The structure of Bcl-w reveals a role for the C-terminal residues in modulating biological activity (Q24683846)

1

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Martin Lackmann

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Gretchen L Skea

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Penny J Harrison

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David C S Huang

Rationale for Bcl-xL/Bad peptide complex formation from structure, mutagenesis, and biophysical studies

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language of work or name

English

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publication date

1 April 2003

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published in

The EMBO Journal

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volume

22

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issue

7

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page(s)

1497-507

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cites work

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Conformation of the Bax C-terminus regulates subcellular location and cell death

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The conserved N-terminal BH4 domain of Bcl-2 homologues is essential for inhibition of apoptosis and interaction with CED-4

7 April 2017

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Bim: a novel member of the Bcl-2 family that promotes apoptosis

7 April 2017

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Cytosol-to-membrane redistribution of Bax and Bcl-X(L) during apoptosis

7 April 2017

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bcl-w, a novel member of the bcl-2 family, promotes cell survival

7 April 2017

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Investigation of the subcellular distribution of the bcl-2 oncoprotein: residence in the nuclear envelope, endoplasmic reticulum, and outer mitochondrial membranes

7 April 2017

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Solution structure of a Bcl-2 homolog from Kaposi sarcoma virus

7 April 2017

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Solution structure of the antiapoptotic protein bcl-2

7 April 2017

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Structure of Bax: coregulation of dimer formation and intracellular localization

7 April 2017

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Solution structure and mutagenesis of the caspase recruitment domain (CARD) from Apaf-1

7 April 2017

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Solution structure of the proapoptotic molecule BID: a structural basis for apoptotic agonists and antagonists

7 April 2017

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Solution structure of BID, an intracellular amplifier of apoptotic signaling

7 April 2017

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Crystal structure of rat Bcl-xL. Implications for the function of the Bcl-2 protein family

7 April 2017

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Structure of Bcl-xL-Bak peptide complex: recognition between regulators of apoptosis

7 April 2017

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

7 April 2017

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7 April 2017

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7 April 2017

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7 April 2017

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7 April 2017

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7 April 2017

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BCL-2, BCL-X(L) sequester BH3 domain-only molecules preventing BAX- and BAK-mediated mitochondrial apoptosis

7 April 2017

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Tissue expression and subcellular localization of the pro-survival molecule Bcl-w

7 April 2017

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Ligand for EPH-related kinase (LERK) 7 is the preferred high affinity ligand for the HEK receptor

7 April 2017

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bcl-XL is the major bcl-x mRNA form expressed during murine development and its product localizes to mitochondria

7 April 2017

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The Bcl2 family: regulators of the cellular life-or-death switch

7 April 2017

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Apoptosis initiated by Bcl-2-regulated caspase activation independently of the cytochrome c/Apaf-1/caspase-9 apoptosome

7 April 2017

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BH3-only proteins that bind pro-survival Bcl-2 family members fail to induce apoptosis in the absence of Bax and Bak

28 September 2017

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Bax and Bak coalesce into novel mitochondria-associated clusters during apoptosis

28 September 2017

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BH3-Only proteins-essential initiators of apoptotic cell death

28 September 2017

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Influence of non-bonded parameters on the quality of NMR structures: a new force field for NMR structure calculation

28 September 2017

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Pro-apoptotic apoptosis protease-activating factor 1 (Apaf-1) has a cytoplasmic localization distinct from Bcl-2 or Bcl-x(L).

28 September 2017

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Bcl-2 family members do not inhibit apoptosis by binding the caspase activator Apaf-1

28 September 2017

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Apoptosis regulator bcl-w is essential for spermatogenesis but appears otherwise redundant

28 September 2017

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

28 September 2017

1 reference

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The bcl-2 candidate proto-oncogene product is a 24-kilodalton integral-membrane protein highly expressed in lymphoid cell lines and lymphomas carrying the t(14;18) translocation

28 September 2017

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=152889

The protein product of the oncogene bcl-2 is a component of the nuclear envelope, the endoplasmic reticulum, and the outer mitochondrial membrane.

28 September 2017

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=152889

Bcl-2 and porin follow different pathways of TOM-dependent insertion into the mitochondrial outer membrane

28 September 2017

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=152889

GXXXG and AXXXA: common alpha-helical interaction motifs in proteins, particularly in extremophiles

28 November 2018

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=152889

Statistical analysis of amino acid patterns in transmembrane helices: the GxxxG motif occurs frequently and in association with beta-branched residues at neighboring positions.

28 November 2018

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=152889

Study of the secondary structure of the C-terminal domain of the antiapoptotic protein bcl-2 and its interaction with model membranes

28 November 2018

1 reference

PubMed

https://pubmed.ncbi.nlm.nih.gov/12660157