Inward-facing conformation of the zinc transporter YiiP revealed by cryoelectron microscopy - Wikidata - awgldk - TriplyDB

Inward-facing conformation of the zinc transporter YiiP revealed by cryoelectron microscopy

Inward-facing conformation of the zinc transporter YiiP revealed by cryoelectron microscopy

http://www.wikidata.org/entity/Q27675959

about

Cation Diffusion Facilitators Transport Initiation and Regulation Is Mediated by Cation Induced Conformational Changes of the Cytoplasmic Domain Bacterial Magnetosome Biomineralization - A Novel Platform to Study Molecular Mechanisms of Human CDF-Related Type-II Diabetes Deducing the symmetry of helical assemblies: Applications to membrane proteins.Recent developments in copper and zinc homeostasis in bacterial pathogens Visualizing the kinetic power stroke that drives proton-coupled zinc(II) transport Nicotinic acetylcholine receptor and the structural basis of neuromuscular transmission: insights from Torpedo postsynaptic membranes Advances in the molecular understanding of biological zinc transport.Heterodimerization, altered subcellular localization, and function of multiple zinc transporters in viable cells using bimolecular fluorescence complementation Computation and Functional Studies Provide a Model for the Structure of the Zinc Transporter hZIP4.A Ferrous Iron Exporter Mediates Iron Resistance in Shewanella oneidensis MR-1.Functional Determinants of Metal Ion Transport and Selectivity in Paralogous Cation Diffusion Facilitator Transporters CzcD and MntE in Streptococcus pneumoniae Molecular Basis of Transient Neonatal Zinc Deficiency: NOVEL ZnT2 MUTATIONS DISRUPTING ZINC BINDING AND PERMEATION.Disease-Homologous Mutation in the Cation Diffusion Facilitator Protein MamM Causes Single-Domain Structural Loss and Signifies Its Importance.Role of transition metal exporters in virulence: the example of Neisseria meningitidis In situ dimerization of multiple wild type and mutant zinc transporters in live cells using bimolecular fluorescence complementation.Current understanding of ZIP and ZnT zinc transporters in human health and diseases.Relationship between the architecture of zinc coordination and zinc binding affinity in proteins--insights into zinc regulation.Cation Diffusion Facilitator family: Structure and function.The Physiological, Biochemical, and Molecular Roles of Zinc Transporters in Zinc Homeostasis and Metabolism.The PP-motif in luminal loop 2 of ZnT transporters plays a pivotal role in TNAP activation Direct Comparison of Manganese Detoxification/Efflux Proteins and Molecular Characterization of ZnT10 Protein as a Manganese Transporter.Bacterial Strategies to Maintain Zinc Metallostasis at the Host-Pathogen Interface.Zinc Homeostasis at the Bacteria/Host Interface-From Coordination Chemistry to Nutritional Immunity.Zinc transport and the inhibition of the L-type calcium channel are two separable functions of ZnT-1.The role of the zinc transporter SLC30A2/ZnT2 in transient neonatal zinc deficiency.Proton-Detected Solid-State NMR Spectroscopy of a Zinc Diffusion Facilitator Protein in Native Nanodiscs.Structural Elements in the Transmembrane and Cytoplasmic Domains of the Metal Transporter SLC30A10 Are Required for Its Manganese Efflux Activity.Biocide Selective TolC-Independent Efflux Pumps in Enterobacteriaceae.Understanding the Contribution of Zinc Transporters in the Function of the Early Secretory Pathway.Zinc Signal in Brain Diseases.The C-terminal cytosolic domain of the human zinc transporter ZnT8 and its diabetes risk variant.Structural basis for the alternating access mechanism of the cation diffusion facilitator YiiP.Protonendetektierte Festkörper-NMR-Spektroskopie an einem Zinktransporter-Membranprotein in nativen Nanoscheiben Function, Structure, and Transport Aspects of ZIP and ZnT Zinc Transporters in Immune Cells Evaluation of the roles of the cytosolic N-terminus and His-rich loop of ZNT proteins using ZNT2 and ZNT3 chimeric mutants

P2860

Q27682386-88DFD078-E91E-4B2A-989B-829C2313114F Q27683741-83F39C8C-4C93-48C5-BF10-911C993923F8 Q30152776-8505873C-E4D6-4344-96E9-771A8E35BB7C Q33560715-2447988D-9818-4B8F-9D0E-2D9DE7F7B943 Q34087059-E858212C-945B-438E-BE24-A4854415D451 Q34372276-FE24F61A-7FFC-4A49-9F4B-216BC5B8A917 Q34459994-3DF0DD7A-B4EA-49ED-A8B5-1ADB55A9C196 Q35580837-CF91D0AD-F50D-4FFA-B88A-2C0761398E26 Q35859485-D0C7DFC0-DECA-4C8D-9A11-CC65E370313A Q36196167-26084473-A7E9-4037-8581-D3B94786A63F Q36709434-08ADFBDE-E149-4CE8-9311-1FFAFB9C9958 Q37034380-47F23089-CE4C-4633-B100-F465D3E7528F Q37195617-C1929622-8082-412D-91B3-66B1B49068AD Q37408492-F0A2F8F6-EF63-4C95-B977-115AA6C4A466 Q37635752-CA70660F-1D48-4C79-A221-C91F6746C3BE Q38202894-27E9C92F-A29A-44E7-ABE5-934B0BFEFA06 Q38254214-A51C20D3-9BF3-4753-95FA-45B7BF88EBC4 Q38431694-9FA81598-BB30-4302-A769-4EAF7EB73470 Q38530500-98971B67-F6A6-43EB-80A8-B5B2B39BB43F Q38764363-A74A8637-C935-436C-8C6A-9F03E60EBC84 Q38768341-29897EA9-0F0B-43BB-A9A6-A895C310FE33 Q38909813-CC071539-97ED-4119-8E4F-C20A16C482F8 Q38935738-20B72320-B1C7-449C-AD49-8A8106FC2696 Q39018860-520D597E-78B8-4876-92F5-B641393BED76 Q39406979-D24BC58D-CC23-4011-8F88-BAAFBF081BFE Q42147541-1E44EDB7-6D42-4037-9DCA-FA4DCFCA7273 Q42395510-0945D782-EB03-4CF3-AA5E-64F9AD18F569 Q46276454-446F9594-1355-479C-9D1D-00ED66C2C139 Q47163079-14E175CF-92AE-4BB7-9B51-577B8D82D327 Q47371072-08D743AD-E186-4D47-96CF-2014DCFA76E9 Q50071047-737725BF-E048-424A-9D22-F31D29925A2B Q52673222-F745A0F8-8668-45B8-B88C-8C6581D055E8 Q57896466-EF775DC4-E60A-420C-BD74-13BF881A4897 Q58123991-7A6CE8FE-C212-42B7-8177-62E2C98A20AA Q58712633-2A328CA0-F40C-4563-AD04-CB6EFC6BD7FC

P2860

Inward-facing conformation of the zinc transporter YiiP revealed by cryoelectron microscopy

http://www.wikidata.org/entity/Q27675959

description

2013 nî lūn-bûn

@nan

2013 թուականի Փետրուարին հրատարակուած գիտական յօդուած

@hyw

2013 թվականի փետրվարին հրատարակված գիտական հոդված

@hy

2013年の論文

@ja

2013年論文

@yue

2013年論文

@zh-hant

2013年論文

@zh-hk

2013年論文

@zh-mo

2013年論文

@zh-tw

2013年论文

@wuu

name

Inward-facing conformation of ...... led by cryoelectron microscopy

@ast

Inward-facing conformation of ...... led by cryoelectron microscopy

@en

Inward-facing conformation of ...... led by cryoelectron microscopy

@nl

type

label

Inward-facing conformation of ...... led by cryoelectron microscopy

@ast

Inward-facing conformation of ...... led by cryoelectron microscopy

@en

Inward-facing conformation of ...... led by cryoelectron microscopy

@nl

prefLabel

Inward-facing conformation of ...... led by cryoelectron microscopy

@ast

Inward-facing conformation of ...... led by cryoelectron microscopy

@en

Inward-facing conformation of ...... led by cryoelectron microscopy

@nl

P1433

Q27675959-28C479FF-5496-49BE-A143-8D0823E07B4B

P1476

Q27675959-62497E11-CDC4-4D74-8057-196D292FE51C

P2093

Q27675959-293792A5-E0E3-4E07-8C1E-ED2BB8E1DEC4

Q27675959-39FFBDEC-FB28-405A-B925-E7D1E546EB09

Q27675959-60CAB302-FC67-464B-A7CA-F34248D34FF5

Q27675959-7AA8CF97-E049-4C1F-8A91-92A2CFDEFFBD

Q27675959-9EA645B1-B2CC-4C7C-BA8B-98463C67BBBD

Q27675959-A7AA27C0-D4D0-43A2-88DF-3A0302C87A6F

Q27675959-B1794FD3-35FE-4B29-89B4-63AD9C753CDC

Q27675959-BB6C91D2-3603-46CE-8BFC-8D0A177DC72F

Q27675959-CA9716AD-D8DF-4EC0-AB55-9726EF5B6B6A

Q27675959-DDF7D915-6DDA-43EA-80E0-2FC87F48FDCB

P2860

Q27675959-15D50198-0C37-413A-83AC-C1B6BE0ABBA8

Q27675959-19475A9A-8120-47CB-B7A3-6F7737A1DD99

Q27675959-1C5BDDBB-15CE-423B-B8C0-321C8166BC94

Q27675959-2F181DD8-CE8D-4B1E-81E6-95EEF87F3C24

Q27675959-3785D864-6210-4AE6-BCC8-776889FCCA16

Q27675959-37A81DA9-9875-4010-ACB0-C9215EE9A749

Q27675959-3989B37E-D31D-446C-92DB-C5DC5046A365

Q27675959-4AD7F0B3-30C0-4A44-95FD-EDF17746ABF6

Q27675959-52EE7F37-AF99-4603-8F56-16FBB0859711

Q27675959-55C9EB76-E6A2-4C83-BF23-F35B41404FBB

P304

Q27675959-B3A913A0-30E6-4264-A0BC-99D3DEC6CF4A

P31

Q27675959-E7F7AB43-8313-429E-8E5D-B5B03118E059

P3181

Q27675959-6A0EC7F3-0D8D-434F-99CF-AAC9ED0065B8

P356

Q27675959-BB396C8C-1858-4F71-8BB1-681F9F8676CA

P407

Q27675959-9CFD2B07-06F4-421C-9274-97094109B1CA

P433

Q27675959-44DD42C8-830B-411E-B309-1D86012768D3

P478

Q27675959-C0FC9DD6-86B1-4948-A242-D85A0C2F1E5E

P50

Q27675959-60AF265A-3E5F-42F2-B1D8-F3185595C21D

Q27675959-8F1C2D45-719E-4B88-85B8-6D9074A07832

P577

Q27675959-7AABAF40-6C7F-402E-B011-96240369070A

P5875

Q27675959-C3C40722-BA4E-47B4-8BCF-0FBF399CCF0C

P698

Q27675959-FADA33D7-3E35-4768-95AA-2B260E73A254

P932

Q27675959-8EED2F53-CA94-4529-84AD-3ED342F508CD

P3181

P356

PNAS.1215455110

P1433

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

P1476

Inward-facing conformation of ...... led by cryoelectron microscopy

@en

P2093

Changki Kim

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

David L Stokes

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

Davide Provasi

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

Iban Ubarretxena-Belandia

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

Jia Fang

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

Juoehi Tao

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

Martin Vink

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

Ming Zhou

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

Minghui Hu

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

Pawel A Penczek

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

P2860

Cloning and functional characterization of a mammalian zinc transporter that confers resistance to zinc

Membrane protein structure determination by electron crystallography

Structure of the zinc transporter YiiP

Insights into the Mode of Action of a Putative Zinc Transporter CzrB in Thermus thermophilus

Protein-folding location can regulate manganese-binding versus copper- or zinc-binding

Crystal structure of the cytosolic domain of the cation diffusion facilitator family protein

Structural basis for autoregulation of the zinc transporter YiiP

The yeast ZRT1 gene encodes the zinc transporter protein of a high-affinity uptake system induced by zinc limitation.

Femtomolar sensitivity of metalloregulatory proteins controlling zinc homeostasis

Flexible fitting of atomic structures into electron microscopy maps using molecular dynamics.

P304

2140-2145

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

P31

scholarly article

P3181

3943239

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

P356

10.1073/PNAS.1215455110

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

P407

P433

6

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

P478

110

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

P50

Nicolas Coudray

P577

2013-01-22T00:00:00Z

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

P5875

235363959

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

P698

23341604

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

P932

3568326

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