Evidence map›Paper›PMID 20939100›Full record

ArticleProteins2010

Computational modeling of laminin N-terminal domains using sparse distance constraints from disulfide bonds and chemical cross-linking.

Stefan Kalkhof, Sebastian Haehn, Mats Paulsson, Neil Smyth, Jens Meiler, Andrea Sinz

Abstract read
In one paragraph

Article in Proteins, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 17 papers.

0numbers the graph read from it
0cells of the map it votes in
17citing papers in PubMed
–field-weighted citation impact
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

17 citing papers in PubMed.

  1. Article
  2. Article
  3. Article
  4. Novel Concepts of MS-Cleavable Cross-linkers for Improved Peptide Structure Analysis.Journal of the American Society for Mass Spectrometry · 2017
    Article
  5. Article
  6. Article
  7. Automated assignment of MS/MS cleavable cross-links in protein 3D-structure analysis.Journal of the American Society for Mass Spectrometry · 2015
    Article
  8. Article
  9. Article
  10. Article
  11. Article
  12. Article
  13. StavroX--a software for analyzing crosslinked products in protein interaction studies.Journal of the American Society for Mass Spectrometry · 2012
    Article
  14. Article
  15. Article
  16. Article
  17. 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

6 authors.

Stefan KalkhofDepartment of Pharmaceutical Chemistry and Bioanalytics, Institute of Pharmacy, Martin Luther University Halle-Wittenberg, Halle (Saale), Germany.
Sebastian Haehn
Mats Paulsson
Neil Smyth
Jens Meiler
Andrea Sinz

Funding

Membrane Protein Structure Elucidation from sparse NMR data (KAMP)R01GM080403 · NIGMS · VANDERBILT UNIVERSITY · PI MEILER, JENS · 2007 to 2019
$3.0M
NIGMS NIH HHS R01 GM080403
6 · The paper itself

Abstract

Basement membranes are thin extracellular protein layers, which separate endothelial and epithelial cells from the underlying connecting tissue. The main noncollagenous components of basement membranes are laminins, trimeric glycoproteins, which form polymeric networks by interactions of their N-terminal (LN) domains; however, no high-resolution structure of laminin LN domains exists so far. To construct models for laminin β(1) and γ(1) LN domains, 14 potentially suited template structures were determined using fold recognition methods. For each target/template-combination comparative models were created with Rosetta. Final models were selected based on their agreement with experimentally obtained distance constraints from natural cross-links, that is, disulfide bonds as well as chemical cross-links obtained from reactions with two amine-reactive cross-linkers. We predict that laminin β(1) and γ(1) LN domains share the galactose-binding domain-like fold.

Indexed as

Models, MolecularAmino Acid SequenceAnimalsComputational BiologyCross-Linking ReagentsDisulfidesHumansLamininMiceMolecular Sequence DataProtein Structure, TertiaryRecombinant ProteinsReproducibility of ResultsSequence Analysis, ProteinSpectrometry, Mass, Matrix-Assisted Laser Desorption-IonizationTemplates, GeneticCross-Linking ReagentsDisulfidesLamininRecombinant Proteins

Identifiers

PMID20939100
PMCPMC5079110

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Registered trials

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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.