ReviewExperientia1994
Hsp70s and lysosomal proteolysis.
Review in Experientia, 1994. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers.
What it found
Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.
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
8 citing papers in PubMed, 43 citations in OpenAlex.
- Preferential secretion of inducible HSP70 by vitiligo melanocytes under stress.Pigment cell & melanoma research · 2014Article
- A central role for inducible heat-shock protein 70 in autoimmune vitiligo.Experimental dermatology · 2013Review
- Increased proteolysis of diphtheria toxin by human monocytes after heat shock: a subsidiary role for heat-shock protein 70 in antigen processing.Immunology · 2007Article
- Relationship between heat shock protein levels and infectivity in Trichinella spiralis larvae exposed to different stressors.Parasitology research · 2005Article
- Import into and degradation of cytosolic proteins by isolated yeast vacuoles.Molecular biology of the cell · 1999Article
- Processing of the DRB1*1103-restricted measles virus nucleoprotein determinant 185-199 in the endosomal compartment.Clinical and experimental immunology · 1998Article
- Autophagic proteolysis: control and specificity.The Histochemical journal · 1997Review
- Hsp70--a multi-gene, multi-structure, multi-function family with potential clinical applications.Experientia · 1994Review
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
Confluent cultured cells activate a lysosomal pathway of polypeptide breakdown in response to withdrawal of serum growth factors. The substrates for this proteolytic pathway are a restricted class of cytosolic polypeptides containing peptide sequences biochemically related to lysine-phenylalanine-glutamate-arginine-glutamine, or, in single amino acid abbreviations, KFERQ. The heat shock cognate protein of 73 kD (hsc73) binds to a variety of polypeptides via this molecular determinant and facilitates their lysosomal import and degradation. In addition, a portion of intracellular hsc73 resides within the lysosome and appears to be an essential component of the proteolytic machinery. Several potential mechanisms by which hsc73 mediates selective lysosomal import and degradation of polypeptides are discussed.
Indexed as
Identifiers
What OpenQuestion holds
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.