ArticleMolecular biology of the cell2007
A developmentally regulated chaperone complex for the endoplasmic reticulum of male haploid germ cells.
Article in Molecular biology of the cell, 2007. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 19 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.
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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.
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Who cites it
19 citing papers in PubMed, 42 citations in OpenAlex.
- Proteome-wide survey of the autoimmune target repertoire in autoimmune polyendocrine syndrome type 1.Scientific reports · 2016Trial
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- TMX4-driven LINC complex disassembly and asymmetric autophagy of the nuclear envelope upon acute ER stress.Nature communications · 2023Article
- Genome assembly of the Pendlebury's roundleaf bat, Hipposideros pendleburyi, revealed the expansion of Tc1/Mariner DNA transposons in Rhinolophoidea.DNA research : an international journal for rapid publication of reports on genes and genomes · 2022Article
- Chronic exercise training attenuates prostate cancer-induced molecular remodelling in the testis.Cellular oncology (Dordrecht, Netherlands) · 2021Article
- Article
- Crystal and solution structures of human protein-disulfide isomerase-like protein of the testis (PDILT) provide insight into its chaperone activity.The Journal of biological chemistry · 2018Article
- The control of male fertility by spermatid-specific factors: searching for contraceptive targets from spermatozoon's head to tail.Cell death & disease · 2016Review
- Expression, sorting, and segregation of Golgi proteins during germ cell differentiation in the testis.Molecular biology of the cell · 2015Article
- Structural insight into the dimerization of human protein disulfide isomerase.Protein science : a publication of the Protein Society · 2014Article
- Structure of the substrate-binding b' domain of the Protein Disulfide Isomerase-Like protein of the Testis.Scientific reports · 2014Article
- Stage-specific quantitative changes in renal and urinary proteome during the progression and development of streptozotocin-induced diabetic nephropathy in rats.Molecular and cellular biochemistry · 2014Article
- Linking spermatid ribonucleic acid (RNA) binding protein and retrogene diversity to reproductive success.Molecular & cellular proteomics : MCP · 2013Article
- The human protein disulfide isomerase gene family.Human genomics · 2012Article
- Protein disulfide isomerase homolog PDILT is required for quality control of sperm membrane protein ADAM3 and male fertility [corrected].Proceedings of the National Academy of Sciences of the United States of America · 2012Article
- Calsperin is a testis-specific chaperone required for sperm fertility.The Journal of biological chemistry · 2011Article
- The tissue-specific Rep8/UBXD6 tethers p97 to the endoplasmic reticulum membrane for degradation of misfolded proteins.PloS one · 2011Article
- Protein quality control in the early secretory pathway.The EMBO journal · 2008Review
- The effect of calnexin deletion on the expression level of binding protein (BiP) under heat stress conditions in Saccharomyces cerevisiae.Cellular & molecular biology letters · 2008Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
7 authors at 3 institutions in 2 countries.
Funding
Abstract
Glycoprotein folding is mediated by lectin-like chaperones and protein disulfide isomerases (PDIs) in the endoplasmic reticulum. Calnexin and the PDI homologue ERp57 work together to help fold nascent polypeptides with glycans located toward the N-terminus of a protein, whereas PDI and BiP may engage proteins that lack glycans or have sugars toward the C-terminus. In this study, we show that the PDI homologue PDILT is expressed exclusively in postmeiotic male germ cells, in contrast to the ubiquitous expression of many other PDI family members in the testis. PDILT is induced during puberty and represents the first example of a PDI family member under developmental control. We find that PDILT is not active as an oxido-reductase, but interacts with the model peptide Delta-somatostatin and nonnative bovine pancreatic trypsin inhibitor in vitro, indicative of chaperone activity. In vivo, PDILT forms a tissue-specific chaperone complex with the calnexin homologue calmegin. The identification of a redox-inactive chaperone partnership defines a new system of testis-specific protein folding with implications for male fertility.
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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.