Beryllofluoride mimics phosphorylation of NtrC and other bacterial response regulators - Wikidata - wikimedia - TriplyDB

Beryllofluoride mimics phosphorylation of NtrC and other bacterial response regulators

Beryllofluoride mimics phosphorylation of NtrC and other bacterial response regulators

http://www.wikidata.org/entity/Q36774475

about

BeF(3)(-) acts as a phosphate analog in proteins phosphorylated on aspartate: structure of a BeF(3)(-) complex with phosphoserine phosphatase Crystal structure of activated CheY. Comparison with other activated receiver domains Crystal structure of a phosphatase with a unique substrate binding domain fromThermotoga maritima Solution structure and DNA binding of the effector domain from the global regulator PrrA (RegA) from Rhodobacter sphaeroides: insights into DNA binding specificity An atypical receiver domain controls the dynamic polar localization of the Myxococcus xanthus social motility protein FrzS Crystal Structure of a Complex between the Phosphorelay Protein YPD1 and the Response Regulator Domain of SLN1 Bound to a Phosphoryl Analog Interaction of CheY with the C-Terminal Peptide of CheZ Determinants for the Activation and Autoinhibition of the Diguanylate Cyclase Response Regulator WspR Crystal Structure of Activated CheY1 from Helicobacter pylori Structure and binding specificity of the receiver domain of sensor histidine kinase CKI1 from Arabidopsis thaliana Structural basis for sigma factor mimicry in the general stress response of Alphaproteobacteria Structural Basis of a Physical Blockage Mechanism for the Interaction of Response Regulator PmrA with Connector Protein PmrD fromKlebsiella pneumoniae An asymmetric heterodomain interface stabilizes a response regulator–DNA complex Basis of Mutual Domain Inhibition in a Bacterial Response Regulator The mRNA transcription/processing factor Ssu72 is a potential tyrosine phosphatase.The mechanism for RNA recognition by ANTAR regulators of gene expression Structure of FliM provides insight into assembly of the switch complex in the bacterial flagella motor Sinorhizobium meliloti CheA complexed with CheS exhibits enhanced binding to CheY1, resulting in accelerated CheY1 dephosphorylation A Variable Active Site Residue Influences the Kinetics of Response Regulator Phosphorylation and Dephosphorylation.Nitrogen assimilation in Escherichia coli: putting molecular data into a systems perspective Inhibitors of bacterial two-component signalling systems.How signals are heard during bacterial chemotaxis: protein-protein interactions in sensory signal propagation.Fluoride and organic weak acids as modulators of microbial physiology.The biochemistry and physiology of metallic fluoride: action, mechanism, and implications.Functional dissection of adenylate cyclase R, an inducer of spore encapsulation.Activation of the diguanylate cyclase PleD by phosphorylation-mediated dimerization.The structural basis for regulated assembly and function of the transcriptional activator NtrC.The crystal structure of beryllofluoride Spo0F in complex with the phosphotransferase Spo0B represents a phosphotransfer pretransition state Small-molecule inhibition of bacterial two-component systems to combat antibiotic resistance and virulence.Nitric Oxide Mediates Biofilm Formation and Symbiosis in Silicibacter sp. Strain TrichCH4B Conformational coupling in the chemotaxis response regulator CheY.Chemistry and biology NMR Study Reveals the Receiver Domain of Arabidopsis ETHYLENE RESPONSE1 Ethylene Receptor as an Atypical Type Response Regulator.A common dimerization interface in bacterial response regulators KdpE and TorR.Hybrid promiscuous (Hypr) GGDEF enzymes produce cyclic AMP-GMP (3', 3'-cGAMP)Activation of the global gene regulator PrrA (RegA) from Rhodobacter sphaeroides.Crystal structures of beryllium fluoride-free and beryllium fluoride-bound CheY in complex with the conserved C-terminal peptide of CheZ reveal dual binding modes specific to CheY conformation.Regulation of the Rhodobacter sphaeroides 2.4.1 hemA gene by PrrA and FnrL Mechanism of activation for transcription factor PhoB suggested by different modes of dimerization in the inactive and active states Structural analysis and solution studies of the activated regulatory domain of the response regulator ArcA: a symmetric dimer mediated by the alpha4-beta5-alpha5 face.

P2860

Q24630619-8D58F3B6-9634-4EE0-A00C-901B94CDAD05 Q27630942-86D0D2DE-0C78-4017-99BA-15DC14BC160C Q27641505-559FEFB6-A3D4-4CAB-9CCE-A6F06F7D1B42 Q27642600-AE20B9F8-94B4-4E54-87DE-806339370C09 Q27645973-D07F40EE-4680-46E2-A874-0FD242AC8D4D Q27649301-5722EE1C-3967-4354-925B-1985C64E544A Q27649334-1A58FBF7-E2CD-477A-93D9-236C25E6A2FC Q27657101-36A8CEB6-58C3-49B8-AFA6-FC808B7499F0 Q27660132-98BC8FE3-41D9-42B1-86BD-C4BF829D7D93 Q27667838-97627064-F0B4-40B2-B3A7-F0FE1CC92730 Q27678856-7CE3CCAA-498C-4271-A626-63DF21B72589 Q27679111-EED925C0-CDE7-4192-9FBB-C44CA5CEBD6A Q27681718-2B2788F8-C071-4027-B81D-EE4FE8CB89D9 Q27727690-953547FB-270C-444F-B824-7323B5FABD74 Q27939321-DBBBAEC0-089C-4A4E-BB3E-2E76DC625D9B Q28484158-88D34DF8-CAAC-4A10-B044-128A1CDB7829 Q28485426-967F2BF7-0F2C-4C8A-93FA-67F02C06A704 Q28500964-E102DCA4-2EDC-4912-8CC9-4743E24EB076 Q30392523-6E96CC2B-8B89-495D-80FE-E3A1E83B7AA1 Q30705590-97B62D11-CDC3-4C67-A543-865A2F7FD712 Q33181385-71E434D8-C592-4C4E-BD18-79DCE4A867AF Q34090837-50140818-FC50-4B9F-838F-4459EEF713BF Q34177145-1C7566C2-F304-4454-9C79-9C532C01C787 Q34199497-9C343D49-753D-4C95-AD64-14D5321F1758 Q34438909-237ACA06-9451-4B85-88EA-FC05308048EE Q34653754-EF95DFFF-C525-459F-B810-117B7E57A1D4 Q34666822-B2F9B4E9-3244-42EA-9EF3-0961C8C2D710 Q34697698-D2F607F1-7D93-468C-A31C-948AC83A8C9D Q34823364-292BAD65-5ADF-422F-B100-BD97329ED888 Q35620206-B256C154-1FB3-4953-AB1B-F3299DFE1115 Q35953097-CB2252C2-8B11-4879-9651-C4F4120C9445 Q36093381-9F1769B5-AD70-4594-BCC8-9A071AB2FD17 Q36093671-3ACB07D7-837A-4DF0-9087-059FAD107474 Q36476585-72722B6E-E836-4E12-8174-F0585370524D Q36607610-0595E5CE-8D27-405D-980D-5C8EE06D8F7A Q36839157-BCAA54F3-69CF-47A1-8B7C-4DAA35880A7F Q36883672-DE55107E-6006-4534-BBB0-53C03D4BC152 Q36933783-EE26685F-ACDD-4A49-8CB1-95B8E63D0FAD Q36937590-CFE25D89-64CD-4C47-9275-63D7B15C4407 Q36949989-3BB61526-EA6B-49F1-B33B-B42A5B0635B1

P2860

Beryllofluoride mimics phosphorylation of NtrC and other bacterial response regulators

http://www.wikidata.org/entity/Q36774475

description

1999 nî lūn-bûn

@nan

1999年の論文

@ja

1999年論文

@yue

1999年論文

@zh-hant

1999年論文

@zh-hk

1999年論文

@zh-mo

1999年論文

@zh-tw

1999年论文

@wuu

1999年论文

@zh

1999年论文

@zh-cn

name

Beryllofluoride mimics phosphorylation of NtrC and other bacterial response regulators

@ast

Beryllofluoride mimics phosphorylation of NtrC and other bacterial response regulators

@en

type

label

Beryllofluoride mimics phosphorylation of NtrC and other bacterial response regulators

@ast

Beryllofluoride mimics phosphorylation of NtrC and other bacterial response regulators

@en

prefLabel

Beryllofluoride mimics phosphorylation of NtrC and other bacterial response regulators

@ast

Beryllofluoride mimics phosphorylation of NtrC and other bacterial response regulators

@en

P1433

Q36774475-9AFBF510-B1FE-4516-9EA0-8462A17380FA

P1476

Q36774475-4CD3F474-AC8F-486E-9A25-F93A7624FFFF

P2093

Q36774475-15624D9A-270F-42F7-83C0-66B2D6A41A8E

Q36774475-4809D7FB-59AE-45D8-AB93-2999CC3CC680

Q36774475-4A870EA2-09BF-480A-B7BD-2D4820C0DBBC

Q36774475-5ED6BB7D-38F6-455E-AA0C-C28DF078E2BE

Q36774475-86AA77F2-B830-425B-92A1-8839D1603AEF

Q36774475-AC5A8C90-3AC4-4676-86B5-D90D86A4784A

Q36774475-C2450FB8-C0E9-4D94-AEBC-3B0AD858A136

Q36774475-CE8988DF-EFB1-4101-BBBA-3D0E7F36AD61

Q36774475-FFCD7483-32E0-4ACD-B325-051DC7A71AB8

P2860

Q36774475-02BDDBF1-63D8-4D94-B60D-3A33EB42E337

Q36774475-0EFF70C0-3123-4613-A6BB-06A81B6A51DF

Q36774475-1727E418-C5AB-4B08-B178-C9A10011D4D2

Q36774475-1B6E0E1F-B38B-41EB-8D44-6F3A0BDDDB40

Q36774475-1CBD6D0B-D915-4DEE-B695-B6141E858B22

Q36774475-1EEF47B2-12D4-47EB-9012-517284E14C26

Q36774475-1FEFFE90-9590-466A-ACCE-6FDD65107BD0

Q36774475-2127FD5A-0182-4A05-AB35-2C7B0FF4AF68

Q36774475-2DB79F6E-E6B2-47D5-91EA-289910C1E71B

Q36774475-2FADCF41-0E9A-4ECE-938E-1D99E1689D8F

P304

Q36774475-F8B7727E-394E-4EC4-B7CC-052B9949B94C

P31

Q36774475-33834800-85FF-4222-BE3D-823B1A62B254

P356

Q36774475-098674AD-917E-4D56-9499-95C83F7BDB94

P407

Q36774475-55D91494-309B-45CF-919A-D1970BF6DE76

P433

Q36774475-F585A124-FBC5-413F-987F-32914F7ABA93

P478

Q36774475-CD3D7935-41C7-4F02-A8FC-EAC733C2C286

P577

Q36774475-5A3E9851-A480-456F-A430-58A74FA67BC8

P5875

Q36774475-62C8CC02-D10C-4871-9CF4-7489F4A36F69

P698

Q36774475-3B5A84C0-8574-4A6B-9EC7-91331A576606

P921

Q36774475-50D4DDE3-539B-4774-A851-C5886DC49CC6

P932

Q36774475-9ABEC5ED-2098-4C56-97CD-432580998231

P356

PNAS.96.26.14789

P1433

Proceedings of the National Academy of Sciences of the United States of America

P1476

Beryllofluoride mimics phosphorylation of NtrC and other bacterial response regulators

@en

P2093

C A Hastings

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

D E Wemmer

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

D Yan

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

H S Cho

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

J G Pelton

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

M M Igo

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

S Kustu

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

S Y Lee

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

V Stewart

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

P2860

Three-dimensional structure of CheY, the response regulator of bacterial chemotaxis

Three-dimensional structure of chemotactic Che Y protein in aqueous solution by nuclear magnetic resonance methods

Three-dimensional solution structure of the N-terminal receiver domain of NTRC

Assignments, secondary structure, global fold, and dynamics of chemotaxis Y protein using three- and four-dimensional heteronuclear (13C,15N) NMR spectroscopy

Structure of the Escherichia coli response regulator NarL

High-resolution NMR structure and backbone dynamics of the Bacillus subtilis response regulator, Spo0F: implications for phosphorylation and molecular recognition

Structural basis for methylesterase CheB regulation by a phosphorylation-activated domain

NarL dimerization? Suggestive evidence from a new crystal form

Three-dimensional crystal structure of the transcription factor PhoB receiver domain

A two-component system that regulates an osmosensing MAP kinase cascade in yeast.

P304

14789-14794

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

P31

scholarly article

P356

10.1073/PNAS.96.26.14789

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

P407

P433

26

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

P478

96

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

P577

1999-12-01T00:00:00Z

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

P5875

235607561

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

P698

10611291

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

P921

phosphorylation

P932

24726

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