Evidence map›Paper›PMID 32545195›Full record

ArticleInternational journal of molecular sciences2020

Ultrastructural Location and Interactions of the Immunoglobulin Receptor Binding Sequence within Fibrillar Type I Collagen.

Jie Zhu, Rama S Madhurapantula, Aruna Kalyanasundaram, Tanya Sabharwal, Olga Antipova, Sandra W Bishnoi, Joseph P R O Orgel

Open access · goldAbstract read
In one paragraph

Article in International journal of molecular sciences, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.

0numbers the graph read from it
0cells of the map it votes in
10citing papers in PubMed
0.8field-weighted citation impact, top 33% 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

10 citing papers in PubMed, 17 citations in OpenAlex.

  1. Review
  2. Article
  3. Review
  4. Molecular Tissue Responses to Mechanical Loading.International journal of molecular sciences · 2022
    Article
  5. Review
  6. Review
  7. Review
  8. Review
  9. Review
  10. Review
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

7 authors at 2 institutions in 2 countries.

Jie ZhuInstitute of Biophysics, College of science, Northwest A&F University, Yangling 712100, China.
Rama S MadhurapantulaDepartment of Biology, Illinois Institute of Technology, Chicago, IL 60616, USA.ORCID 0000-0001-9477-9171
Aruna KalyanasundaramDepartment of Biology, Illinois Institute of Technology, Chicago, IL 60616, USA.
Tanya SabharwalDepartment of Biology, Illinois Institute of Technology, Chicago, IL 60616, USA.
Olga AntipovaDepartment of Biology, Illinois Institute of Technology, Chicago, IL 60616, USA.
Sandra W BishnoiDepartment of Chemistry, Illinois Institute of Technology, Chicago, IL 60616, USA.
Joseph P R O OrgelDepartment of Biology, Illinois Institute of Technology, Chicago, IL 60616, USA.ORCID 0000-0002-1050-9391
Illinois Institute of Technology · USArgonne National Laboratory · US

Funding

Time resolved SAXS studies on the RP2/Arl3 complex pp.484-485P41GM103622 · NIGMS · ILLINOIS INSTITUTE OF TECHNOLOGY · PI IRVING, THOMAS C · 2012 to 2020
$11.9M
Development and Research Center of Sichuan Cuisine, Sichuan Provincial Department of Education CC18Z16Fundamental Research Funds for the Central Universities 2452019074National Institute of General Medical Sciences of the National Institutes of Health 9 P41 GM103622U.S. Department of Energy (DOE) Office of Science User Facility DE-AC02-06CH11357
6 · The paper itself

Abstract

Collagen type I is a major constituent of animal bodies. It is found in large quantities in tendon, bone, skin, cartilage, blood vessels, bronchi, and the lung interstitium. It is also produced and accumulates in large amounts in response to certain inflammations such as lung fibrosis. Our understanding of the molecular organization of fibrillar collagen and cellular interaction motifs, such as those involved with immune-associated molecules, continues to be refined. In this study, antibodies raised against type I collagen were used to label intact D-periodic type I collagen fibrils and observed with atomic force microscopy (AFM), and X-ray diffraction (XRD) and immunolabeling positions were observed with both methods. The antibodies bind close to the C-terminal telopeptide which verifies the location and accessibility of both the major histocompatibility complex (MHC) class I (MHCI) binding domain and C-terminal telopeptide on the outside of the collagen fibril. The close proximity of the C-telopeptide and the MHC1 domain of type I collagen to fibronectin, discoidin domain receptor (DDR), and collagenase cleavage domains likely facilitate the interaction of ligands and receptors related to cellular immunity and the collagen-based Extracellular Matrix.

Indexed as

AnimalsBinding SitesCollagen Type IDiscoidin Domain Receptor 1Elastic ModulusFourier AnalysisGoldImmunoglobulinsMicroscopy, Atomic ForcePeptidesRats, WistarReceptors, ImmunologicScattering, Small AngleX-Ray DiffractionCollagen Type Icollagen type I trimeric cross-linked peptideDDR1 protein, humanDiscoidin Domain Receptor 1GoldImmunoglobulinsPeptidesReceptors, Immunologicatomic force microscopycollagenimmunogold labelinglung diseaseMHC class Inanomechanical propertiesX-ray diffraction

Identifiers

PMID32545195
PMCPMC7312686
OpenAlexW3034845009

What OpenQuestion holds

Textmetadata
LicenceCC BY
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.