Evidence map›Paper›PMID 37931179›Full record

ArticleThe journal of physical chemistry. B2023

Catalytic Mechanism of Collagen Hydrolysis by Zinc(II)-Dependent Matrix Metalloproteinase-1.

Ann Varghese, Sodiq O Waheed, Koteswararao Gorantla, Isabella DiCastri, Ciara LaRouche, Brendan Kaski, Gregg B Fields, Tatyana G Karabencheva-Christova

Open access · greenAbstract read
In one paragraph

Article in The journal of physical chemistry. B, 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 2 papers.

0numbers the graph read from it
0cells of the map it votes in
2citing papers in PubMed
2.6field-weighted citation impact, top 10% 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

2 citing papers in PubMed, 11 citations in OpenAlex.

  1. Transitioning enzyme catalysis towards photocatalysis.Philosophical transactions. Series A, Mathematical, physical, and engineering sciences · 2025
    Review
  2. 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

8 authors at 2 institutions in 1 country.

Ann VargheseDepartment of Chemistry, Michigan Technological University, Houghton, Michigan 49931, United States.
Sodiq O WaheedDepartment of Chemistry, Michigan Technological University, Houghton, Michigan 49931, United States.ORCID 0000-0003-3422-4531
Koteswararao GorantlaDepartment of Chemistry, Michigan Technological University, Houghton, Michigan 49931, United States.ORCID 0000-0003-4541-8796
Isabella DiCastriDepartment of Chemical Engineering, Michigan Technological University, Houghton, Michigan 49931, United States.
Ciara LaRoucheDepartment of Chemical Engineering, Michigan Technological University, Houghton, Michigan 49931, United States.
Brendan KaskiDepartment of Kinesiology and Integrative Physiology, Michigan Technological University, Houghton, Michigan 49931, United States.
Gregg B FieldsDepartment of Chemistry and Biochemistry and I-HEALTH, Florida Atlantic University, Jupiter, Florida 33458, United States.
Tatyana G Karabencheva-ChristovaDepartment of Chemistry, Michigan Technological University, Houghton, Michigan 49931, United States.ORCID 0000-0001-8629-4377
Michigan Technological University · USFlorida Atlantic University · US

Funding

Insights into Structure-Function Relationships of Matrix Metalloproteinase-1 from Computational and Experimental StudiesR15GM132873 · NIGMS · MICHIGAN TECHNOLOGICAL UNIVERSITY · PI KARABENCHEVA-CHRISTOVA, TATYANA · 2020 to 2023
$867k
NIGMS NIH HHS R15 GM132873
6 · The paper itself

Abstract

Human matrix metalloproteinase-1 (MMP-1) is a zinc(II)-dependent enzyme that catalyzes collagenolysis. Despite the availability of extensive experimental data, the mechanism of MMP-1-catalyzed collagenolysis remains poorly understood due to the lack of experimental structure of a catalytically productive enzyme-substrate complex of MMP-1. In this study, we apply molecular dynamics and combined quantum mechanics/molecular mechanics to reveal the reaction mechanism of MMP-1 based on a computationally modeled structure of the catalytically competent complex of MMP-1 that contains a large triple-helical peptide substrate. Our proposed mechanism involves the participation of an auxiliary (second) water molecule (wat

Indexed as

Matrix Metalloproteinase 1ZincCatalysisCollagenHumansHydrolysisMolecular Dynamics SimulationProtonsWaterCollagenMatrix Metalloproteinase 1ProtonsWaterZinc

Identifiers

PMID37931179
PMCPMC10659029
OpenAlexW4388406663

What OpenQuestion 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 OpenQuestion graph.