Evidence map›Paper›PMID 30429330›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America2018

Dynamic interactions of type I cohesin modules fine-tune the structure of the cellulosome of

Anders Barth, Jelle Hendrix, Daniel Fried, Yoav Barak, Edward A Bayer, Don C Lamb

Open access · greenAbstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 14 papers.

0numbers the graph read from it
0cells of the map it votes in
14citing papers in PubMed
1.8field-weighted citation impact, top 16% 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

14 citing papers in PubMed, 38 citations in OpenAlex.

  1. Review
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  4. The Onset of Molecule-Spanning Dynamics in Heat Shock Protein Hsp90.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2023
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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

6 authors at 2 institutions in 2 countries.

Anders BarthPhysical Chemistry, Department of Chemistry, Ludwig-Maximilians-Universität München, 81377 Munich, Germany.ORCID 0000-0003-3671-3072
Jelle HendrixPhysical Chemistry, Department of Chemistry, Ludwig-Maximilians-Universität München, 81377 Munich, Germany.ORCID 0000-0001-5731-1297
Daniel FriedDepartment of Biomolecular Sciences, The Weizmann Institute of Science, Rehovot 7610001, Israel.
Yoav BarakDepartment of Biomolecular Sciences, The Weizmann Institute of Science, Rehovot 7610001, Israel.
Edward A BayerDepartment of Biomolecular Sciences, The Weizmann Institute of Science, Rehovot 7610001, Israel.
Don C LambPhysical Chemistry, Department of Chemistry, Ludwig-Maximilians-Universität München, 81377 Munich, Germany; d.lamb@lmu.de.ORCID 0000-0002-0232-1903
Center for Integrated Protein Science Munich · DEWeizmann Institute of Science · IL

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Efficient degradation of plant cell walls by selected anaerobic bacteria is performed by large extracellular multienzyme complexes termed cellulosomes. The spatial arrangement within the cellulosome is organized by a protein called scaffoldin, which recruits the cellulolytic subunits through interactions between cohesin modules on the scaffoldin and dockerin modules on the enzymes. Although many structural studies of the individual components of cellulosomal scaffoldins have been performed, the role of interactions between individual cohesin modules and the flexible linker regions between them are still not entirely understood. Here, we report single-molecule measurements using FRET to study the conformational dynamics of a bimodular cohesin segment of the scaffoldin protein CipA of

Indexed as

Acetivibrio thermocellusBacterial ProteinsCell Cycle ProteinsCellulosomesChromosomal Proteins, Non-HistoneCohesinsFluorescence Resonance Energy TransferMembrane ProteinsProtein BindingBacterial ProteinsCell Cycle ProteinsChromosomal Proteins, Non-HistoneCipA protein, ClostridiumCohesinsMembrane Proteinsconformational dynamicsfluorescenceFRETmolecular dynamicssingle molecule

Identifiers

PMID30429330
PMCPMC6275499
OpenAlexW2804544930

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.