Crosslinking of membrane-embedded cysteines reveals contact points in the EmrE oligomer. - Wikidata - awgldk - TriplyDB

Crosslinking of membrane-embedded cysteines reveals contact points in the EmrE oligomer.

Crosslinking of membrane-embedded cysteines reveals contact points in the EmrE oligomer.

http://www.wikidata.org/entity/Q34155142

about

Positioning of proteins in membranes: a computational approach Analyzing conformational changes in the transport cycle of EmrE X-ray structure of EmrE supports dual topology model.Organic and inorganic mercurials have distinct effects on cellular thiols, metal homeostasis, and Fe-binding proteins in Escherichia coli Xenobiotic efflux in bacteria and fungi: a genomics update A photochemical approach to the lipid accessibility of engineered cysteinyl residues.Evidence for assembly of small multidrug resistance proteins by a "two-faced" transmembrane helix.Outer membrane protein OmpW participates with small multidrug resistance protein member EmrE in quaternary cationic compound efflux Topologically random insertion of EmrE supports a pathway for evolution of inverted repeats in ion-coupled transporters Structural basis of G protein-coupled receptor-Gi protein interaction: formation of the cannabinoid CB2 receptor-Gi protein complex Three-dimensional structure of the bacterial multidrug transporter EmrE shows it is an asymmetric homodimer.Structure, dynamics, and substrate-induced conformational changes of the multidrug transporter EmrE in liposomes.Crosstalk in G protein-coupled receptors: changes at the transmembrane homodimer interface determine activation.Making structural sense of dimerization interfaces of delta opioid receptor homodimers.A structural model of EmrE, a multi-drug transporter from Escherichia coli.Structure of the multidrug resistance efflux transporter EmrE from Escherichia coli Linking of Glycine Receptor Transmembrane Segments Three and Four Allows Assignment of Intrasubunit-Facing Residues.Experimental phasing for structure determination using membrane-protein crystals grown by the lipid cubic phase method.Structure and function of efflux pumps that confer resistance to drugs Undecided membrane proteins insert in random topologies. Up, down and sideways: it does not really matter In vitro synthesis of fully functional EmrE, a multidrug transporter, and study of its oligomeric state Conformational changes involved in G-protein-coupled-receptor activation Parallel topology of genetically fused EmrE homodimers.Cross-linking of sites involved with alcohol action between transmembrane segments 1 and 3 of the glycine receptor following activation Inter- and Intra-Subunit Butanol/Isoflurane Sites of Action in the Human Glycine Receptor.Deducing the transmembrane domain organization of presenilin-1 in gamma-secretase by cysteine disulfide cross-linking.An emerging consensus for the structure of EmrE.NMR and EPR studies of membrane transporters.Modulation of substrate efflux in bacterial small multidrug resistance proteins by mutations at the dimer interface.Identification of a glycine motif required for packing in EmrE, a multidrug transporter from Escherichia coli.The human dopamine transporter forms a tetramer in the plasma membrane: cross-linking of a cysteine in the fourth transmembrane segment is sensitive to cocaine analogs.New insights into the structure and oligomeric state of the bacterial multidrug transporter EmrE: an unusual asymmetric homo-dimer.The assembly motif of a bacterial small multidrug resistance protein.Drug efflux by a small multidrug resistance protein is inhibited by a transmembrane peptide.Membrane topology of ABC-type macrolide antibiotic exporter MacB in Escherichia coli.Direct evidence for substrate-induced proton release in detergent-solubilized EmrE, a multidrug transporter.Complete topology inversion can be part of normal membrane protein biogenesis.The key residue for substrate transport (Glu14) in the EmrE dimer is asymmetric.The membrane topology of EmrE - a small multidrug transporter from Escherichia coli.Full-length cellular β-secretase has a trimeric subunit stoichiometry, and its sulfur-rich transmembrane interaction site modulates cytosolic copper compartmentalization.

P2860

Q24647761-5E90378A-FF5A-4AF2-A435-2857AEDA533C Q26829989-78FEAF2C-17C4-4EFE-B018-F53AB5E7A4C0 Q27649102-77B19FCA-A26E-447F-A9F6-DEDA3409C308 Q28601001-C3BBA390-7BC0-41BA-87BF-9B82A3E112B7 Q28834633-6A9AFB07-79CD-46EA-8627-4C6F87155C53 Q30451175-C280B1E8-9C2C-4CD8-9A6B-3F45D7F20515 Q33238086-81853850-4535-4EA1-A9D8-02CEB6C22905 Q33570226-175B6EB8-4598-4D39-A0B4-58BD99E09049 Q33832720-44F2666F-BFE0-415D-8328-BF9ED0A2C152 Q33931230-EEF1FD21-9C19-4937-B22B-1C5AB47592F3 Q34053453-86B94A35-6D5B-4BD1-B4F8-C658F77A0D43 Q34074515-10854C08-D9BA-451E-A9A3-59C38804E13D Q34142522-7EC75B38-6E4B-47C3-9E8D-83595E398FB4 Q34160481-319EBACF-7829-4C91-BA1B-923D7C6CDA2D Q34185881-81459C89-7328-4BBF-970F-56B5F973C5D0 Q34299369-466127DE-C740-41A9-BA44-88D9685C6C30 Q34572493-D2EB3BBD-DD65-4B92-8F83-5BDDC25C845E Q35006822-9537DAC6-9195-4A96-AB57-9945102C53E5 Q35294152-D0829869-32D0-496B-9571-7BE56C8785A1 Q36024435-5B0A4254-154B-4F2F-82FD-02D56EEC779A Q36159680-AB92001E-3FE6-4828-A212-30BDD92105D7 Q36329546-A0DF7DD9-8A42-412C-8C33-5CB3B508C18E Q36391998-8F70FDCA-AEB2-49FD-B975-58F5D0C7292C Q36663068-670D24B5-FA88-436A-AC38-CCBB72CBB1D7 Q36999846-710F7EB7-F3A4-4D34-A98A-7675009A3F7A Q37003150-83FED39C-DA6D-4BBA-8E63-7631AF709554 Q37074615-0B1AFD5B-7855-4FD4-92A1-0EA55BC87519 Q37488240-F76258A9-99F9-4E2C-9524-17BAC0BEA961 Q38724801-D6D3134F-6C23-42F3-8E90-E328FD875854 Q39259841-A9DE78A3-BEFA-42FA-8164-40B7E14DECBC Q40629961-4ED19BC8-9948-4D96-A39A-6BB2B5DA0169 Q41628403-E777B95F-55E4-4794-A0B2-C31A05CC9B40 Q41862362-12FF756E-4B94-4AC1-9649-DDF6241DA7AE Q41994971-63F83206-8687-48A4-A0EB-EDDF6C8D83BE Q44495023-C7D6420F-B68D-4493-933C-79B352F05A9A Q44710560-99804EF4-7301-4981-A201-F4DEFD11BEC2 Q46474386-A05FB6DB-AC35-42B4-8682-949754ED6893 Q46879457-93692DDB-C4C4-4595-992A-4DA3F08D0AA0 Q47883865-78E3F18E-E0F1-431D-937E-0D7A8E7D0BE1 Q48059222-C4F96730-BE52-48BA-8BD8-049A68584F41

P2860

Crosslinking of membrane-embedded cysteines reveals contact points in the EmrE oligomer.

http://www.wikidata.org/entity/Q34155142

description

2002 nî lūn-bûn

@nan

2002 թուականի Սեպտեմբերին հրատարակուած գիտական յօդուած

@hyw

2002 թվականի սեպտեմբերին հրատարակված գիտական հոդված

@hy

2002年の論文

@ja

2002年論文

@yue

2002年論文

@zh-hant

2002年論文

@zh-hk

2002年論文

@zh-mo

2002年論文

@zh-tw

2002年论文

@wuu

name

Crosslinking of membrane-embedded cysteines reveals contact points in the EmrE oligomer.

@ast

Crosslinking of membrane-embedded cysteines reveals contact points in the EmrE oligomer.

@en

Crosslinking of membrane-embedded cysteines reveals contact points in the EmrE oligomer.

@nl

type

label

Crosslinking of membrane-embedded cysteines reveals contact points in the EmrE oligomer.

@ast

Crosslinking of membrane-embedded cysteines reveals contact points in the EmrE oligomer.

@en

Crosslinking of membrane-embedded cysteines reveals contact points in the EmrE oligomer.

@nl

prefLabel

Crosslinking of membrane-embedded cysteines reveals contact points in the EmrE oligomer.

@ast

Crosslinking of membrane-embedded cysteines reveals contact points in the EmrE oligomer.

@en

Crosslinking of membrane-embedded cysteines reveals contact points in the EmrE oligomer.

@nl

P1433

Q34155142-738B5C62-0ED5-4B5C-896A-47680839FC71

P1476

Q34155142-7615A8D5-59D7-44EF-955C-A6DA19ABDFA6

P2093

Q34155142-132B1499-A405-477C-B695-733E349986CF

Q34155142-23B6CE14-D1C8-4B46-9D11-E535C36FE69A

Q34155142-E3EFF9F7-2A55-4BF8-BE62-52A977A9F7C7

P2860

Q34155142-143E05B3-E09A-4B9B-B567-67EDC0B3E91B

Q34155142-1D78DF0E-B9BC-4C96-87B4-FD7C3188E2AE

Q34155142-20C981B3-16C9-4AB1-BEEC-27388CECDFE9

Q34155142-3420B438-1299-48F2-9CD0-95035C537D40

Q34155142-38087B18-ED7D-40F4-BFD9-6A6885FA1BC1

Q34155142-4F138149-0AB3-453D-A184-E6EE816E9AB6

Q34155142-50C662A7-F682-4C93-A50F-1925C1FB893C

Q34155142-559B2554-900A-43EB-83D8-26D3E805C58D

Q34155142-589EB104-A4B1-499A-AEDA-D9D964CCC119

Q34155142-5B6ED8F9-0CA9-48B4-82A5-72FD93800287

P304

Q34155142-F2F90350-6302-4520-9216-1208038D00C0

P31

Q34155142-42E7440F-2182-43B3-AAC5-B8583990DCF8

P356

Q34155142-27288D99-CB81-4342-90CA-9CFF186FC7C7

P407

Q34155142-210EDC66-8EB5-4D8D-BFE3-274A8A33843C

P433

Q34155142-EDFAD604-99AC-426D-BCB9-DEA560A1BCC5

P478

Q34155142-F7DF1A86-638A-488E-B958-34178B124980

P577

Q34155142-D3925053-B552-4F6D-A971-B89CE95A3CC5

P5875

Q34155142-5D10AC63-2E00-47DE-BB59-961F33B29C73

P698

Q34155142-F6A7DD3F-7846-40DB-9C54-70878AAA8FAB

P932

Q34155142-FD6E1F4F-D3E7-4620-A4EB-EFD2AF07B28D

P356

P1433

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

P1476

Crosslinking of membrane-embedded cysteines reveals contact points in the EmrE oligomer.

@en

P2093

Misha Soskine

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

Shimon Schuldiner

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

Sonia Steiner-Mordoch

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

P2860

Improved M13 phage cloning vectors and host strains: nucleotide sequences of the M13mp18 and pUC19 vectors

Site-directed mutagenesis by overlap extension using the polymerase chain reaction

Tricine-sodium dodecyl sulfate-polyacrylamide gel electrophoresis for the separation of proteins in the range from 1 to 100 kDa

Functional analysis of novel multidrug transporters from human pathogens

A bacteriophage T7 RNA polymerase/promoter system for controlled exclusive expression of specific genes

Precious things come in little packages.

A common binding site for substrates and protons in EmrE, an ion-coupled multidrug transporter.

Small is mighty: EmrE, a multidrug transporter as an experimental paradigm.

The projection structure of EmrE, a proton-linked multidrug transporter from Escherichia coli, at 7 A resolution

Characterization of a Na+/H+ antiporter gene of Escherichia coli.

P304

12043-12048

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

P31

scholarly article

P356

10.1073/PNAS.192392899

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

P407

P433

19

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

P478

99

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

P577

2002-09-09T00:00:00Z

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

P5875

11168766

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

P698

12221291

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

P932

129395

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