Structures of the cancer-related Aurora-A, FAK, and EphA2 protein kinases from nanovolume crystallography (Q27640105)

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Ciarán N Cronin

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Duncan E McRee

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Christian G Nelson

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Nikola P Pavletich

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Joe Rogers

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Bi-Ching Sang

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Daniel N Scheibe

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Ronald V Swanson

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Devon A Thompson

Protein kinases--the major drug targets of the twenty-first century?

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language of work or name

English

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publication date

December 2002

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published in

Structure

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volume

10

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issue

12

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page(s)

1659-67

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The ephrin-A1 ligand and its receptor, EphA2, are expressed during tumor neovascularization

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Activation of EphA2 kinase suppresses integrin function and causes focal-adhesion-kinase dephosphorylation

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EphrinA1-induced cytoskeletal re-organization requires FAK and p130(cas).

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cDNA cloning, expression, subcellular localization, and chromosomal assignment of mammalian aurora homologues, aurora-related kinase (ARK) 1 and 2

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A homologue of Drosophila aurora kinase is oncogenic and amplified in human colorectal cancers

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A putative serine/threonine kinase encoding gene BTAK on chromosome 20q13 is amplified and overexpressed in human breast cancer cell lines

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Association of centrosomal kinase STK15/BTAK mRNA expression with chromosomal instability in human breast cancers

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Interaction and feedback regulation between STK15/BTAK/Aurora-A kinase and protein phosphatase 1 through mitotic cell division cycle

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Identifiers

DOI

1 reference

Consolidated OpenCitations Corpus – April 2017

1 reference

Consolidated OpenCitations Corpus – April 2017

PubMed publication ID

12467573

1 reference

Consolidated OpenCitations Corpus – April 2017