ArticleThe EMBO journal1996
A microsomal ATP-binding protein involved in efficient protein transport into the mammalian endoplasmic reticulum.
Article in The EMBO journal, 1996. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 41 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
41 citing papers in PubMed, 128 citations in OpenAlex.
- Rules of Engagement for Components of Membrane Protein Biogenesis at the Human Endoplasmic Reticulum.International journal of molecular sciences · 2025Review
- Toward Understanding the Mechanism of Client-Selective Small Molecule Inhibitors of the Sec61 Translocon.Journal of molecular recognition : JMR · 2025Review
- Quantitative Mass Spectrometry Characterizes Client Spectra of Components for Targeting of Membrane Proteins to and Their Insertion into the Membrane of the Human ER.International journal of molecular sciences · 2023Review
- AMPylation and Endoplasmic Reticulum Protein Folding Homeostasis.Cold Spring Harbor perspectives in biology · 2023Review
- Signal Peptide Features Determining the Substrate Specificities of Targeting and Translocation Components in Human ER Protein Import.Frontiers in physiology · 2022Review
- Complexity and Specificity of Sec61-Channelopathies: Human Diseases Affecting Gating of the Sec61 Complex.Cells · 2021Review
- Role of the HSP70 Co-Chaperone SIL1 in Health and Disease.International journal of molecular sciences · 2021Review
- Calcium depletion challenges endoplasmic reticulum proteostasis by destabilising BiP-substrate complexes.eLife · 2020Article
- Understanding the mammalian TRAP complex function(s).Open biology · 2020Review
- Immunological Significance of HMGB1 Post-Translational Modification and Redox Biology.Frontiers in immunology · 2020Review
- The enigmatic ATP supply of the endoplasmic reticulum.Biological reviews of the Cambridge Philosophical Society · 2019Review
- Inhibitors of protein translocation across membranes of the secretory pathway: novel antimicrobial and anticancer agents.Cellular and molecular life sciences : CMLS · 2018Review
- The ribosome quality control pathway can access nascent polypeptides stalled at the Sec61 translocon.Molecular biology of the cell · 2015Article
- BiP and its nucleotide exchange factors Grp170 and Sil1: mechanisms of action and biological functions.Journal of molecular biology · 2015Review
- BiP clustering facilitates protein folding in the endoplasmic reticulum.PLoS computational biology · 2014Article
- The Endoplasmic Reticulum Chaperone GRP170: From Immunobiology to Cancer Therapeutics.Frontiers in oncology · 2014Review
- Orchestration of secretory protein folding by ER chaperones.Biochimica et biophysica acta · 2013Review
- High molecular weight stress proteins: Identification, cloning and utilisation in cancer immunotherapy.International journal of hyperthermia : the official journal of European Society for Hyperthermic Oncology, North American Hyperthermia Group · 2013Review
- A multifunctional chimeric chaperone serves as a novel immune modulator inducing therapeutic antitumor immunity.Cancer research · 2013Article
- BiP-mediated closing of the Sec61 channel limits Ca2+ leakage from the ER.The EMBO journal · 2012Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
10 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Protein transport into the mammalian endoplasmic reticulum depends on nucleoside triphosphates. Photoaffinity labelling of microsomes with azido-ATP prevents protein transport at the level of association of precursor proteins with the components of the transport machinery, Sec61alpha and TRAM proteins. The same phenotype of inactivation was observed after depleting a microsomal detergent extract of ATP-binding proteins by passage through ATP-agarose and subsequent reconstitution of the pass-through into proteoliposomes. Transport was restored by co-reconstitution of the ATP eluate. This eluate showed eight distinct bands in SDS gels. We identified five lumenal proteins (Grp170, Grp94, BiP/Grp78, calreticulin and protein disulfide isomerase), one membrane protein (ribophorin I) and two ribosomal proteins (L4 and L5). In addition to BiP (Grp78), Grp170 was most efficiently retained on ATP-agarose. Purified BiP did not stimulate transport activity. Sequence analysis revealed a striking similarity of Grp170 and the yeast microsomal protein Lhs1p which was recently shown to be involved in protein transport into yeast microsomes. We suggest that Grp170 mediates efficient insertion of polypeptides into the microsomal membrane at the expense of nucleoside triphosphates.
Indexed as
Identifiers
9003769PMC452519W1807523145What 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.