Glutamate receptor desensitization is mediated by changes in quaternary structure of the ligand binding domain. - Test2 - elhamkhani - TriplyDB

Glutamate receptor desensitization is mediated by changes in quaternary structure of the ligand binding domain.

Glutamate receptor desensitization is mediated by changes in quaternary structure of the ligand binding domain.

http://www.wikidata.org/entity/Q30538804

about

Structure, Dynamics, and Allosteric Potential of Ionotropic Glutamate Receptor N-Terminal Domains Structural Insights into Competitive Antagonism in NMDA Receptors Structural basis of kainate subtype glutamate receptor desensitization.The auxiliary subunits Neto1 and Neto2 have distinct, subunit-dependent effects at recombinant GluK1- and GluK2-containing kainate receptors Single-particle electron microscopy in the study of membrane protein structure Structural mechanism of glutamate receptor activation and desensitization.Structure and organization of heteromeric AMPA-type glutamate receptors Mechanism of NMDA Receptor Inhibition and Activation.Glycine activated ion channel subunits encoded by ctenophore glutamate receptor genes.Contributions of different kainate receptor subunits to the properties of recombinant homomeric and heteromeric receptors.Self-assembled monolayers improve protein distribution on holey carbon cryo-EM supports.Structure and dynamics of AMPA receptor GluA2 in resting, pre-open, and desensitized states Emerging structural insights into the function of ionotropic glutamate receptors.Cooperative Dynamics of Intact AMPA and NMDA Glutamate Receptors: Similarities and Subfamily-Specific Differences.Pharmacology and Structural Analysis of Ligand Binding to the Orthosteric Site of Glutamate-Like GluD2 Receptors The Transmembrane Domain Mediates Tetramerization of α-Amino-3-hydroxy-5-methyl-4-isoxazolepropionic Acid (AMPA) Receptors Protein Crowding within the Postsynaptic Density Can Impede the Escape of Membrane Proteins.The multifaceted subunit interfaces of ionotropic glutamate receptors.Structure and gating of tetrameric glutamate receptors.Retour aux sources: defining the structural basis of glutamate receptor activation.The structure and function of glutamate receptors: Mg2+ block to X-ray diffraction.Structure and symmetry inform gating principles of ionotropic glutamate receptors.Mapping the interaction sites between AMPA receptors and TARPs reveals a role for the receptor N-terminal domain in channel gating.The N-terminal domain modulates α-amino-3-hydroxy-5-methyl-4-isoxazolepropionic acid (AMPA) receptor desensitization.Heteromerization of ligand binding domains of N-methyl-D-aspartate receptor requires both coagonists, L-glutamate and glycine.Defining the structural relationship between kainate-receptor deactivation and desensitization Modulation of homomeric and heteromeric kainate receptors by the auxiliary subunit Neto1.Preferential assembly of heteromeric kainate and AMPA receptor amino terminal domains.The Challenge of Interpreting Glutamate-Receptor Ion-Channel Structures.Configurational Preference of the Glutamate Receptor Ligand Binding Domain Dimers.The dynamic AMPA receptor extracellular region: a platform for synaptic protein interactions.

P2860

Q26800669-4B49EFC6-8F79-4A96-8514-DC2CEB2B5870 Q27681450-808FBF5D-BB08-418C-A28D-BDC390216F25 Q27727973-4C1B2F0A-7FA6-4CBD-A780-E41871525BC4 Q28596597-A734850C-2840-4550-AB71-180F5F11B4EC Q30380310-78E2F6B6-9FC4-4A4D-9F4D-C562892B4642 Q30593263-7822F094-0894-41D7-A691-659ED4738E12 Q30750616-C873A21A-9D5D-448A-AC90-9E6FBBE71174 Q30774134-5CB12B1E-4740-49F3-BD6F-5430EC1A413D Q34045128-B169B774-9442-468F-BF8E-D142A79B1B6E Q34232103-8233A991-98A4-491C-938E-4282CAB7D928 Q34529888-D0BDFAFE-8A8C-4799-9CA2-EBB9CF6F173B Q34679225-CAFB9365-6BCF-4B6F-B5BA-9F78538E140A Q35731584-458F0877-361B-49E9-BB11-4EAB23AB3AB6 Q36021526-376AA266-0C3C-4523-88D9-2C06D4119E80 Q36559637-04A5655C-A56A-4C6B-9807-9FEBBDA3DF6E Q36744741-4D81310C-7997-4623-8D94-97D3ED70D6D2 Q36792602-E77B015E-7555-4712-8EDC-F24F1417CBE5 Q38218392-0F329460-8236-42AB-83D3-69E48FA451BB Q38306571-71B6E922-2CE9-478B-87D5-4E78F227486F Q38306583-15AC41B1-0629-47F5-B02F-8FB7D73460F1 Q38821887-E632E9B9-99A8-4EC4-BAAA-3824533690E1 Q38963180-765A59DF-871B-4427-BBEA-E8E482B9D0B7 Q39856314-A2C24ACB-3381-4C66-B965-213ACCD07ADA Q39999426-0049A0A5-7575-4915-9E7F-274EB4EB6068 Q41786510-F49910E0-879D-4560-BF13-AF13E1CB6285 Q42382298-499EC531-CCFF-4E7E-BA27-12C8538CFF1B Q45755617-7B79FC74-EBA0-4E9D-990C-B2084ACED722 Q47100457-0C6550E0-F046-45EE-B94E-FF2C3173C55C Q47900203-1B69A05F-BB01-4C84-82E0-ECD7A00F3C4D Q48013620-A65C0F82-752D-49D6-8A73-E2A1A2A683F8 Q52884291-9AC11E3C-6609-417A-853D-532686B1BA20

P2860

Glutamate receptor desensitization is mediated by changes in quaternary structure of the ligand binding domain.

http://www.wikidata.org/entity/Q30538804

description

2013 nî lūn-bûn

@nan

2013 թուականի Մարտին հրատարակուած գիտական յօդուած

@hyw

2013 թվականի մարտին 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

Glutamate receptor desensitiza ...... of the ligand binding domain.

@ast

Glutamate receptor desensitiza ...... of the ligand binding domain.

@en

type

label

Glutamate receptor desensitiza ...... of the ligand binding domain.

@ast

Glutamate receptor desensitiza ...... of the ligand binding domain.

@en

prefLabel

Glutamate receptor desensitiza ...... of the ligand binding domain.

@ast

Glutamate receptor desensitiza ...... of the ligand binding domain.

@en

P1433

Q30538804-49AB09ED-A3C8-481D-B914-1BCB977F566B

P1476

Q30538804-C4CF7FC2-639A-468F-99DC-0BECAB578ABC

P2093

Q30538804-0043DDEC-566A-4FAB-9CC3-71B65DF449E8

Q30538804-0428D044-CED2-4FA8-8469-559F437DE499

Q30538804-253B747D-2888-4659-A00B-9D55471C8958

Q30538804-7079D820-DD53-44EC-9037-1E18B813953A

Q30538804-8A8F9F32-F9E8-4E1E-88A9-DD2C593ABD6F

Q30538804-C9F53E56-BD8F-4E94-98E5-267828CEFB10

Q30538804-D0910F32-6A73-48E2-B62F-FB5E37247A4E

Q30538804-DFBD8871-4144-45F9-B340-AA9C1C1730C2

P2860

Q30538804-01982CA6-CD88-4DE1-B408-D6FD605D76AD

Q30538804-092250E2-30A5-41A5-88E1-C1E5698D4A6B

Q30538804-100449FC-1971-4DEE-B164-34D3CD02BC9E

Q30538804-13909F25-F6C6-4A29-9D36-8503298BED02

Q30538804-156AF53B-3EF6-490F-A056-EAC05F8BBE6A

Q30538804-1C93D021-14AA-43C7-8ADD-560F4F0FEE56

Q30538804-20B9D3DB-B249-4147-A9E9-990220464C42

Q30538804-23FFF4F8-B592-467B-9A8F-1F1A4CD76E1C

Q30538804-2A73ED02-3EF8-4D7A-B807-25057E26199C

Q30538804-2AB2740A-46A5-4F7D-8AC8-B89F8A2DEA91

P304

Q30538804-13D40CDF-13A1-4107-B9E1-6D454016CCD6

P31

Q30538804-9B0D63DE-20D7-4BEC-B6BB-2FF703E406DC

P356

Q30538804-84A4228A-DB1A-4E27-B566-CE9104E32CA8

P407

Q30538804-53AB30AA-7A05-4DD8-97E9-2E4F131F3E93

P433

Q30538804-14F2B448-F736-4693-BCB2-9C128D30FCC6

P478

Q30538804-0F8BEAC2-1C74-42DA-AB91-57B434895791

P577

Q30538804-037CD2F8-9D2B-4460-A004-2F8E9E419A8A

P5875

Q30538804-23BC95C2-8E1D-4D9C-8736-81418C42D1EB

P698

Q30538804-33F67DCF-5903-4307-AA34-E5D76C4856F6

P921

Q30538804-E1ECF1E4-DC03-48DB-AAA0-D48D8B2BDB78

P932

Q30538804-AF9E68B2-68DB-497E-A9E7-E13FFF4828AB

P356

PNAS.1217549110

P1433

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

P1476

Glutamate receptor desensitiza ...... of the ligand binding domain.

@en

P2093

Alberto Bartesaghi

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

David M Schauder

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

Jinjin Zhang

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

Katherine Klymko

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

Mario J Borgnia

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

Mark L Mayer

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

Oleg Kuybeda

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

Sriram Subramaniam

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

P2860

Emerging models of glutamate receptor ion channel structure and function

Mechanism of glutamate receptor desensitization

Structure and mechanism of kainate receptor modulation by anions

Molecular Basis of Kainate Receptor Modulation by Sodium

Stability of ligand-binding domain dimer assembly controls kainate receptor desensitization

The N-terminal domain of GluR6-subtype glutamate receptor ion channels

X-ray structure, symmetry and mechanism of an AMPA-subtype glutamate receptor

Binding site and ligand flexibility revealed by high resolution crystal structures of GluK1 competitive antagonists

Subunit-selective N-terminal domain associations organize the formation of AMPA receptor heteromers

Conformational flexibility of the ligand-binding domain dimer in kainate receptor gating and desensitization

P304

5921-5926

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

P31

scholarly article

P356

10.1073/PNAS.1217549110

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

P407

P433

15

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

P478

110

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

P577

2013-03-25T00:00:00Z

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

P5875

236081877

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

P698

23530186

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

P921

P932

3625259

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