Structural basis for the transforming activity of human cancer-related signaling adaptor protein CRK
about
The proximal signaling network of the BCR-ABL1 oncogene shows a modular organizationOnD-CRF: predicting order and disorder in proteins using [corrected] conditional random fieldsThe Role of Crk Adaptor Proteins in T-Cell Adhesion and MigrationThe adaptor protein Crk in immune responseRole of Exosomal Noncoding RNAs in Lung CarcinogenesisThe Tumor Cytosol miRNAs, Fluid miRNAs, and Exosome miRNAs in Lung CancerStructural basis for regulation of the Crk signaling protein by a proline switch.Domain organization differences explain Bcr-Abl's preference for CrkL over CrkIIThe SH2 domain-containing proteins in 21 species establish the provenance and scope of phosphotyrosine signaling in eukaryotesThe language of SH2 domain interactions defines phosphotyrosine-mediated signal transductionSH3 domains: modules of protein-protein interactions.A pre-metazoan origin of the CRK gene family and co-opted signaling networkA lack of peptide binding and decreased thermostability suggests that the CASKIN2 scaffolding protein SH3 domain may be vestigial.Cyclophilin A promotes cell migration via the Abl-Crk signaling pathway.Reciprocal regulation of Abl kinase by Crk Y251 and Abi1 controls invasive phenotypes in glioblastoma.Prolyl isomerization as a molecular memory in the allosteric regulation of the signal adapter protein c-CrkII.Iterative tyrosine phosphorylation controls non-canonical domain utilization in Crk.Essential roles of Crk and CrkL in fibroblast structure and motility.Models of crk adaptor proteins in cancer.Commentary: The carboxyl-terminal Crk SH3 domain: Regulatory strategies and new perspectives.Functional mechanisms and roles of adaptor proteins in abl-regulated cytoskeletal actin dynamics.Domain cooperativity in multidomain proteins: what can we learn from molecular alignment in anisotropic media?Phosphorylation of Crk on tyrosine 251 in the RT loop of the SH3C domain promotes Abl kinase transactivationProteins that bind the Src homology 3 domain of CrkI have distinct roles in Crk transformationDistinct roles for Crk adaptor isoforms in actin reorganization induced by extracellular signalsCrk adaptor protein-induced phosphorylation of Gab1 on tyrosine 307 via Src is important for organization of focal adhesions and enhanced cell migration.A crucial role in cell spreading for the interaction of Abl PxxP motifs with Crk and Nck adaptors.Real-time fluorescent resonance energy transfer analysis to monitor drug resistance in chronic myelogenous leukemia.CRK proteins selectively regulate T cell migration into inflamed tissues.Tyr724 phosphorylation of ELMO1 by Src is involved in cell spreading and migration via Rac1 activation.CrkII transgene induces atypical mammary gland development and tumorigenesis.Molecular dynamics of the proline switch and its role in Crk signaling.microRNAs and lung cancer: tumors and 22-mers.Genetic susceptibility on CagA-interacting molecules and gene-environment interaction with phytoestrogens: a putative risk factor for gastric cancer.Secondary structure, a missing component of sequence-based minimotif definitions.Contribution of Crk adaptor proteins to host cell and bacteria interactions.Emerging roles for crk in human cancer.Crk adaptors negatively regulate actin polymerization in pedestals formed by enteropathogenic Escherichia coli (EPEC) by binding to Tir effector.Binding cavities and druggability of intrinsically disordered proteins.Analysis of an independent tumor suppressor locus telomeric to Tp53 suggested Inpp5k and Myo1c as novel tumor suppressor gene candidates in this region.
P2860
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
P248
Q24294830-574DAB45-A6E2-423E-9960-A9CC03C8813CQ24653665-2FCBA6D8-4CF9-4C92-9BB1-3704CE28F39CQ26779209-618706E9-FCED-4A31-B52E-9A26A5CC5A3CQ26849320-1ED351E8-12A1-4026-8DEF-7263E4289D4EQ27000282-88E73BA4-23F8-492C-8EF9-63D518BD0AFBQ27012447-A56E7D60-5CB0-4B88-AD52-0E89C2F631BEQ27666184-673C01C1-21DB-4E6F-87BB-B7ACA7A38CF8Q27679069-8EE0F695-AAB4-4335-AED9-0B33EE22B09DQ28255020-738BD2B3-F890-4C38-BF22-FEAA45571591Q28266221-0B72022D-981E-4988-B0C1-4E9C728B33C5Q30008731-71771B2D-20FE-472B-B511-1C1964782789Q30008856-6594321B-17AD-48AA-AC4B-1F5FE919B0AEQ30008864-7F63CB6E-0DE9-4E7D-B6B3-F6B1F463CF13Q30009060-55FCAF71-7D7E-4FC6-8071-D82F3130B57AQ30009085-9D2C8556-B2B9-46A6-80DC-990D96F0EA04Q30009258-C7FE7342-9BE0-4DA8-AC5B-3803E20B6295Q30009282-90515DD3-E8F1-4649-9B56-0E1CEF8C68A2Q30009535-FAF700FD-957B-4FDC-B594-A4BC92BDF386Q30009961-D2BBEB7D-53CC-4ABE-A953-E96F89050895Q30010069-1BC2CC0B-A412-443E-ACCC-DA0A6E71550FQ30010077-1666721F-C403-4679-953E-9E6BE0B4BBFEQ30010233-9A16EA64-CFED-4902-A709-94035E45CA83Q30010491-0F1AAE12-51A9-406C-809F-76986CD80617Q30156056-CC7E1623-A14C-4BB6-9C82-F79F4D249288Q30157067-C7D6EC46-384B-4283-9605-6884E58EF8BCQ30157305-8A9BDE4C-6B2E-4828-B869-5F9FCF7D4BB3Q30157529-430A7A1F-6CBF-41C8-9615-24AC8EFC4A3BQ30512706-291EEC24-93B7-4C24-A71E-EB51967538B3Q30628412-5FC2B05B-7779-442B-83EE-3F34B22EF482Q30658863-2B3EF107-665A-4D9C-BDE1-A851F0B7D902Q33556409-E30DB670-BE31-43F0-BA91-0A267106DC31Q33558265-D661A187-ECFB-4E68-A1EA-6D3754718D11Q33910328-F75A9762-64CC-4A8E-9921-E2D759F1E890Q34181602-8154ED29-ABDC-4035-A666-B5AC6D86B6D6Q34510288-C2901128-94F3-4134-877D-8CF4DC8A9253Q34660465-16CC734C-469A-4EB8-A7C4-C2CD54881C7BQ34972759-5086FDEF-5DA4-40B4-96FE-C7F2D0A9F344Q35133400-AAF600F1-3414-4E53-84B2-06B7FC3BB295Q35571730-1C7C5AA9-F3F3-4C8D-AF98-526A6B58D4FBQ35690131-580A8030-AD6A-43D4-A9E5-4118A4BE5C9F
P2860
Structural basis for the transforming activity of human cancer-related signaling adaptor protein CRK
description
2007 nî lūn-bûn
@nan
2007 թուականի Յունիսին հրատարակուած գիտական յօդուած
@hyw
2007 թվականի հունիսին հրատարակված գիտական հոդված
@hy
2007年の論文
@ja
2007年論文
@yue
2007年論文
@zh-hant
2007年論文
@zh-hk
2007年論文
@zh-mo
2007年論文
@zh-tw
2007年论文
@wuu
name
Structural basis for the trans ...... signaling adaptor protein CRK
@ast
Structural basis for the trans ...... signaling adaptor protein CRK
@en
Structural basis for the trans ...... signaling adaptor protein CRK
@nl
type
label
Structural basis for the trans ...... signaling adaptor protein CRK
@ast
Structural basis for the trans ...... signaling adaptor protein CRK
@en
Structural basis for the trans ...... signaling adaptor protein CRK
@nl
prefLabel
Structural basis for the trans ...... signaling adaptor protein CRK
@ast
Structural basis for the trans ...... signaling adaptor protein CRK
@en
Structural basis for the trans ...... signaling adaptor protein CRK
@nl
P2093
P2860
P921
P3181
P356
P1476
Structural basis for the trans ...... signaling adaptor protein CRK
@en
P2093
Hiroyuki Kumeta
Kenji Ogura
Masashi Yokochi
Masato Naito
Mieko Sakai
Shinya Tanaka
Yoshihiro Kobashigawa
Yoshinori Makino
P2860
P2888
P304
P3181
P356
10.1038/NSMB1241
P577
2007-06-01T00:00:00Z
P5875
P6179
1006835088