Crystal structure of the cytoskeleton-associated protein glycine-rich (CAP-Gly) domain - Test2 - elhamkhani - TriplyDB

Crystal structure of the cytoskeleton-associated protein glycine-rich (CAP-Gly) domain

Crystal structure of the cytoskeleton-associated protein glycine-rich (CAP-Gly) domain

http://www.wikidata.org/entity/Q27639629

about

Structural basis of microtubule plus end tracking by XMAP215, CLIP-170, and EB1 Microtubule binding proteins CLIP-170, EB1, and p150Glued form distinct plus-end complexes CLIPs and CLASPs and cellular dynamics MolProbity: all-atom structure validation for macromolecular crystallography An ENU-induced mutation in mouse glycyl-tRNA synthetase (GARS) causes peripheral sensory and motor phenotypes creating a model of Charcot-Marie-Tooth type 2D peripheral neuropathy The microtubule plus-end proteins EB1 and dynactin have differential effects on microtubule polymerization Domain analysis of the tubulin cofactor system: a model for tubulin folding and dimerization SGCEdb: a flexible database and web interface integrating experimental results and analysis for structural genomics focusing on Caenorhabditis elegans.Crystal structure of the amino-terminal microtubule-binding domain of end-binding protein 1 (EB1)Structural basis for tubulin recognition by cytoplasmic linker protein 170 and its autoinhibition The architecture ofTrypanosoma bruceitubulin-binding cofactor B and implications for function Three-Dimensional Structure of CAP-Gly Domain of Mammalian Dynactin Determined by Magic Angle Spinning NMR Spectroscopy: Conformational Plasticity and Interactions with End-Binding Protein EB1 S-SAD phasing study of death receptor 6 and its solution conformation revealed by SAXS 3MATRIX and 3MOTIF: a protein structure visualization system for conserved sequence motifs.Internal dynamics of dynactin CAP-Gly is regulated by microtubules and plus end tracking protein EB1.Against the odds? De novo structure determination of a pilin with two cysteine residues by sulfur SAD.Minimal plus-end tracking unit of the cytoplasmic linker protein CLIP-170.Solution structure of a ubiquitin-like domain from tubulin-binding cofactor B.The solution structure of the N-terminal domain of human tubulin binding cofactor C reveals a platform for tubulin interaction.Dynactin is required for transport initiation from the distal axon Ordered recruitment of dynactin to the microtubule plus-end is required for efficient initiation of retrograde axonal transport.Phenotypic spectrum of disorders associated with glycyl-tRNA synthetase mutations.In vivo roles of the basic domain of dynactin p150 in microtubule plus-end tracking and dynein function A pachygyria-causing alpha-tubulin mutation results in inefficient cycling with CCT and a deficient interaction with TBCB.The G59S mutation in p150(glued) causes dysfunction of dynactin in mice.Faithful chaperones.Autoinhibition of TBCB regulates EB1-mediated microtubule dynamics.DCTN1-related neurodegeneration: Perry syndrome and beyond.Dynactin has two antagonistic regulatory domains and exerts opposing effects on dynein motility.The tumor suppressor CYLD regulates microtubule dynamics and plays a role in cell migration.The novel microtubule-associated CAP-glycine protein Cgp1 governs growth, differentiation, and virulence of Cryptococcus neoformans.A SxIP motif interaction at the microtubule plus end is important for processive retrograde axonal transport.

P2860

Q24294735-DAF0DC87-6DDD-43A0-941B-E576C2996630 Q24303467-55A6E146-1952-4242-8A4D-811267BAEC54 Q24304264-22651A7F-91B0-47CF-BF68-064F1C2DE57D Q24649111-C2CD092F-3874-40E9-81F6-80D18F18FC37 Q24651733-82519A91-5FC9-4281-91B9-570F30D4AC7C Q24683085-7A8B33F1-F574-471E-A8BB-D3C97032CF7B Q24793246-C3BFB55A-A67D-4D0C-9B5F-2F3B93FCDA13 Q25257790-E123F62A-53F6-4BF9-A711-CDD11342F838 Q27641666-CA6D5486-D640-42B8-A1F3-FE320BB92B17 Q27645613-E62AFC76-5D91-4464-8D57-6A5B8F31FD81 Q27677849-143FE76F-C6C9-46A3-B10B-33795143AA20 Q27678013-A3511532-A4AB-4DE8-A58F-C6B219839C83 Q27678676-8653E7CC-B6EC-4592-B41B-BCFD6DFF79B4 Q30333048-9D75BD67-A90F-4C19-93E0-BE5C18B09758 Q30369179-56463133-F6EB-4943-95A0-C0CF5706636E Q30374426-28B0AFB0-5720-4058-94A5-55E6847CA7D6 Q30486352-4E57FB1D-4C56-43D2-9618-0194EE41F3AD Q33206776-3F216E9C-BD8B-4376-BDB6-1E3FFF37253E Q34058343-C79D4DF6-5E20-4633-81A9-8716FD63CB23 Q34271545-F0CB0095-9EEC-4A1E-B9BE-D729DBD3AD8E Q34362627-33260A8E-809A-4E97-824C-509B825D2CAD Q34433595-107CF2B4-99A7-4743-AB34-34D3CADA1063 Q35748592-3902767C-A4AA-4D42-8C02-C16CC538E5BD Q36489030-5ABCB284-920D-4209-BCE9-AC0FB334B459 Q36632294-4B7C7FC0-0736-422F-93DC-4A696A823E71 Q37886778-6800C23C-68DB-491D-A8FA-309CF03969B7 Q39286907-6CBEA953-9693-42CD-9121-5E90494F717A Q39381016-7F731C9E-447C-469F-A48E-E2208910AE95 Q41545103-96F608BC-89C5-4738-B46C-392CDF196AD7 Q46789192-7DF2B369-D83A-4326-95EA-631CFD29C663 Q48507287-ECDAAC28-6136-4AF0-BB02-44C8F9D7CA92 Q52649006-E2F0F1B7-1068-4037-8B10-318328E39EB8

P2860

Crystal structure of the cytoskeleton-associated protein glycine-rich (CAP-Gly) domain

http://www.wikidata.org/entity/Q27639629

description

2002 nî lūn-bûn

@nan

2002 թուականի Դեկտեմբերին հրատարակուած գիտական յօդուած

@hyw

2002 թվականի դեկտեմբերին հրատարակված գիտական հոդված

@hy

2002年の論文

@ja

2002年学术文章

@wuu

2002年学术文章

@zh-cn

2002年学术文章

@zh-hans

2002年学术文章

@zh-my

2002年学术文章

@zh-sg

2002年學術文章

@yue

name

Crystal structure of the cytoskeleton-associated protein glycine-rich (CAP-Gly) domain

@ast

Crystal structure of the cytoskeleton-associated protein glycine-rich (CAP-Gly) domain

@en

Crystal structure of the cytoskeleton-associated protein glycine-rich (CAP-Gly) domain

@nl

type

label

Crystal structure of the cytoskeleton-associated protein glycine-rich (CAP-Gly) domain

@ast

Crystal structure of the cytoskeleton-associated protein glycine-rich (CAP-Gly) domain

@en

Crystal structure of the cytoskeleton-associated protein glycine-rich (CAP-Gly) domain

@nl

prefLabel

Crystal structure of the cytoskeleton-associated protein glycine-rich (CAP-Gly) domain

@ast

Crystal structure of the cytoskeleton-associated protein glycine-rich (CAP-Gly) domain

@en

Crystal structure of the cytoskeleton-associated protein glycine-rich (CAP-Gly) domain

@nl

P1433

Q27639629-A7E234BF-267A-4D7D-885E-7240D4F7CEA2

P1476

Q27639629-98EAE397-FEAB-4A12-849B-F05FA1E8563A

P2093

Q27639629-094B6DCC-A0DE-4E63-A008-F301FA90FC92

Q27639629-09C25A15-4C34-4803-AE76-ADECFA6ECE0E

Q27639629-127CA69C-9818-4929-861B-CC853235B0D4

Q27639629-3D58FD28-EEB9-45A9-99D1-E090137175CB

Q27639629-5E0DBFE3-FE8B-404D-B05F-4500859C3C84

Q27639629-85CBE0BE-1B58-44D9-9719-DB69358C8B23

Q27639629-861284A0-A252-4A31-989C-3FF51B67A18F

Q27639629-9C9CAB12-815E-4CEA-B71E-04D13CA7CCED

Q27639629-C3609D71-E68A-4B5F-A8D1-3936E8C6F09C

Q27639629-C5B44534-BF4B-4302-BB33-517F05C1A789

P2860

Q27639629-08FEFE97-3A34-4D69-9F8A-41BDA8576424

Q27639629-0FAD3CB5-72F0-42E2-9BEA-EB3E135FB0FF

Q27639629-116A6362-2F17-4E3F-B478-D543A1147F32

Q27639629-1933B097-9EF6-48F2-A786-FB5A1FEB0346

Q27639629-2054FC30-D222-4D90-8536-A4FB527D82B7

Q27639629-2F7DB8FE-776C-4271-8069-AE9EF4D7D202

Q27639629-34A267CD-CA38-4931-9B7C-0FFB38CA88A1

Q27639629-36529F5E-3F96-416E-A721-00ADC9A931D7

Q27639629-3692C23E-00FE-46BD-90E2-EA00EE1F83B9

Q27639629-3FF94657-1468-4DC3-810A-CC9C6D8B8556

P304

Q27639629-B7F448F3-E770-4432-90E6-AC1777A9D632

P31

Q27639629-AA80B41D-AC7D-4321-9790-73A753B6878E

P356

Q27639629-021B8B55-3174-40CE-B01E-B4BF921F7369

P407

Q27639629-429D7048-9532-4D7B-B9E2-0F7644F1827B

P433

Q27639629-D6653298-3B46-4506-9F2A-59642A33061C

P478

Q27639629-182E3DD2-89F4-414F-B875-7CC7DD0A1049

P50

Q27639629-314713DA-03B3-423B-858F-A052229E1959

P577

Q27639629-46FCB340-C83B-46BD-825E-6E4BF8844624

P698

Q27639629-31F8B4D2-0693-422C-B617-0E696C8DA4B0

P921

Q27639629-201F414C-2009-464A-96D3-9173BAC2A370

Q27639629-2B3F89F0-89ED-433A-BF8E-F823573BD73C

Q27639629-633AD67F-E8A0-43F8-A30F-F302A47C2FF3

P356

P1433

Journal of Biological Chemistry

P1476

Crystal structure of the cytoskeleton-associated protein glycine-rich (CAP-Gly) domain

@en

P2093

Bingdong Sha

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

Chi-Hao Luan

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

David Johnson

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

Guangda Lin

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

Hongli Chen

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

Jim Finley

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

Jun Tsao

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

Jun Zhao

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

Lawrence J DeLucas

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

Lisa A Nagy

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

P2860

Cloning, expression, and mapping of CKAPI, which encodes a putative cytoskeleton-associated protein containing a CAP-GLY domain

CLIP-170 links endocytic vesicles to microtubules

Methods for assessing the statistical significance of molecular sequence features by using general scoring schemes

Improved methods for building protein models in electron density maps and the location of errors in these models

Crystallography & NMR System: A New Software Suite for Macromolecular Structure Determination

Processing of X-ray diffraction data collected in oscillation mode

Structure of the Ca2+-regulated photoprotein obelin at 1.7 Å resolution determined directly from its sulfur substructure

The Pfam protein families database

Genome sequence of the nematode C. elegans: a platform for investigating biology

CLIP-170 highlights growing microtubule ends in vivo

P304

48596-601

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

P31

scholarly article

P356

10.1074/JBC.M208512200

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

P407

P433

50

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

P478

277

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

P50

P577

2002-12-13T00:00:00Z

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

P698

12221106

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

P921

protein structure

crystal structure