Disrupting the scaffold to improve focal adhesion kinase-targeted cancer therapeutics - Test2 - elhamkhani - TriplyDB

Disrupting the scaffold to improve focal adhesion kinase-targeted cancer therapeutics

Disrupting the scaffold to improve focal adhesion kinase-targeted cancer therapeutics

http://www.wikidata.org/entity/Q36956868

about

FAK and paxillin, two potential targets in pancreatic cancer FAK in cancer: mechanistic findings and clinical applications FAK acts as a suppressor of RTK-MAP kinase signalling in Drosophila melanogaster epithelia and human cancer cells Cell cycle-dependent Rho GTPase activity dynamically regulates cancer cell motility and invasion in vivo Binding of the WASP/N-WASP-interacting protein WIP to actin regulates focal adhesion assembly and adhesion Pan-cancer analysis of TCGA data reveals notable signaling pathways.A heteromeric molecular complex regulates the migration of lung alveolar epithelial cells during wound healing.Functions of the FAK family kinases in T cells: beyond actin cytoskeletal rearrangement.Targeting the C-terminal focal adhesion kinase scaffold in pancreatic cancer High focal adhesion kinase expression in breast carcinoma is associated with lymphovascular invasion and triple-negative phenotype.Periostin is a novel therapeutic target that predicts and regulates glioma malignancy.Increased H⁺ efflux is sufficient to induce dysplasia and necessary for viability with oncogene expression.Pharmacokinetic analysis of the FAK scaffold inhibitor C4 in dogs FAK/PYK2 promotes the Wnt/β-catenin pathway and intestinal tumorigenesis by phosphorylating GSK3β.Design, synthesis, and biological evaluation of novel FAK scaffold inhibitors targeting the FAK-VEGFR3 protein-protein interaction.A FAK scaffold inhibitor disrupts FAK and VEGFR-3 signaling and blocks melanoma growth by targeting both tumor and endothelial cells Focal Adhesion Kinase: Insight into Molecular Roles and Functions in Hepatocellular Carcinoma Integr(at)in(g) EGFR therapy in HNSCC The FAK scaffold inhibitor C4 disrupts FAK-VEGFR-3 signaling and inhibits pancreatic cancer growth.Kindlin-3 enhances breast cancer progression and metastasis by activating Twist-mediated angiogenesis.Targeting FAK in human cancer: from finding to first clinical trials.Focal adhesion kinase inhibitors in the treatment of metastatic cancer: a patent review.Gene Expression Profiling Identifies Important Genes Affected by R2 Compound Disrupting FAK and P53 Complex.Oncogenic Receptor Tyrosine Kinases Directly Phosphorylate Focal Adhesion Kinase (FAK) as a Resistance Mechanism to FAK-Kinase Inhibitors.Molecular Pathways: Endothelial Cell FAK-A Target for Cancer Treatment.Targeting FAK scaffold functions inhibits human renal cell carcinoma growth.Simultaneous β1 integrin-EGFR targeting and radiosensitization of human head and neck cancer.Clinical significance of GAB2, a scaffolding/docking protein acting downstream of EGFR in human colorectal cancer.In vivo toxicity, metabolism and pharmacokinetic properties of FAK inhibitor 14 or Y15 (1, 2, 4, 5-benzenetetramine tetrahydrochloride).FAK Expression, Not Kinase Activity, Is a Key Mediator of Thyroid Tumorigenesis and Protumorigenic Processes.The extracellular matrix and focal adhesion kinase signaling regulate cancer stem cell function in pancreatic ductal adenocarcinoma.The discovery of new and more potent chloropyramine (C4) analogues for the potential treatment of invasive breast cancer.Kinase-targeted cancer therapies: progress, challenges and future directions.Endogenous Control Mechanisms of FAK and PYK2 and Their Relevance to Cancer Development.Targeting Focal Adhesion Kinase Using Inhibitors of Protein-Protein Interactions Imidazoles as potential anticancer agents

P2860

Q26765360-D6E177A8-00F0-40F7-83CA-80A526042F41 Q27026533-1E79F30D-F799-4E6B-9E25-ED88D52FF24E Q27316587-155B34B9-32B7-4540-AE90-4FD2B2092AC0 Q27339470-D24C77F3-8936-44A1-A0F8-39EE6C5D9E2C Q30583693-48824D92-C431-4176-8046-C81431ED5521 Q30980050-094F8F0E-5A90-4123-A082-FE0924BBC658 Q33708583-5530A7AE-B6EF-443E-B762-B1DCD4931E2E Q34016697-8F84D592-13A7-4E9D-BEFB-1965F9DC8D60 Q34173290-5787433F-21D1-4384-B606-F8274D8375AE Q34423151-FCF6F62C-8F98-4A97-A911-D2FAACA92E98 Q34434262-FEE37586-51AF-4FF9-B508-DC76D06F623B Q35354608-DFBF69A8-39F1-4B37-AC0B-8F8AFE1D7D31 Q35582654-3E019288-F7C9-46C0-98F5-47D3D50C97DF Q36023053-5DB455DE-D11A-4F05-B3E2-7CBB529C9769 Q36051470-6DBC5365-3079-480B-A3A0-0D8853842E01 Q36188833-950E57E1-7C2A-4CB6-9425-25A6C81F0546 Q36244298-DC95C1BE-889F-4535-86E9-A6EA4FE0B9E9 Q36403862-D60D3D11-144D-46AA-AAF2-F87E5219BB8D Q37381588-46848F3F-CF2E-41F7-9637-F630BC049A58 Q37702930-42FC72F2-E0DE-42CA-B6C5-937630F38E9C Q38175738-E74FE85C-C6E7-472F-BE4E-AE2BC1028FF8 Q38239003-BF6524C7-2798-4173-9850-FCEA41B76F29 Q38671984-991EBC76-196A-4EA2-9C00-92A16AB2DE5F Q38745849-57394477-5B49-44AF-B7B5-F94D8075C629 Q38854580-68434B80-42CF-46F1-A40E-717A52B64FE7 Q38895097-512D48CA-4FF0-4324-9733-D86AE4C08361 Q38911597-F22B2EE8-55B9-4700-971C-42AB1AA21139 Q38974852-909D32A4-0853-4200-921B-7A23D6FE1FB1 Q39177740-BC5454D0-EA93-445B-8A5F-FBEDF6BDBEDB Q39711361-7CAA3F8D-789F-45B6-83EE-646ED8E98EFE Q40969084-F3F3BCA0-5E84-4829-955C-B0482882129F Q47665634-382920C8-B61F-4EED-AF0D-71724E9BCF09 Q49887882-E7126501-38B2-471E-AF79-ECF44241BB97 Q54976490-AF221657-013B-43ED-BFBD-E239B1175A4B Q58726403-657EFC67-7358-483C-B858-4C89559EA14D Q59149996-4814A6CD-8DC4-4121-BE9A-9BCA6D31FE6D

P2860

Disrupting the scaffold to improve focal adhesion kinase-targeted cancer therapeutics

http://www.wikidata.org/entity/Q36956868

description

2013 nî lūn-bûn

@nan

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

2013年论文

@zh

2013年论文

@zh-cn

name

Disrupting the scaffold to improve focal adhesion kinase-targeted cancer therapeutics

@en

type

label

Disrupting the scaffold to improve focal adhesion kinase-targeted cancer therapeutics

@en

prefLabel

Disrupting the scaffold to improve focal adhesion kinase-targeted cancer therapeutics

@en

P1433

Q36956868-4B711D2C-02FD-4CD7-96B0-57FFF79D86A5

P1476

Q36956868-CED771A0-323C-418B-B196-1001AFA86225

P2093

Q36956868-0910262D-E987-45B7-ACBF-1CCCB6C5B501

Q36956868-2749E0CC-42A5-48E2-974D-4A039B08E216

Q36956868-3B8E9048-5794-456C-A459-23289D0E14AF

Q36956868-E0E0947A-E4EF-49C5-89FF-916E0AEAB5EE

P2860

Q36956868-0702C5FF-5FBA-4084-801B-4F91E61E716C

Q36956868-10BA335E-9175-43D5-AB6E-CDC6F7830949

Q36956868-1623C773-E096-4136-A456-E5CA9DF8D5C2

Q36956868-233F00F3-C339-4E8D-9874-C345BCC212DA

Q36956868-2B5B4526-55E4-456B-B098-4B3523800337

Q36956868-3B300508-8E06-4754-B458-45C265F9A7E9

Q36956868-3BA7EAC6-CFA8-442D-86CE-A18B87756290

Q36956868-5F4EE108-BEDE-407A-B8A1-628E79AF9847

Q36956868-639E5D92-C51A-430A-913B-5AC16A6DF458

Q36956868-646DF82B-9C7E-4F28-87BF-D81CF6CD99F7

P304

Q36956868-AEF0E4D3-681C-43FD-A545-E6AEC1F0BAFB

P31

Q36956868-42E1A351-F69B-4E84-97DF-42F3340E2F9E

P356

Q36956868-80C2C9DC-474C-4C15-ABBC-82B8B627BB97

P433

Q36956868-1ED1DB09-BDCB-4677-BDAB-4AAA4BCFB754

P478

Q36956868-EA7B6D51-F26E-4230-89FA-DFFA2F94D4EB

P577

Q36956868-6A2C4735-4690-4CF4-BE60-CA3C3922CC1C

P698

Q36956868-E74DB59A-FE19-4FDA-B313-7A9F30F51842

P932

Q36956868-3A5A887E-2FF3-497B-85EA-E2471FC17A8F

P356

SCISIGNAL.2004021

P1433

Science Signaling

P1476

Disrupting the scaffold to improve focal adhesion kinase-targeted cancer therapeutics

@en

P2093

Elena Kurenova

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

Timothy Marlowe

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

Vita Golubovskaya

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

William G Cance

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

P2860

Hallmarks of Cancer: The Next Generation

Phosphorylation of focal adhesion kinase on tyrosine 194 by Met leads to its activation through relief of autoinhibition

Direct interaction of the N-terminal domain of focal adhesion kinase with the N-terminal transactivation domain of p53

pp125FAK a structurally distinctive protein-tyrosine kinase associated with focal adhesions.

Autophosphorylation of the focal adhesion kinase, pp125FAK, directs SH2-dependent binding of pp60src

Structural basis for the autoinhibition of focal adhesion kinase

In vivo activation of the p53 pathway by small-molecule antagonists of MDM2

Antitumor activity and pharmacology of a selective focal adhesion kinase inhibitor, PF-562,271

FAK integrates growth-factor and integrin signals to promote cell migration

Regulation of focal adhesion-associated protein tyrosine kinase by both cellular adhesion and oncogenic transformation

P304

pe10

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

P31

scholarly article

P356

10.1126/SCISIGNAL.2004021

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

P433

268

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

P478

6

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

P577

2013-03-26T00:00:00Z

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

P698

23532331

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

P932

3693475

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