Evidence map›Paper›PMID 22898990›Full record

ArticleProtein science : a publication of the Protein Society2012

Bacterial collagen-binding domain targets undertwisted regions of collagen.

Sagaya Theresa Leena Philominathan, Takaki Koide, Osamu Matsushita, Joshua Sakon

Abstract read
In one paragraph

Article in Protein science : a publication of the Protein Society, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 19 papers.

0numbers the graph read from it
0cells of the map it votes in
19citing papers in PubMed
2.1field-weighted citation impact, top 13% 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

19 citing papers in PubMed, 27 citations in OpenAlex.

  1. Article
  2. Article
  3. Review
  4. Review
  5. Article
  6. Salivary esterases dramatically reduce biostability of dentin collagen treated with galloylated polyphenols.Dental materials : official publication of the Academy of Dental Materials · 2022
    Article
  7. Article
  8. Article
  9. Article
  10. Distinct effects of polyphenols and solvents on dentin collagen crosslinking interactions and biostability.Dental materials : official publication of the Academy of Dental Materials · 2021
    Article
  11. Article
  12. CaThe FEBS journal · 2018
    Article
  13. Article
  14. Article
  15. Article
  16. Article
  17. Article
  18. Interstitial collagen catabolism.The Journal of biological chemistry · 2013
    Review
  19. Article
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

4 authors at 4 institutions in 2 countries.

Sagaya Theresa Leena PhilominathanDepartment of Chemistry and Biochemistry, University of Arkansas, Fayetteville, Arkansas 72701, USA. pstleena@gmail.com
Takaki Koide
Osamu Matsushita
Joshua Sakon
Kitasato University · JPUniversity of Arkansas at Fayetteville · USUniversity of Arkansas System · USWaseda University · JP

Funding

VIRULENCE MECHANISMS IN ESCHERICHIA COLIP20RR016460 · NCRR · UNIV OF ARKANSAS FOR MED SCIS · PI HENSLEY, LORI · 2001 to 2011
$33.1M
Structure based drug discoveryP20RR015569 · NCRR · UNIVERSITY OF ARKANSAS AT FAYETTEVILLE · PI MILLETT, FRANCIS S · 2000 to 2009
$21.4M
Center for Protein Structure and FunctionP30GM103450 · NIGMS · UNIVERSITY OF ARKANSAS AT FAYETTEVILLE · PI MILLETT, FRANCIS S · 2012 to 2014
$3.2M
NCRR NIH HHS 1 P20RR15569NCRR NIH HHS P20RR16460NIGMS NIH HHS P30 GM103450
6 · The paper itself

Abstract

Clostridium histolyticum collagenase causes extensive degradation of collagen in connective tissue that results in gas gangrene. The C-terminal collagen-binding domain (CBD) of these enzymes is the minimal segment required to bind to a collagen fibril. CBD binds unidirectionally to the undertwisted C-terminus of triple helical collagen. Here, we examine whether CBD could also target undertwisted regions even in the middle of the triple helix. Collageneous peptides with an additional undertwisted region were synthesized by introducing a Gly → Ala substitution [(POG)(x) POA(POG)(y)]₃, where x + y = 9 and x > 3). ¹H-¹⁵N heteronuclear single quantum coherence nuclear magnetic resonance (HSQC NMR) titration studies with ¹⁵N-labeled CBD demonstrated that the minicollagen binds to a 10 Å wide 25 Å long cleft. Six collagenous peptides each labeled with a nitroxide radical were then titrated with ¹⁵N-labeled CBD. CBD binds to either the Gly → Ala substitution site or to the C-terminus of each minicollagen. Small-angle X-ray scattering measurements revealed that CBD prefers to bind the Gly → Ala site to the C-terminus. The HSQC NMR spectra of ¹⁵N-labeled minicollagen and minicollagen with undertwisted regions were unaffected by the titration of unlabeled CBD. The results imply that CBD binds to the undertwisted region of the minicollagen but does not actively unwind the triple helix.

Indexed as

Amino Acid SubstitutionBacterial ProteinsBinding SitesCollagenCollagenasesNitrogen IsotopesNuclear Magnetic Resonance, BiomolecularPeptidesProtein BindingProtein ConformationProtein Structure, TertiaryScattering, Small AngleX-Ray DiffractionBacterial ProteinsColH protein, Clostridium histolyticumCollagenCollagenasesNitrogen IsotopesPeptides

Identifiers

PMID22898990
PMCPMC3526996
OpenAlexW2132472454

What OpenQuestion holds

Textmetadata
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.