Novel functions of CCM1 delimit the relationship of PTB/PH domains. (Q38683544)

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25 March 2020

title

Novel functions of CCM1 delimit the relationship of PTB/PH domains (English)

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author name string

Jun Zhang

1

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25 March 2020

Pallavi Dubey

2

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Akhil Padarti

3

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Aileen Zhang

4

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Rinkal Patel

5

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Vipulkumar Patel

6

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David Cistola

7

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Ahmed Badr

8

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publication date

8 July 2017

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BBA - Proteins and Proteomics

25 March 2020

published in

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volume

1865

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issue

10

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page(s)

1274-1286

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The disabled 1 phosphotyrosine-binding domain binds to the internalization signals of transmembrane glycoproteins and to phospholipids

25 March 2020

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CCM2 expression parallels that of CCM1.

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Sorting nexin 17, a non-self-assembling and a PtdIns(3)P high class affinity protein, interacts with the cerebral cavernous malformation related protein KRIT1

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ccm1 cell autonomously regulates endothelial cellular morphogenesis and vascular tubulogenesis in zebrafish

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Crystal structure of the human Fe65-PTB1 domain

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Structural basis for the autoinhibition of talin in regulating integrin activation

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Structure of the C-terminal phosphotyrosine interaction domain of Fe65L1 complexed with the cytoplasmic tail of amyloid precursor protein reveals a novel peptide binding mode

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10.1016/J.BBAPAP.2017.07.002

Identifiers

DOI

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25 March 2020

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25 March 2020

PubMed publication ID

28698152

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