(Q34101310)

31 July 2017

title

Ras-activated endocytosis is mediated by the Rab5 guanine nucleotide exchange activity of RIN1. (English)

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31 July 2017

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G G Tall

1

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31 July 2017

M A Barbieri

series ordinal

2

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31 July 2017

P D Stahl

series ordinal

3

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31 July 2017

B F Horazdovsky

series ordinal

4

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31 July 2017

language of work or name

English

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publication date

1 July 2001

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31 July 2017

number of pages

10

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inferred from page(s)

published in

Developmental Cell

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31 July 2017

volume

1

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31 July 2017

issue

1

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31 July 2017

page(s)

73-82

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Regulation of the oncogenic activity of BCR-ABL by a tightly bound substrate protein RIN1.

31 July 2017

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Evidence for a symmetrical requirement for Rab5-GTP in in vitro endosome-endosome fusion

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Protein kinase B/akt and rab5 mediate Ras activation of endocytosis

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Co-operative regulation of endocytosis by three Rab5 isoforms

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The small GTPase rab5 functions as a regulatory factor in the early endocytic pathway

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Regulation of signal transduction by endocytosis

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Cell movement elicited by epidermal growth factor receptor requires kinase and autophosphorylation but is separable from mitogenesis

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Functional independence of the epidermal growth factor receptor from a domain required for ligand-induced internalization and calcium regulation

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Expression of three mammalian cDNAs that interfere with RAS function in Saccharomyces cerevisiae

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Vps9p is a guanine nucleotide exchange factor involved in vesicle-mediated vacuolar protein transport

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A human protein selected for interference with Ras function interacts directly with Ras and competes with Raf1

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7 January 2021

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Ligand-induced transformation by a noninternalizing epidermal growth factor receptor

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7 January 2021

Multiple Ras functions can contribute to mammalian cell transformation

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7 January 2021

10.1016/S1534-5807(01)00008-9

Identifiers

DOI

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31 July 2017

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