ArticleMolecular and cellular biology1993
Cloning of the gene encoding peptide-binding protein 74 shows that it is a new member of the heat shock protein 70 family.
Article in Molecular and cellular biology, 1993. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 36 papers.
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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.
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Who cites it
36 citing papers in PubMed, 147 citations in OpenAlex.
- Review
- The Effect of Global Warming on Complex Disorders (Mental Disorders, Primary Hypertension, and Type 2 Diabetes).International journal of environmental research and public health · 2022Review
- Abrogating the Interaction Between p53 and Mortalin (Grp75/HSPA9/mtHsp70) for Cancer Therapy: The Story so far.Frontiers in cell and developmental biology · 2022Review
- Diversity in heat shock protein families: functional implications in virus infection with a comprehensive insight of their role in the HIV-1 life cycle.Cell stress & chaperones · 2021Review
- A Comprehensive Review of Alzheimer's Association with Related Proteins: Pathological Role and Therapeutic Significance.Current neuropharmacology · 2020Review
- The role of heat shock proteins and co-chaperones in heart failure.Philosophical transactions of the Royal Society of London. Series B, Biological sciences · 2018Review
- Mitochondrial Hsp70 and the troubles of nomenclature: leaving behind tradition to gain intuitiveness and clarity.Cell stress & chaperones · 2016Article
- Targeted heat shock protein 72 for pulmonary cytoprotection.Annals of the New York Academy of Sciences · 2016Review
- Intermediate filament protein accumulation in motor neurons derived from giant axonal neuropathy iPSCs rescued by restoration of gigaxonin.Human molecular genetics · 2015Article
- Article
- Monitoring charge flux to quantify unusual ligand-induced ion channel activity for use in biological nanopore-based sensors.Analytical chemistry · 2014Article
- Mortalin, apoptosis, and neurodegeneration.Biomolecules · 2012Article
- Secretion modification region-derived peptide disrupts HIV-1 Nef's interaction with mortalin and blocks virus and Nef exosome release.Journal of virology · 2012Article
- Multifaceted role of heat shock protein 70 in neurons.Molecular neurobiology · 2010Review
- NPM/ALK binds and phosphorylates the RNA/DNA-binding protein PSF in anaplastic large-cell lymphoma.Blood · 2007Article
- Identification and characterization of molecular interactions between mortalin/mtHsp70 and HSP60.The Biochemical journal · 2005Article
- Expression of heat shock proteins and heat shock protein messenger ribonucleic acid in human prostate carcinoma in vitro and in tumors in vivo.Cell stress & chaperones · 2005Article
- Cloning and sxpression of mitochondrial heat shock protein 70 of Trypanosoma congolense and potential use as a diagnostic antigen.Clinical and diagnostic laboratory immunology · 2003Article
- Lipid interaction differentiates the constitutive and stress-induced heat shock proteins Hsc70 and Hsp70.Cell stress & chaperones · 2002Article
- An Hsp70 family chaperone, mortalin/mthsp70/PBP74/Grp75: what, when, and where?Cell stress & chaperones · 2002Review
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Authors and funding
5 authors at 1 institution in 1 country.
Funding
Abstract
We have previously described peptide-binding proteins of 72 and 74 kDa (PBP72/74), which have been implicated as playing a role in antigen processing and are serologically related to the 70-kDa heat shock protein (hsp70) family. Here we report the cloning and sequencing of the cDNA encoding PBP74 in mice and in humans, accomplished by using amino acid sequence information obtained from the purified protein. We show that PBP74 is highly homologous to members of the hsp70 family but, significantly, is not identical to any known member of this family. Inspection of the cDNA nucleotide sequence indicates that it encodes a 46-residue N-terminal peptide which is not present in the mature protein. Transcription and translation in vitro of the PBP74 cDNA verified that it encodes a form of PBP74 which is larger than the mature protein. The presequence does not conform to known motifs for organelle-targeting sequences, and at present, its function is not known. By confocal microscopy, PBP74 was localized to cytoplasmic vesicles but not to the nucleus, mitochondria, or plasma membrane by using antibodies specific for the N-terminal 16 residues of PBP74. By RNA filter hybridization analysis, PBP74 mRNAs are detected in all cell types tested. Exposure of cells to heat shock does not result in an increase in the mRNA levels of PBP74, unlike the dramatic increase observed for the stress-inducible hsp70 mRNA. Thus, PBP74 appears to be a constitutive, new member of the hsp70 family.
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