Evidence map›Paper›PMID 37700555›Full record

ArticleProteins2024

Rate limiting step of the allosteric activation of the bacterial adhesin FimH investigated by molecular dynamics simulations.

Gianluca Interlandi

Abstract read
PubMed Full text at PMC Publisher
In one paragraph

Article in Proteins, 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 1 paper.

0numbers the graph read from it
0cells of the map it votes in
1citing 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

1 citing paper in PubMed.

  1. 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

1 author.

Gianluca InterlandiDepartment of Bioengineering, University of Washington, Seattle, Washington, USA.ORCID 0000-0001-5445-9587

Funding

Dynamic Properties of Bacterial AdhesionsR01AI050940 · NIAID · UNIVERSITY OF WASHINGTON · PI SOKURENKO, EVGENI VENIAMINOVIC · 2002 to 2011
$4.7M
Allosteric adhesins of enterobacterial pathogensR01AI171570 · NIAID · UNIVERSITY OF WASHINGTON · PI Rachel E Klevit, EVGENI Veniaminovic SOKURENKO · 2022 to 2026
$3.5M
Conformational dynamics of adhesive bondsR01AI119675 · NIAID · UNIVERSITY OF WASHINGTON · PI SOKURENKO, EVGENI VENIAMINOVIC, THOMAS, WENDY E · 2016 to 2020
$2.9M
Differential targeting of von Willebrand factor depending on oxidizing conditionsR01HL153253 · NHLBI · UNIVERSITY OF WASHINGTON · PI INTERLANDI, GIANLUCA · 2021 to 2024
$1.6M
NHLBI NIH HHS R01 HL153253NHLBI NIH HHS R01HL153253NIAID NIH HHS R01 AI050940NIAID NIH HHS R01 AI119675NIAID NIH HHS R01 AI171570
6 · The paper itself

Abstract

The bacterial adhesin FimH is a model for the study of protein allostery because its structure has been resolved in multiple configurations, including the active and the inactive state. FimH consists of a pilin domain (PD) that anchors it to the rest of the fimbria and an allosterically regulated lectin domain (LD) that binds mannose on the surface of infected cells. Under normal conditions, the two domains are docked to each other and LD binds mannose weakly. However, in the presence of tensile force generated by shear the domains separate and conformational changes propagate across LD resulting in a stronger bond to mannose. Recently, the crystallographic structure of a variant of FimH has been resolved, called

Indexed as

MannoseMolecular Dynamics SimulationAdhesins, Escherichia coliAllosteric RegulationEscherichia coliFimbriae ProteinsLectinsAdhesins, Escherichia coliFimbriae ProteinsLectinsMannoseallosteric regulationbacterial adhesionbiophysicsFimH adhesinfree energy profileJarzynski equalitypulling simulations

Identifiers

PMID37700555
PMCPMC10873117

What OpenQuestion holds

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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.