Evidence map›Paper›PMID 23188794›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America2012

Single-molecule dissection of the high-affinity cohesin-dockerin complex.

Stefan W Stahl, Michael A Nash, Daniel B Fried, Michal Slutzki, Yoav Barak, Edward A Bayer, Hermann E Gaub

Open access · bronzeAbstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 53 papers.

0numbers the graph read from it
0cells of the map it votes in
53citing papers in PubMed
5.8field-weighted citation impact, top 3% 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

53 citing papers in PubMed, 137 citations in OpenAlex.

  1. Evolution of N-terminal mechanical lability as a determinant for Type III secretion.Protein science : a publication of the Protein Society · 2026
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  7. Mechanochemistry: Fundamental Principles and Applications.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2025
    Review
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  10. Structural Basis of High-Precision Protein Ligation and Its Application.Journal of the American Chemical Society · 2025
    Article
  11. Review
  12. Article
  13. Acoustic force spectroscopy reveals subtle differences in cellulose unbinding behavior of carbohydrate-binding modules.Proceedings of the National Academy of Sciences of the United States of America · 2022
    Article
  14. One-step asparaginyl endopeptidase (RSC chemical biology · 2022
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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

7 authors at 3 institutions in 2 countries.

Stefan W StahlLehrstuhl für Angewandte Physik, Center for NanoScience and Center for Integrative Protein Science, Ludwig-Maximilians-Universität, 80799 Munich, Germany.
Michael A Nash
Daniel B Fried
Michal Slutzki
Yoav Barak
Edward A Bayer
Hermann E Gaub
Ludwig-Maximilians-Universität München · DECenter for NanoScience · DEWeizmann Institute of Science · IL

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Cellulose-degrading enzyme systems are of significant interest from both a scientific and technological perspective due to the diversity of cellulase families, their unique assembly and substrate binding mechanisms, and their potential applications in several key industrial sectors, notably cellulose hydrolysis for second-generation biofuel production. Particularly fascinating are cellulosomes, the multimodular extracellular complexes produced by numerous anaerobic bacteria. Using single-molecule force spectroscopy, we analyzed the mechanical stability of the intermolecular interfaces between the cohesin and the dockerin modules responsible for self-assembly of the cellulosomal components into the multienzyme complex. The observed cohesin-dockerin rupture forces (>120 pN) are among the highest reported for a receptor-ligand system to date. Using an atomic force microscope protocol that quantified single-molecule binding activity, we observed force-induced dissociation of calcium ions from the duplicated loop-helix F-hand motif located within the dockerin module, which in the presence of EDTA resulted in loss of affinity to the cohesin partner. A cohesin amino acid mutation (D39A) that eliminated hydrogen bonding with the dockerin's critically conserved serine residues reduced the observed rupture forces. Consequently, no calcium loss occurred and dockerin activity was maintained throughout multiple forced dissociation events. These results offer insights at the single-molecule level into the stability and folding of an exquisite class of high-affinity protein-protein interactions that dictate fabrication and architecture of cellulose-degrading molecular machines.

Indexed as

Acetivibrio thermocellusAmino Acid SubstitutionBacterial ProteinsBiophysicsCalciumCell Cycle ProteinsChromosomal Proteins, Non-HistoneCohesinsCrystallography, X-RayHydrogen BondingMicroscopy, Atomic ForceModels, MolecularMultiprotein ComplexesMutagenesis, Site-DirectedProtein Interaction Domains and MotifsProtein MultimerizationBacterial ProteinsCalciumCell Cycle ProteinsChromosomal Proteins, Non-HistoneCohesinsMultiprotein ComplexesRecombinant Fusion Proteins

Identifiers

PMID23188794
PMCPMC3528535
OpenAlexW2140838214

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.