Evidence map›Paper›PMID 36528062›Full record

ArticleThe Journal of biological chemistry2023

A solution structure analysis reveals a bent collagen triple helix in the complement activation recognition molecule mannan-binding lectin.

Hina Iqbal, Ka Wai Fung, Jayesh Gor, Anthony C Bishop, George I Makhatadze, Barbara Brodsky, Stephen J Perkins

Open access · goldAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 4 papers.

0numbers the graph read from it
0cells of the map it votes in
4citing papers in PubMed
0.6field-weighted citation impact, top 37% 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

4 citing papers in PubMed, 9 citations in OpenAlex.

  1. Gene sequencing andJournal of advanced veterinary and animal research · 2025
    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

7 authors at 3 institutions in 2 countries.

Hina IqbalDepartment of Structural and Molecular Biology, University College London, London, United Kingdom.
Ka Wai FungDepartment of Structural and Molecular Biology, University College London, London, United Kingdom.
Jayesh GorDepartment of Structural and Molecular Biology, University College London, London, United Kingdom.
Anthony C BishopCenter for Biotechnology and Interdisciplinary Studies, Rensselaer Polytechnic Institute, Troy, New York, USA.
George I MakhatadzeCenter for Biotechnology and Interdisciplinary Studies, Rensselaer Polytechnic Institute, Troy, New York, USA.
Barbara BrodskyDepartment of Biomedical Engineering, Science and Technology Center, Tufts University, Medford, Massachusetts, USA.
Stephen J PerkinsDepartment of Structural and Molecular Biology, University College London, London, United Kingdom. Electronic address: s.perkins@ucl.ac.uk.
Institute of Structural and Molecular Biology · GBRensselaer Polytechnic Institute · USTufts University · US

Funding

Stuctural studies of triple-helical proteinsR01GM060048 · NIGMS · UNIV OF MED/DENT NJ-R W JOHNSON MED SCH · PI BRODSKY, BARBARA M · 1999 to 2016
$5.1M
Medical Research Council MR/K011715/1NIGMS NIH HHS R01 GM060048
6 · The paper itself

Abstract

Collagen triple helices are critical in the function of mannan-binding lectin (MBL), an oligomeric recognition molecule in complement activation. The MBL collagen regions form complexes with the serine proteases MASP-1 and MASP-2 in order to activate complement, and mutations lead to common immunodeficiencies. To evaluate their structure-function properties, we studied the solution structures of four MBL-like collagen peptides. The thermal stability of the MBL collagen region was much reduced by the presence of a GQG interruption in the typical (X-Y-Gly)n repeat compared to controls. Experimental solution structural data were collected using analytical ultracentrifugation and small angle X-ray and neutron scattering. As controls, we included two standard Pro-Hyp-Gly collagen peptides (POG)

Indexed as

CollagenComplement ActivationMannose-Binding LectinCrystallography, X-RayMolecular Dynamics SimulationNeutron DiffractionPeptide FragmentsPliabilityProtein ConformationProtein StabilityScattering, Small AngleSolutionsStructure-Activity RelationshipUltracentrifugationCollagenMannose-Binding LectinPeptide FragmentsSolutionsanalytical ultracentrifugationatomistic modelingcollagencomplementmolecular dynamicssmall-angle neutron scatteringsmall-angle X-ray scattering

Identifiers

PMID36528062
PMCPMC9898670
OpenAlexW4311456158

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.