Metalloregulatory proteins: metal selectivity and allosteric switching. - Test2 - elhamkhani - TriplyDB

Metalloregulatory proteins: metal selectivity and allosteric switching.

Metalloregulatory proteins: metal selectivity and allosteric switching.

http://www.wikidata.org/entity/Q34990148

about

Biomolecular electrostatics and solvation: a computational perspective Protein design: toward functional metalloenzymes Metal preferences and metallation Solution Structure of Mycobacterium tuberculosis NmtR in the Apo State: Insights into Ni(II)-Mediated Allostery New insights into histidine triad proteins: solution structure of a Streptococcus pneumoniae PhtD domain and zinc transfer to AdcAII Metal sensing and signal transduction by CnrX from Cupriavidus metallidurans CH34: role of the only methionine assessed by a functional, spectroscopic, and theoretical study Structural analysis and insight into metal-ion activation of the iron-dependent regulator from Thermoplasma acidophilum Response of CnrX from Cupriavidus metallidurans CH34 to nickel binding The zinc-responsive regulon of Neisseria meningitidis comprises 17 genes under control of a Zur element.Characterization of the functional domains of the SloR metalloregulatory protein in Streptococcus mutans Zn(II) and Hg(II) binding to a designed peptide that accommodates different coordination geometries.Recent developments in copper and zinc homeostasis in bacterial pathogens Zinc-dependent regulation of zinc import and export genes by Zur Communication between binding sites is required for YqjI regulation of target promoters within the yqjH-yqjI intergenic region.Structural and mechanistic basis of zinc regulation across the E. coli Zur regulon.Advances in the molecular understanding of biological zinc transport.The CsoR-like sulfurtransferase repressor (CstR) is a persulfide sensor in Staphylococcus aureus Metal impurities cause false positives in high-throughput screening campaigns Sequential binding and sensing of Zn(II) by Bacillus subtilis Zur.Crystallization and preliminary X-ray diffraction analysis of the metalloregulatory protein DtxR from Thermoplasma acidophilum Metal site occupancy and allosteric switching in bacterial metal sensor proteins.The X-ray absorption spectroscopic model of the copper(II) imidazole complex ion in liquid aqueous solution: a strongly solvated square pyramid.Structural basis of the mercury(II)-mediated conformational switching of the dual-function transcriptional regulator MerR Resolution of Stepwise Cooperativities of Copper Binding by the Homotetrameric Copper-Sensitive Operon Repressor (CsoR): Impact on Structure and Stability.The S2 Cu(i) site in CupA from Streptococcus pneumoniae is required for cellular copper resistance.Mechanisms of copper homeostasis in bacteria.Structure and dynamics of the N-terminal domain of the Cu(I) binding protein CusB.Prediction of gene phenotypes based on GO and KEGG pathway enrichment scores.Manganese acquisition and homeostasis at the host-pathogen interface.Physical characterization of the manganese-sensing pneumococcal surface antigen repressor from Streptococcus pneumoniae The Chromobacterium violaceum ArsR Arsenite Repressor Exerts Tighter Control on Its Cognate Promoter Than the Escherichia coli System.Mechanisms of nickel toxicity in microorganisms.Heavy metals and metalloids as a cause for protein misfolding and aggregation.Effects of trace metal ions on secondary metabolism and the morphological development of streptomycetes.Bacterial Strategies to Maintain Zinc Metallostasis at the Host-Pathogen Interface.Zinc Homeostasis at the Bacteria/Host Interface-From Coordination Chemistry to Nutritional Immunity.Mycobacterium tuberculosis NmtR harbors a nickel sensing site with parallels to Escherichia coli RcnR.Density functional tight binding: values of semi-empirical methods in an ab initio era.Copper-zinc cross-modulation in prion protein binding.Generating a Metal-responsive Transcriptional Regulator to Test What Confers Metal Sensing in Cells

P2860

Q26853115-B29299CD-919C-4573-B2C8-0A3F5910F215 Q26866201-2CA6B4E1-3D75-4EAC-AC47-79B1B1D64065 Q27015688-A95D2F2B-40B8-406F-B03D-D19AD264BE03 Q27677867-C18235D5-FDCC-426B-B5C2-EB44443AD278 Q27680795-5450F66D-59A0-451D-B46F-DDCE0B67B0BD Q27687343-527073CA-DEDA-421D-878C-7D27AA7CAD4D Q27690190-23F26E38-AD36-4A9E-A228-3A120265AE05 Q27697674-A091D08D-03D6-4D00-A085-67051404BDC4 Q29346569-2BFF9795-BE96-4E09-A9BA-7BFDE222EF69 Q30009985-52444372-1B6A-4D9E-B925-81FC21CD9B51 Q30964852-91F7F27E-BEBA-4C08-9FE0-DE4E8FB9280D Q33560715-DAD9EF11-4297-40ED-BFA7-3ABDC45CD900 Q33804498-E7C96EAB-31D3-4453-AF15-9E75AE6D4B88 Q34056770-90D0EFEC-3289-4CFB-B99A-B491C51A4F08 Q34446236-82BB8C5E-73DC-4804-ACE1-6503708BEC5F Q34459994-DBA1CB83-B514-43C7-8C30-6128EEB4F661 Q34687415-009B114D-C42C-4AB8-8246-9D454D61BB93 Q35181932-EAFDCE44-B7A7-445B-8BDD-59DD4D93FDA0 Q35620880-6315A850-CDA0-450F-AD74-5DEFE6227C1F Q35742048-A979DA66-B029-4D6E-B86E-2BD766E01141 Q35851912-43650681-397C-4C21-9BB4-B16848ABE11E Q35895055-187F67B5-9FB4-40A8-AF34-C12C6D9052CA Q36002447-28E879B0-27BB-422D-8234-9A3A1D53BAA1 Q36358265-527F7AA1-1455-4418-9C84-3CBE8EA7EC64 Q36483926-7E0E96B2-232F-48F7-B965-73B893559DE9 Q37279465-4B9476E7-8987-4868-A7C8-D4ED73E03790 Q37280077-1B10415E-1805-4A01-AE94-F19A84E91C39 Q37338200-9D9F6435-F38C-457B-9014-32615C3CF3F0 Q37365396-D76D66AC-8C18-4272-8F64-FA984D7DAFC9 Q37385014-8DA03B34-A36E-42A0-B775-871113D2DA5F Q37424436-77FF1430-C370-4DE2-9A7F-679576226632 Q37907877-5CBEF1EF-2112-4234-8971-577AAC424B4E Q38223690-3044B701-3F89-4B91-8C71-496457534688 Q38816452-F7D5231B-199B-4B60-A89B-963323860FDD Q38909813-FE575D60-FC94-49A7-A525-86FD9BF6C939 Q38935738-5EEFFBA9-B211-4268-9841-97CA95C41319 Q39407946-66E7D3D9-D2B3-4E0C-9635-4D4FB0F7CD2D Q40354891-E1F34D26-0C53-44BC-87FB-58ECE51C1A20 Q40441989-D8EA7839-AAA4-4D6A-9667-CB4B45C8BA36 Q40799720-992CC00F-1116-484C-96FE-C4EA7F42EE9F

P2860

Metalloregulatory proteins: metal selectivity and allosteric switching.

http://www.wikidata.org/entity/Q34990148

description

2011 nî lūn-bûn

@nan

2011 թուականի Ապրիլին հրատարակուած գիտական յօդուած

@hyw

2011 թվականի ապրիլին հրատարակված գիտական հոդված

@hy

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

name

Metalloregulatory proteins: metal selectivity and allosteric switching.

@ast

Metalloregulatory proteins: metal selectivity and allosteric switching.

@en

Metalloregulatory proteins: metal selectivity and allosteric switching.

@nl

type

label

Metalloregulatory proteins: metal selectivity and allosteric switching.

@ast

Metalloregulatory proteins: metal selectivity and allosteric switching.

@en

Metalloregulatory proteins: metal selectivity and allosteric switching.

@nl

prefLabel

Metalloregulatory proteins: metal selectivity and allosteric switching.

@ast

Metalloregulatory proteins: metal selectivity and allosteric switching.

@en

Metalloregulatory proteins: metal selectivity and allosteric switching.

@nl

P1433

Q34990148-F59FAEDD-A4E7-4F0B-BE91-479C68F5B32B

P1476

Q34990148-3DF12AEA-DA7D-4C81-B655-4A3B28D097B2

P2093

Q34990148-3087674A-142A-4C01-AA10-C98AEF083EC5

Q34990148-6662B372-65FD-439B-8C68-ADD3FCBA6C32

Q34990148-EE1595BC-FB23-465F-A798-8D5F098AF4F7

P2860

Q34990148-0116A190-A3CE-44ED-93E9-574C447FC19F

Q34990148-02415E5F-8DC1-419D-A404-B3043DC256D2

Q34990148-029F1980-E264-40C0-8BA0-ABEED797CBA5

Q34990148-09B27137-821F-4752-9825-944B65985749

Q34990148-0A75F311-1708-4592-A9BF-B0761B536472

Q34990148-0AE1CEFE-053D-4741-9566-06357E71A4C9

Q34990148-0B3FF6E6-9DC7-4F06-9E85-C4F7B959A7B0

Q34990148-0BB2D0D0-5641-4673-B809-029488754636

Q34990148-0D12E6EC-04C3-44BE-841F-A00B4C068A00

Q34990148-0D35749B-FDE5-48BD-9EC0-45EE4218EF36

P304

Q34990148-B93CF3C5-9E9F-4B62-9083-EFA113DE1A32

P31

Q34990148-3188CD50-B599-4F2E-8D75-11DE5089F540

P356

Q34990148-71C3FE63-0D9F-451F-9A24-9D8CBD7A37EF

P433

Q34990148-F2AE8EEA-1E07-466D-8101-796CFE92058D

P478

Q34990148-3CD3F353-6B0C-4947-A1D0-FE0027EC844D

P577

Q34990148-46019ED9-C5CF-4BE0-8161-DDDE3952D3A8

P5875

Q34990148-FBF0F496-EF9C-4C4F-9710-8B7A11D98BB7

P698

Q34990148-BD3790D3-F430-4808-901F-3221AB159EA7

P932

Q34990148-51F718C1-F4F2-472A-BC3B-E1B34248E1AE

P356

J.BPC.2011.03.010

P1433

Biophysical Chemistry

P1476

Metalloregulatory proteins: metal selectivity and allosteric switching.

@en

P2093

David P Giedroc

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

Gregory C Campanello

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

Hermes Reyes-Caballero

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

P2860

Fur and the novel regulator YqjI control transcription of the ferric reductase gene yqjH in Escherichia coli

Metal stoichiometry and functional studies of the diphtheria toxin repressor

Architecture of a protein central to iron homeostasis: crystal structure and spectroscopic analysis of the ferric uptake regulator

Structure of the manganese-bound manganese transport regulator of Bacillus subtilis

Molecular basis of metal-ion selectivity and zeptomolar sensitivity by CueR

Crystal structure of the nickel-responsive transcription factor NikR

A metal-ligand-mediated intersubunit allosteric switch in related SmtB/ArsR zinc sensor proteins

Crystal structures, metal activation, and DNA-binding properties of two-domain IdeR from Mycobacterium tuberculosis

Crystal structure and function of the zinc uptake regulator FurB from Mycobacterium tuberculosis

Structural basis of the metal specificity for nickel regulatory protein NikR

P304

103-114

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

P31

scholarly article

P356

10.1016/J.BPC.2011.03.010

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

P433

2-3

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

P478

156

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

P577

2011-04-05T00:00:00Z

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

P5875

51068707

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

P698

21511390

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

P932

3097251

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