Evidence map›Paper›PMID 28177155›Full record

ArticleJournal of bone and mineral research : the official journal of the American Society for Bone and Mineral Research2017

A Chaperone Complex Formed by HSP47, FKBP65, and BiP Modulates Telopeptide Lysyl Hydroxylation of Type I Procollagen.

Ivan Duran, Jorge H Martin, Mary Ann Weis, Pavel Krejci, Peter Konik, Bing Li, Yasemin Alanay, Caressa Lietman, Brendan Lee, David Eyre and 2 more

Open access · bronzeAbstract read
In one paragraph

Article in Journal of bone and mineral research : the official journal of the American Society for Bone and Mineral Research, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 38 papers.

0numbers the graph read from it
0cells of the map it votes in
38citing papers in PubMed
6.6field-weighted citation impact, top 3% of its field
1 · What the graph read from it

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.

2 · The registry

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.

3 · Its place in the literature

Who cites it

38 citing papers in PubMed, 73 citations in OpenAlex.

  1. Review
  2. Article
  3. Collagen IV biosynthesis: Intracellular choreography of post-translational modifications.Matrix biology : journal of the International Society for Matrix Biology · 2025
    Review
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  8. Loss of the long form of Plod2 phenocopies contractures of Bruck syndrome-osteogenesis imperfecta.Journal of bone and mineral research : the official journal of the American Society for Bone and Mineral Research · 2024
    Article
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4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

12 authors at 6 institutions in 4 countries.

Ivan DuranDepartment of Orthopaedic Surgery, David Geffen School of Medicine, University of California at Los Angeles, Los Angeles, CA, USA.
Jorge H MartinDepartment of Orthopaedic Surgery, David Geffen School of Medicine, University of California at Los Angeles, Los Angeles, CA, USA.
Mary Ann WeisDepartment of Orthopaedics and Sports Medicine, University of Washington, Seattle, WA, USA.
Pavel KrejciDepartment of Biology, Faculty of Medicine, Masaryk University, International Clinical Research Center, St. Anne's University Hospital, Brno, Czech Republic.
Peter KonikFaculty of Science, University of South Bohemia, Ceske Budejovice, Czech Republic.
Bing LiDepartment of Molecular, Cell, and Developmental Biology, University of California at Los Angeles, Los Angeles, CA, USA.
Yasemin AlanayPediatric Genetics Unit, Department of Pediatrics, Acibadem University School of Medicine, Istanbul, Turkey.
Caressa LietmanDepartment of Molecular and Human Genetics, Baylor College of Medicine, Houston, TX, USA.
Brendan LeeDepartment of Molecular and Human Genetics, Baylor College of Medicine, Houston, TX, USA.
David EyreDepartment of Orthopaedics and Sports Medicine, University of Washington, Seattle, WA, USA.
Daniel H CohnDepartment of Orthopaedic Surgery, David Geffen School of Medicine, University of California at Los Angeles, Los Angeles, CA, USA.
Deborah KrakowDepartment of Human Genetics, David Geffen School of Medicine, University of California at Los Angeles, Los Angeles, CA, USA.
University of California, Los Angeles · USBaylor College of Medicine · USUniversity of Washington · USAcıbadem University · TRSt. Anne's University Hospital Brno · CZUniversity of South Bohemia in České Budějovice · CZ

Funding

Tumor BiologyP30CA125123 · NCI · BAYLOR COLLEGE OF MEDICINE · PI DAVID R ROWLEY · 2007 to 2026
$73.9M
UNDERSTANDING FXTAS AMONG MALES WITH THE FMR1 PREMUTATIONP30HD024064 · NICHD · BAYLOR COLLEGE OF MEDICINE · PI TOLIAS, KIMBERLY R · 1988 to 2013
$29.4M
Virology CoreP30AI036211 · NIAID · BAYLOR COLLEGE OF MEDICINE · PI BUTEL, JANET S · 1994 to 2015
$21.7M
Project 3: Collagen post-translational modification and cross-linking in OIP01HD070394 · NICHD · BAYLOR COLLEGE OF MEDICINE · PI LEE, BRENDAN · 2011 to 2020
$13.4M
PROGRAM IN HUMAN MOLECULAR GENETICST32GM008307 · NIGMS · BAYLOR COLLEGE OF MEDICINE · PI SHAULSKY, GAD · 1990 to 2020
$6.6M
Collagen Cross-linking in Skeletal Aging and DiseaseR37AR037318 · NIAMS · UNIVERSITY OF WASHINGTON · PI EYRE, DAVID R · 2010 to 2019
$3.4M
Exome sequencing in the skeletal dysplasiasR01AR062651 · NIAMS · UNIVERSITY OF CALIFORNIA LOS ANGELES · PI COHN, DANIEL H · 2013 to 2017
$1.7M
BD Biosciences Special Order LSRIIS10RR024574 · NCRR · BAYLOR COLLEGE OF MEDICINE · PI LUMPKIN, ELLEN A · 2009 to 2009
$430k
The Role of FKBP10 in Recessive Osteogenesis ImperfectaF31DE022483 · NIDCR · BAYLOR COLLEGE OF MEDICINE · PI LIETMAN, CARESSA · 2011 to 2013
$129k
NCI NIH HHS P30 CA125123NCRR NIH HHS S10 RR024574NIAID NIH HHS P30 AI036211NIAMS NIH HHS R01 AR062651NIAMS NIH HHS R37 AR037318NICHD NIH HHS P01 HD070394NICHD NIH HHS P30 HD024064NIDCR NIH HHS F31 DE022483NIGMS NIH HHS T32 GM008307
6 · The paper itself

Abstract

Lysine hydroxylation of type I collagen telopeptides varies from tissue to tissue, and these distinct hydroxylation patterns modulate collagen cross-linking to generate a unique extracellular matrix. Abnormalities in these patterns contribute to pathologies that include osteogenesis imperfecta (OI), fibrosis, and cancer. Telopeptide procollagen modifications are carried out by lysyl hydroxylase 2 (LH2); however, little is known regarding how this enzyme regulates hydroxylation patterns. We identified an ER complex of resident chaperones that includes HSP47, FKBP65, and BiP regulating the activity of LH2. Our findings show that FKBP65 and HSP47 modulate the activity of LH2 to either favor or repress its activity. BiP was also identified as a member of the complex, playing a role in enhancing the formation of the complex. This newly identified ER chaperone complex contributes to our understanding of how LH2 regulates lysyl hydroxylation of type I collagen C-telopeptides to affect the quality of connective tissues. © 2017 American Society for Bone and Mineral Research.

Indexed as

AnimalsCell LineCollagen Type IEndoplasmic Reticulum Chaperone BiPEnzyme StabilityHeat-Shock ProteinsHSP47 Heat-Shock ProteinsHumansHydroxylationLysineMass SpectrometryMiceModels, BiologicalMultiprotein ComplexesMutationPeptidesCollagen Type Icollagen type I trimeric cross-linked peptideEndoplasmic Reticulum Chaperone BiPFKBP10 protein, humanHeat-Shock ProteinsHSP47 Heat-Shock ProteinsLysineMultiprotein ComplexesPeptidesProcollagenProcollagen-Lysine, 2-Oxoglutarate 5-DioxygenaseSERPINH1 protein, humanTacrolimus Binding Proteins

Identifiers

PMID28177155
PMCPMC5466459
OpenAlexW2587713374

What OpenQuestion holds

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Read underepoch 390

Registered trials

None linked

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.