Bcl-2 targets the protein kinase Raf-1 to mitochondria (Q24321753)

GOA release 2020-03-11

apoptotic process

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ORCID Public Data File 2021

GOA release 2020-03-11

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author name string

H G Wang

series ordinal

1

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U R Rapp

series ordinal

2

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J C Reed

series ordinal

3

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language of work or name

English

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publication date

15 November 1996

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published in

Cell

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volume

87

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page(s)

629-38

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issue

4

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cites work

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The protein bcl-2 alpha does not require membrane attachment, but two conserved domains to suppress apoptosis

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Diminished cell proliferation associated with the death-protective activity of Bcl-2

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Serum-, TPA-, and Ras-induced expression from Ap-1/Ets-driven promoters requires Raf-1 kinase

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The ins and outs of Raf kinases

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Correlation of two-hybrid affinity data with in vitro measurements

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Molecular glue: kinase anchoring and scaffold proteins

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A biochemical function for ras--at last

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C. elegans lin-45 raf gene participates in let-60 ras-stimulated vulval differentiation.

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Structure-function analysis of Bcl-2 protein. Identification of conserved domains important for homodimerization with Bcl-2 and heterodimerization with Bax.

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A 70-kd protein of the yeast mitochondrial outer membrane is targeted and anchored via its extreme amino terminus

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Bcl-2 functions in an antioxidant pathway to prevent apoptosis

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Functional dissection of the human Bc12 protein: sequence requirements for inhibition of apoptosis

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Ras-induced activation of Raf-1 is dependent on tyrosine phosphorylation

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Bcl-2 inhibition of neural death: decreased generation of reactive oxygen species

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Raf-1 protein kinase is required for growth of induced NIH/3T3 cells

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Raf-1 activates MAP kinase-kinase

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Requirement for Ras in Raf activation is overcome by targeting Raf to the plasma membrane

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Induction of apoptotic program in cell-free extracts: requirement for dATP and cytochrome c

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Regulation of cell division cycle progression by bcl-2 expression: a potential mechanism for inhibition of programmed cell death

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X-ray and NMR structure of human Bcl-xL, an inhibitor of programmed cell death

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Cell-free apoptosis in Xenopus egg extracts: inhibition by Bcl-2 and requirement for an organelle fraction enriched in mitochondria.

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Bcl-2 heterodimerizes in vivo with a conserved homolog, Bax, that accelerates programmed cell death

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Checkpoints of dueling dimers foil death wishes

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c-myc and bcl-2 modulate p53 function by altering p53 subcellular trafficking during the cell cycle

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Interactions among members of the Bcl-2 protein family analyzed with a yeast two-hybrid system.

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Multiple Bcl-2 family members demonstrate selective dimerizations with Bax

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Activation of Raf as a result of recruitment to the plasma membrane

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Cloning and functional analysis of BAG-1: a novel Bcl-2-binding protein with anti-cell death activity

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A protein kinase similar to MAP kinase activator acts downstream of the raf kinase in Drosophila

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R-Ras promotes apoptosis caused by growth factor deprivation via a Bcl-2 suppressible mechanism.

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Bcl-2 interacting protein, BAG-1, binds to and activates the kinase Raf-1

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Constitutive expression of the machinery for programmed cell death

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The intracellular distribution and pattern of expression of Mcl-1 overlap with, but are not identical to, those of Bcl-2

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Mitochondrial control of nuclear apoptosis.

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Proapoptotic protein Bax heterodimerizes with Bcl-2 and homodimerizes with Bax via a novel domain (BH3) distinct from BH1 and BH2

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Normal and oncogenic p21ras proteins bind to the amino-terminal regulatory domain of c-Raf-1

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7 January 2021

10.1016/S0092-8674(00)81383-5

Identifiers

DOI

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Consolidated OpenCitations Corpus – April 2017

962953

962953

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Consolidated OpenCitations Corpus – April 2017

Consolidated OpenCitations Corpus – April 2017

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