Evidence map›Paper›PMID 21620686›Full record

ArticleMatrix biology : journal of the International Society for Matrix Biology2011

Molecular simulations predict novel collagen conformations during cross-link loading.

Jonathan W Bourne, Peter A Torzilli

Abstract read
In one paragraph

Article in Matrix biology : journal of the International Society for Matrix Biology, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.

0numbers the graph read from it
0cells of the map it votes in
12citing papers in PubMed
1.0field-weighted citation impact, top 25% 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

12 citing papers in PubMed, 23 citations in OpenAlex.

  1. Article
  2. Article
  3. Molecular and structural basis of actin filament severing by ADF/cofilin.Computational and structural biotechnology journal · 2022
    Article
  4. Article
  5. Collagen peptide simulated bending after applied axial deformation.Journal of the mechanical behavior of biomedical materials · 2020
    Article
  6. Article
  7. Tension in fibrils suppresses their enzymatic degradation - A molecular mechanism for 'use it or lose it'.Matrix biology : journal of the International Society for Matrix Biology · 2020
    Review
  8. Non-enzymatic cross-linking of collagen type II fibrils is tuned via osmolality switch.Journal of orthopaedic research : official publication of the Orthopaedic Research Society · 2018
    Article
  9. Article
  10. Article
  11. Glycation cross-linking induced mechanical-enzymatic cleavage of microscale tendon fibers.Matrix biology : journal of the International Society for Matrix Biology · 2014
    Article
  12. 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

2 authors at 1 institution in 1 country.

Jonathan W BournePhysiology, Biophysics & Systems Biology Program, Weill Graduate School of Medical Sciences, Cornell University, 1300 York Avenue, New York, NY 10065, USA. BourneJ@HSS.EDU
Peter A Torzilli
Cornell University · US

Funding

CARTILAGE CELL AND MATRIX RESPONSE TO JOINT LOADINGR01AR045748 · NIAMS · HOSPITAL FOR SPECIAL SURGERY · PI TORZILLI, PETER A · 1998 to 2008
$2.4M
Clinical and Translational Science Center (TL1)TL1RR024998 · NCRR · WEILL MEDICAL COLL OF CORNELL UNIV · PI IMPERATO-MCGINLEY, JULIANNE L · 2007 to 2011
$695k
Clinical and Translational Science CenterTL1TR000459 · NCATS · WEILL MEDICAL COLL OF CORNELL UNIV · PI IMPERATO-MCGINLEY, JULIANNE L · 2012 to 2016
$451k
DEFORMATION-DEPENDENT ENZYME CLEAVAGE OF COLLAGENR21AR051636 · NIAMS · HOSPITAL FOR SPECIAL SURGERY · PI TORZILLI, PETER · 2004 to 2005
$170k
EXTRAMURAL RESEARCH FACILITIES CONSTRUCTIONC06RR012538 · NCRR · HOSPITAL FOR SPECIAL SURGERY · PI BOSKEY, ADELE L · 1997 to 1997
–
NCATS NIH HHS TL1 TR000459NCRR NIH HHS C06 RR012538NCRR NIH HHS C06-RR12538-01NCRR NIH HHS TL1 RR024998NCRR NIH HHS TL1RR024998NIAMS NIH HHS R01 AR045748NIAMS NIH HHS R01AR45748NIAMS NIH HHS R21 AR051636NIAMS NIH HHS R21AR051636
6 · The paper itself

Abstract

Collagen cross-linking mechanically strengthens tissues during development and aging, but there is limited data describing how force transmitted across cross-links affects molecular conformation. We used Steered Molecular Dynamics (SMD) to model perpendicular force through a side chain. Results predicted that collagen peptides have negligible bending resistance and that mechanical force causes helix disruption below covalent bond failure strength, suggesting alternative molecular conformations precede cross-link rupture and macroscopic damage during mechanical loading.

Indexed as

Molecular Dynamics SimulationArginineCollagenCross-Linking ReagentsElasticityMechanical PhenomenaModels, ChemicalPeptidesProlineProtein ConformationTensile StrengthArginineCollagenCross-Linking ReagentsPeptidesProline

Identifiers

PMID21620686
PMCPMC3148790
OpenAlexW2017787658

What OpenQuestion holds

Textmetadata
LicenceTDM
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.