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

Deletion mutational analysis of BMRP, a pro-apoptotic protein that binds to Bcl-2.

Molecular and cellular biochemistry - 1 May 2011

Malladi Srinivas, Parsa Kishore V L, Bhupathi Deepthi, Rodríguez-González María A, Conde Juan A, Anumula Pallavi, Romo Hannah E, Claunch Cheryl J, Ballestero Rafael P, González-García Maribel

Abstract excerpt

Bcl-2 is an anti-apoptotic member of the Bcl-2 family of proteins that protects cells from apoptosis induced by a large variety of stimuli. The protein BMRP (MRPL41) was identified as a Bcl-2 binding partner and shown to have pro-apoptotic activity. We have performed deletion mutational analyses to identify the domain(s) of Bcl-2 and BMRP that are involved in the Bcl-2/BMRP interaction, and the region(s) of BMRP...

Read the complete abstract on PubMed

Topics

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

Share to Apoptosis
Share to Blotting, Western

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Mitochondrial Proteins

Share to NIH 3T3 Cells

Share to Proto-Oncogene Proteins c-bcl-2

Share to Ribosomal Proteins

Share to Sequence Deletion

Share to Two-Hybrid System Techniques

Source

Identifiers

PMID: 21253851
DOI: 10.1007/s11010-011-0729-1

Genes

MRPL41

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

Deletion mutational analysis of BMRP, a pro-apoptotic protein that binds to Bcl-2.PMID 21253851Read ↗

Identification of a novel regulatory domain in Bcl-X(L) and Bcl-2.Semantic proximity Read ↗

Role of Bcl-2 family members on apoptosis: what we have learned from knock-out miceSemantic proximity Read ↗

Biological properties of the BCL-2 family protein BCL-RAMBO, which regulates apoptosis, mitochondrial fragmentation, and mitophagySemantic proximity Read ↗

Cell death regulation by B-cell lymphoma protein.Semantic proximity Read ↗

Bcl2's flexible loop domain regulates p53 binding and survival.Semantic proximity Read ↗

The Human Bcl-2 Family Member Bcl-rambo Localizes to Mitochondria and Induces Apoptosis and Morphological Aberrations in Drosophila.Semantic proximity Read ↗

Characterization of the anti-apoptotic mechanism of Bcl-B.Semantic proximity Read ↗

The human Bcl-2 family member Bcl-rambo and voltage-dependent anion channels manifest a genetic interaction in Drosophila and cooperatively promote the activation of effector caspases in human cultured cellsSemantic proximity Read ↗

Functional dissection of the human Bcl2 protein: sequence requirements for inhibition of apoptosis.Semantic proximity Read ↗

Conversion of Bcl-2 to a Bax-like death effector by caspases.Semantic proximity Read ↗

Inhibitors of the anti-apoptotic Bcl-2 proteins: a patent reviewSemantic proximity Read ↗

Modulation of cell death in yeast by the Bcl-2 family of proteins.Semantic proximity Read ↗

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