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

Structural analysis of BAG1 cochaperone and its interactions with Hsc70 heat shock protein.

Nature structural biology - 1 Apr 2001

Briknarová K, Takayama S, Brive L, Havert M L, Knee D A, Velasco J, Homma S, Cabezas E, Stuart J, Hoyt D W, Satterthwait A C, Llinás M, Reed J C, Ely K R

Abstract excerpt

BAG-family proteins share a conserved protein interaction region, called the 'BAG domain', which binds and regulates Hsp70/Hsc70 molecular chaperones. This family of cochaperones functionally regulates signal transducing proteins and transcription factors important for cell stress responses, apop...

Read the complete abstract on PubMed

Topics

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

Share to Adenosine Triphosphatases
Share to COS Cells
Share to HSC70 Heat-Shock Proteins

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to HSP70 Heat-Shock Proteins

Share to Nuclear Magnetic Resonance, Biomolecular

Share to Qa-SNARE Proteins

Share to Receptors, Androgen

Share to Transcriptional Activation

Source

Identifiers

PMID: 11276257
DOI: 10.1038/86236

Genes

BAG1

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 4 Sept 2026. Prepared record publication-11276257-2026-09-04.2. Manifest publication-graph-cohort-2026-09-04.2.

Source receipt: PubMed via Helena Literature Corpus, retrieved 4 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Structural analysis of BAG1 cochaperone and its interactions with Hsc70 heat shock protein.PMID 11276257Read ↗

Short peptides derived from the BAG-1 C-terminus inhibit the interaction between BAG-1 and HSC70 and decrease breast cancer cell growth.Semantic proximity Read ↗

The Role of Non-Canonical Hsp70s (Hsp110/Grp170) in CancerSemantic proximity Read ↗

Bag1 Functions In Vivo as a Negative Regulator of Hsp70 Chaperone ActivitySemantic proximity Read ↗

BAG-1 prevents stress-induced long-term growth inhibition in breast cancer cells via a chaperone-dependent pathway.Semantic proximity Read ↗

Origin and Evolution of the Human Bcl2-Associated Athanogene-1 (BAG-1).Semantic proximity Read ↗

BAG-1 diversely affects steroid receptor activity.Semantic proximity Read ↗

Caught in the middle: the role of Bag3 in disease.Semantic proximity Read ↗

Characterization of the Relationship between the Chaperone and Lipid-Binding Functions of the 70-kDa Heat-Shock Protein, HspA1A.Semantic proximity Read ↗

Phosphorylation-State Modulated Binding of HSP70: Structural Insights and Compensatory Protein EngineeringSemantic proximity Read ↗

Data-driven large-scale genomic analysis reveals an intricate phylogenetic and functional landscape in J-domain proteinsSemantic proximity Read ↗

Insight into residues involved in the structure and function of the breast cancer associated protein human gamma synuclein.Semantic proximity Read ↗

Bag1 is essential for differentiation and survival of hematopoietic and neuronal cells.Semantic proximity Read ↗

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