ReviewCell stress & chaperones2006
Activities of the cochaperones Hap46/BAG-1M and Hap50/BAG-1L and isoforms.
Review in Cell stress & chaperones, 2006. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 2 papers.
What it found
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
The trial behind it
Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.
Who cites it
2 citing papers in PubMed, 8 citations in OpenAlex.
- Interactome analysis of Bag-1 isoforms reveals novel interaction partners in endoplasmic reticulum-associated degradation.PloS one · 2021Article
- Multiple, but concerted cellular activities of the human protein Hap46/BAG-1M and isoforms.International journal of molecular sciences · 2009Review
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
1 author at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Since their discovery about a decade ago, human Hap46/BAG-1M, the larger isoform Hap50/BAG-1L, and related structures have caused quite some astonishment because of the seemingly unlimited array of possible interaction partners belonging to completely unrelated protein families. This problem was partially resolved when it was realized that molecular chaperones of the heat shock protein family Hsp70 are major primary association partners, which in turn, are able to bind a wide variety of unrelated protein structures, thus forming ternary complexes. Moreover, the protein folding activity of Hsp70 chaperones is affected; hence, the designation "cochaperones." Although many different proteins require mediation by Hsp70 chaperones for interactions with Hap50/BAG-1L, Hap46/BAG-1M, and isoforms, several other partner proteins are able to associate directly. In addition, Hap46/BAG-1M and Hap50/BAG-1L are also able to interact with DNA by making use of a positively charged region close to the amino terminal end of the polypeptide chain. This is the molecular basis for their effects on transcriptional activities, which are emphasized in this review and for which a molecular model is presented.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.