Evidence map›Paper›PMID 36215467›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America2022

Acoustic force spectroscopy reveals subtle differences in cellulose unbinding behavior of carbohydrate-binding modules.

Markus Hackl, Edward V Contrada, Jonathan E Ash, Atharv Kulkarni, Jinho Yoon, Hyeon-Yeol Cho, Ki-Bum Lee, John M Yarbrough, Cesar A López, Sandrasegaram Gnanakaran and 1 more

Open access · greenAbstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 3 papers.

0numbers the graph read from it
0cells of the map it votes in
3citing papers in PubMed
0.5field-weighted citation impact, top 41% 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

3 citing papers in PubMed, 7 citations in OpenAlex.

  1. Review
  2. Review
  3. 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

11 authors at 3 institutions in 1 country.

Markus HacklDepartment of Chemical and Biochemical Engineering, Rutgers, The State University of New Jersey, Piscataway, NJ 08854.ORCID 0000-0003-2004-7351
Edward V ContradaDepartment of Chemical and Biochemical Engineering, Rutgers, The State University of New Jersey, Piscataway, NJ 08854.ORCID 0000-0001-8323-4045
Jonathan E AshDepartment of Chemical and Biochemical Engineering, Rutgers, The State University of New Jersey, Piscataway, NJ 08854.ORCID 0000-0003-4878-592X
Atharv KulkarniDepartment of Chemical and Biochemical Engineering, Rutgers, The State University of New Jersey, Piscataway, NJ 08854.
Jinho YoonDepartment of Chemistry and Chemical Biology, Rutgers, The State University of New Jersey, Piscataway, NJ 08854.
Hyeon-Yeol ChoDepartment of Chemistry and Chemical Biology, Rutgers, The State University of New Jersey, Piscataway, NJ 08854.ORCID 0000-0003-1897-1166
Ki-Bum LeeDepartment of Chemistry and Chemical Biology, Rutgers, The State University of New Jersey, Piscataway, NJ 08854.ORCID 0000-0002-8164-0047
John M YarbroughBiosciences Center, National Renewable Energy Laboratory, Golden, CO 80401.ORCID 0000-0001-6921-4208
Cesar A LópezTheoretical Division, Los Alamos National Laboratory, Los Alamos, NM 87545.
Sandrasegaram GnanakaranTheoretical Division, Los Alamos National Laboratory, Los Alamos, NM 87545.ORCID 0000-0002-9368-3044
Shishir P S ChundawatDepartment of Chemical and Biochemical Engineering, Rutgers, The State University of New Jersey, Piscataway, NJ 08854.ORCID 0000-0003-3677-6735
Rutgers, The State University of New Jersey · USLos Alamos National Laboratory · USNational Laboratory of the Rockies · US

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Protein adsorption to solid carbohydrate interfaces is critical to many biological processes, particularly in biomass deconstruction. To engineer more-efficient enzymes for biomass deconstruction into sugars, it is necessary to characterize the complex protein-carbohydrate interfacial interactions. A carbohydrate-binding module (CBM) is often associated with microbial surface-tethered cellulosomes or secreted cellulase enzymes to enhance substrate accessibility. However, it is not well known how CBMs recognize, bind, and dissociate from polysaccharides to facilitate efficient cellulolytic activity, due to the lack of mechanistic understanding and a suitable toolkit to study CBM-substrate interactions. Our work outlines a general approach to study the unbinding behavior of CBMs from polysaccharide surfaces using a highly multiplexed single-molecule force spectroscopy assay. Here, we apply acoustic force spectroscopy (AFS) to probe a

Indexed as

Acetivibrio thermocellusCellulaseAcousticsBacterial ProteinsCarbohydratesCelluloseSpectrum AnalysisSugarsBacterial ProteinsCarbohydratesCellulaseCelluloseSugarsacoustic force spectroscopybiofuelscarbohydrate-binding modulenanocellulosesingle-molecule force spectroscopy

Identifiers

PMID36215467
PMCPMC9586272
OpenAlexW4304099182

What Socratic holds

Textmetadata
LicenceCC BY-NC-ND
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 Socratic graph.