Evidence map›Paper›PMID 25387007›Full record

ArticlePloS one2014

Analysis of nidogen-1/laminin γ1 interaction by cross-linking, mass spectrometry, and computational modeling reveals multiple binding modes.

Philip Lössl, Knut Kölbel, Dirk Tänzler, David Nannemann, Christian H Ihling, Manuel V Keller, Marian Schneider, Frank Zaucke, Jens Meiler, Andrea Sinz

Open access · goldAbstract read
In one paragraph

Article in PloS one, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 30 papers.

0numbers the graph read from it
0cells of the map it votes in
30citing papers in PubMed
3.2field-weighted citation impact, top 8% 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

30 citing papers in PubMed, 50 citations in OpenAlex.

  1. Review
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  5. Shape shifting: The multiple conformational substates of the PTEN N-terminal PIPProtein science : a publication of the Protein Society · 2022
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  6. Protein Structure Prediction with Mass Spectrometry Data.Annual review of physical chemistry · 2022
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  13. Biological Applications for LC-MS-Based Proteomics.Advances in experimental medicine and biology · 2021
    Article
  14. Review
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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

10 authors at 3 institutions in 2 countries.

Philip LösslDepartment of Pharmaceutical Chemistry and Bioanalytics, Institute of Pharmacy, Martin Luther University Halle-Wittenberg, Halle (Saale), Germany.
Knut KölbelDepartment of Pharmaceutical Chemistry and Bioanalytics, Institute of Pharmacy, Martin Luther University Halle-Wittenberg, Halle (Saale), Germany.
Dirk TänzlerDepartment of Pharmaceutical Chemistry and Bioanalytics, Institute of Pharmacy, Martin Luther University Halle-Wittenberg, Halle (Saale), Germany.
David NannemannDepartment of Chemistry and Center for Structural Biology, Vanderbilt University, Nashville, TN, United States of America.
Christian H IhlingDepartment of Pharmaceutical Chemistry and Bioanalytics, Institute of Pharmacy, Martin Luther University Halle-Wittenberg, Halle (Saale), Germany.
Manuel V KellerCenter for Biochemistry, Medical Faculty, University of Cologne, Cologne, Germany.
Marian SchneiderResearch Group Artificial Binding Proteins, Institute of Biochemistry and Biotechnology, Martin Luther University Halle-Wittenberg, Halle (Saale), Germany.
Frank ZauckeCenter for Biochemistry, Medical Faculty, University of Cologne, Cologne, Germany.
Jens MeilerDepartment of Chemistry and Center for Structural Biology, Vanderbilt University, Nashville, TN, United States of America.
Andrea SinzDepartment of Pharmaceutical Chemistry and Bioanalytics, Institute of Pharmacy, Martin Luther University Halle-Wittenberg, Halle (Saale), Germany.
Martin Luther University Halle-Wittenberg · DEUniversity of Cologne · DEVanderbilt University · US

Funding

Membrane Protein Structure Elucidation from sparse NMR data (KAMP)R01GM080403 · NIGMS · VANDERBILT UNIVERSITY · PI MEILER, JENS · 2007 to 2019
$3.0M
Cheminformatics of Allosteric mGluR Modulation promotes Therapeutic DevelopmentR01MH090192 · NIMH · VANDERBILT UNIVERSITY · PI MEILER, JENS · 2010 to 2013
$1.5M
Computational Design of Protein-Ligand Interfaces - a Therapeutic StrategyR01GM099842 · NIGMS · VANDERBILT UNIVERSITY · PI MEILER, JENS · 2012 to 2015
$1.3M
Small Molecule Probes to Investigate Structure and Function of Y ReceptorsR01DK097376 · NIDDK · VANDERBILT UNIVERSITY · PI MEILER, JENS, WEAVER, C DAVID · 2013 to 2015
$1.0M
NIDDK NIH HHS R01 DK097376NIGMS NIH HHS R01 GM080403NIGMS NIH HHS R01 GM099842NIMH NIH HHS R01 MH090192
6 · The paper itself

Abstract

We describe the detailed structural investigation of nidogen-1/laminin γ1 complexes using full-length nidogen-1 and a number of laminin γ1 variants. The interactions of nidogen-1 with laminin variants γ1 LEb2-4, γ1 LEb2-4 N836D, γ1 short arm, and γ1 short arm N836D were investigated by applying a combination of (photo-)chemical cross-linking, high-resolution mass spectrometry, and computational modeling. In addition, surface plasmon resonance and ELISA studies were used to determine kinetic constants of the nidogen-1/laminin γ1 interaction. Two complementary cross-linking strategies were pursued to analyze solution structures of laminin γ1 variants and nidogen-1. The majority of distance information was obtained with the homobifunctional amine-reactive cross-linker bis(sulfosuccinimidyl)glutarate. In a second approach, UV-induced cross-linking was performed after incorporation of the diazirine-containing unnatural amino acids photo-leucine and photo-methionine into laminin γ1 LEb2-4, laminin γ1 short arm, and nidogen-1. Our results indicate that Asn-836 within laminin γ1 LEb3 domain is not essential for complex formation. Cross-links between laminin γ1 short arm and nidogen-1 were found in all protein regions, evidencing several additional contact regions apart from the known interaction site. Computational modeling based on the cross-linking constraints indicates the existence of a conformational ensemble of both the individual proteins and the nidogen-1/laminin γ1 complex. This finding implies different modes of interaction resulting in several distinct protein-protein interfaces.

Indexed as

AnimalsCross-Linking ReagentsHEK293 CellsHumansKineticsLamininMembrane GlycoproteinsMiceModels, MolecularProtein Structure, TertiarySurface Plasmon ResonanceTandem Mass SpectrometryCross-Linking ReagentsLamininlaminin gamma 1Membrane Glycoproteinsnidogen

Identifiers

PMID25387007
PMCPMC4227867
OpenAlexW2073879953

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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.