichia coli aspartate transcarbamoylase

@ast

Allostery and cooperativity in Escherichia coli aspartate transcarbamoylase

@en

type

label

Allostery and cooperativity in Escherichia coli aspartate transcarbamoylase

@ast

Allostery and cooperativity in Escherichia coli aspartate transcarbamoylase

@en

prefLabel

Allostery and cooperativity in Escherichia coli aspartate transcarbamoylase

@ast

Allostery and cooperativity in Escherichia coli aspartate transcarbamoylase

@en

P1433

Q36085714-1B634B6D-8C41-497E-B4BD-B4DE92512E35

P1476

Q36085714-B20978C4-06A1-41A0-8B86-5588D6566A4D

P2093

Q36085714-85389EAF-E4E2-452A-8873-BBA039B07141

P2860

Q36085714-02DBA4FF-4F1D-41AB-90E3-B7D06E80A525

Q36085714-075FC120-67F1-4FB6-B5E4-B71C2CD9A713

Q36085714-0931D1EB-6423-4AF3-A23F-702673A8C354

Q36085714-131DC72B-711C-4E11-8BE1-74495279479C

Q36085714-15589CE5-BC89-4B4C-8B7D-BDBD18B1F346

Q36085714-17D5FA47-96CC-4A8C-95D3-5F6EE396B715

Q36085714-1A65728E-DE6C-47E1-BF28-4D9707DF2399

Q36085714-1A70F80B-CA8F-4401-ACB8-886E112CE07B

Q36085714-1AA22B25-9958-4FFD-A24A-9391D2A6BB04

Q36085714-1DC4F3D9-FFD9-4D7A-8D98-8D6038549D3D

P304

Q36085714-8C974F3E-0A57-4651-B2A0-EA483E1EA537

P31

Q36085714-E470F795-1ACC-4130-B460-447D2AC54960

P356

Q36085714-B5CD0569-5294-43AC-9C2B-29F55F4721F3

P407

Q36085714-2A13E1E9-DA29-42EC-BE53-9B22115412E8

P433

Q36085714-A3E54F83-70C1-42B5-8513-B25EEDA76027

P478

Q36085714-949A56F4-9827-4571-9BBF-53949CE72033

P577

Q36085714-A4BA9B59-6B25-4407-B3BF-AF4202C82D76

P5875

Q36085714-306FEC37-1BEC-4FE4-9316-B52B3A7878DC

P698

Q36085714-0D6095B4-130E-4FA2-9232-A9D90EDFF943

P932

Q36085714-22FA7EE7-EFCF-4907-876D-97DDBD75A3D3

P356

J.ABB.2011.10.024

P1433

Archives of Biochemistry and Biophysics

P1476

Allostery and cooperativity in Escherichia coli aspartate transcarbamoylase

@en

P2093

Evan R Kantrowitz

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

P2860

Structural basis for ordered substrate binding and cooperativity in aspartate transcarbamoylase.

Assessment of the allosteric mechanism of aspartate transcarbamoylase based on the crystalline structure of the unregulated catalytic subunit

Insights into the mechanisms of catalysis and heterotropic regulation of Escherichia coli aspartate transcarbamoylase based upon a structure of the enzyme complexed with the bisubstrate analogue N-phosphonacetyl-L-aspartate at 2.1 A

Binding of bisubstrate analog promotes large structural changes in the unregulated catalytic trimer of aspartate transcarbamoylase: Implications for allosteric regulation

Direct structural evidence for a concerted allosteric transition in Escherichia coli aspartate transcarbamoylase

The Pathway of Product Release from the R State of Aspartate Transcarbamoylase

A Cooperative Escherichia coli Aspartate Transcarbamoylase without Regulatory Subunits,

Structural consequences of effector binding to the T state of aspartate carbamoyltransferase: crystal structures of the unligated and ATP- and CTP-complexed enzymes at 2.6-A resolution

Crystal structures of aspartate carbamoyltransferase ligated with phosphonoacetamide, malonate, and CTP or ATP at 2.8-A resolution and neutral pH

Crystal structures of phosphonoacetamide ligated T and phosphonoacetamide and malonate ligated R states of aspartate carbamoyltransferase at 2.8-A resolution and neutral pH

P304

81-90

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

P31

scholarly article

P356

10.1016/J.ABB.2011.10.024

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

P407

P433

2

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

P478

519

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

P577

2011-12-16T00:00:00Z

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

P5875

51924006

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

P698

22198283

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

P932

3393099

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