Evidence map›Paper›PMID 18547527›Full record

ArticleStructure (London, England : 1993)2008

Integrin conformational regulation: uncoupling extension/tail separation from changes in the head region by a multiresolution approach.

Mattia Rocco, Camillo Rosano, John W Weisel, David A Horita, Roy R Hantgan

Open access · bronzeAbstract read
In one paragraph

Article in Structure (London, England : 1993), 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 23 papers.

0numbers the graph read from it
0cells of the map it votes in
23citing papers in PubMed
3.0field-weighted citation impact, top 9% 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

23 citing papers in PubMed, 35 citations in OpenAlex.

  1. Article
  2. Review
  3. Article
  4. Review
  5. Article
  6. Article
  7. Article
  8. PROBINGNano LIFE · 2013
    Article
  9. Article
  10. Multiscale simulations suggest a mechanism for integrin inside-out activation.Proceedings of the National Academy of Sciences of the United States of America · 2011
    Article
  11. Integrin structure, activation, and interactions.Cold Spring Harbor perspectives in biology · 2011
    Review
  12. Article
  13. Article
  14. Article
  15. Article
  16. Focal adhesions are sites of integrin extension.The Journal of cell biology · 2010
    Article
  17. Article
  18. Article
  19. Article
  20. 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

5 authors at 3 institutions in 2 countries.

Mattia RoccoS.S. Biopolimeri e Proteomica, Istituto Nazionale per la Ricerca sul Cancro, IST c/o CBA, Genoa, Italy. mattia.rocco@istge.it
Camillo Rosano
John W Weisel
David A Horita
Roy R Hantgan
Alleanza Contro il Cancro · ITWake Forest University · USUniversity of Pennsylvania · US

Funding

STRUCTURAL STUDIES OF BLOOD CLOTTING PROTEINSR01HL030954 · NHLBI · UNIVERSITY OF PENNSYLVANIA · PI WEISEL, JOHN W · 1985 to 2008
$3.0M
NHLBI NIH HHS HL 30954NHLBI NIH HHS R01 HL030954
6 · The paper itself

Abstract

Integrin-dependent adhesion and signaling are regulated by conformational changes whose details remain controversial. Crystallography revealed bent shapes for resting and primed integrin ectodomains, whereas large, ligand-induced rearrangements in other constructs suggested extension, "opening," and tail separation. We have used experimental/computed hydrodynamics to discriminate among different alpha(v)beta(3) and alpha(IIb)beta(3) atomic models built on X-ray, NMR, and EM data. In contrast with X-ray structures and EM maps, hydrodynamics indicate that resting integrins are already extended. Furthermore, the hydrodynamics of an alpha(v)beta(3) ectodomain-fibronectin fragment complex support opening via additional head region conformational changes (hybrid domain swing-out), but without tail separation. Likewise, frictional changes induced by priming agents in full-length alpha(IIb)beta(3) correlate well with the swing-out coupled to a simple transmembrane helix shift in an extended, electron tomography-based model. Extension and immediate tail separation are then uncoupled from head region rearrangements following activation, thus underscoring integrins' delicate, finely tuned plasticity.

Indexed as

Models, MolecularCrystallography, X-RayFibronectinsIntegrin alphaVbeta3Intercellular Signaling Peptides and ProteinsNuclear Magnetic Resonance, BiomolecularPeptidesPlatelet Glycoprotein GPIIb-IIIa ComplexProtein BindingProtein Structure, TertiaryWaterechistatinFibronectinsIntegrin alphaVbeta3Intercellular Signaling Peptides and ProteinsPeptidesPlatelet Glycoprotein GPIIb-IIIa ComplexWater

Identifiers

PMID18547527
PMCPMC2848535
OpenAlexW1966781861

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.