Discover Community Create You

Loading publication...

Noodle always counts identifier-free feature events for service operation. With your permission, Google Analytics can also estimate audience and engagement. Search text, publication identifiers, cookies, IP addresses and browser fingerprints are never included in Noodle's first-party event counters.

Privacy details

Article

Subcellular localization and physiological consequences of introducing a mitochondrial matrix targeting signal sequence in bax and its mutants.

Experimental cell research - 15 Aug 2002

John George Babu, Anjum Rana, Khar Ashok, Nagaraj Ramakrishnan

Abstract excerpt

Bax, a proapoptotic member of the Bcl-2 family of proteins, resides in the cytosol and translocates to the mitochondrial membrane upon induction of apoptosis. It has been proposed that Bax does not translocate to mitochondria under normal physiological conditions, due to interaction between amino (ART) and carboxy (TM) terminal domains. Here, we report the physiological consequences of introducing a matrix...

Read the complete abstract on PubMed

Topics

Share this publication in a Topic to start or enrich a Post.

Share to bcl-2-Associated X Protein
Share to Cell Compartmentation

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to COS Cells

Share to Cytochrome c Group

Share to Intracellular Membranes

Share to Protein Sorting Signals

Share to Protein Transport

Share to Proto-Oncogene Proteins c-bcl-2

Source

Identifiers

PMID: 12169275
DOI: 10.1006/excr.2002.5586

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-07.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Subcellular localization and physiological consequences of introducing a mitochondrial matrix targeting signal sequence in bax and its mutants.PMID 12169275Read ↗

Conformation of the Bax C-terminus regulates subcellular location and cell death.Semantic proximity Read ↗

Translocation of a Bak C-terminus mutant from cytosol to mitochondria to mediate cytochrome C release: implications for Bak and Bax apoptotic function.Semantic proximity Read ↗

Bax forms multispanning monomers that oligomerize to permeabilize membranes during apoptosis.Semantic proximity Read ↗

The Bax carboxy-terminal hydrophobic helix does not determine organelle-specific targeting but is essential for maintaining Bax in an inactive state and for stable mitochondrial membrane insertion.Semantic proximity Read ↗

The N-terminal conformation of Bax regulates cell commitment to apoptosis.Semantic proximity Read ↗

Transmembrane pore formation by the carboxyl terminus of Bax protein.Semantic proximity Read ↗

The conformational stability of pro-apoptotic BAX is dictated by discrete residues of the protein core.Semantic proximity Read ↗

Involvement of the N-terminus of Bax in its intracellular localization and function.Semantic proximity Read ↗

Conformational rearrangements in the pro-apoptotic protein, Bax, as it inserts into mitochondria: a cellular death switch.Semantic proximity Read ↗

Stepwise activation of BAX and BAK by tBID, BIM, and PUMA initiates mitochondrial apoptosis.Semantic proximity Read ↗

Bcl-x(S) can form homodimers and heterodimers and its apoptotic activity requires localization of Bcl-x(S) to the mitochondria and its BH3 and loop domains.Semantic proximity Read ↗

Bax-induced cytochrome c release from mitochondria depends on alpha-helices-5 and -6.Semantic proximity Read ↗

⌁Select a neighboring publication to make it the new centre.