Evidence map›Paper›PMID 28844803›Full record

ArticleBioorganic & medicinal chemistry2017

Picomolar inhibition of β-galactosidase (bovine liver) attributed to loop closure.

Jessica B Pickens, Feng Wang, Susanne Striegler

Open access · greenAbstract read
In one paragraph

Article in Bioorganic & medicinal chemistry, 2017. 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
0.4field-weighted citation impact, top 44% 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

1 citing paper in PubMed, 7 citations in OpenAlex.

  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

3 authors at 1 institution in 1 country.

Jessica B PickensUniversity of Arkansas, Department of Chemistry and Biochemistry, 345N Campus Drive, Fayetteville, AR 72701, USA.
Feng WangUniversity of Arkansas, Department of Chemistry and Biochemistry, 345N Campus Drive, Fayetteville, AR 72701, USA.
Susanne StrieglerUniversity of Arkansas, Department of Chemistry and Biochemistry, 345N Campus Drive, Fayetteville, AR 72701, USA. Electronic address: susanne.striegler@uark.edu.
University of Arkansas at Fayetteville · US

Funding

Center for Protein Structure and FunctionP30GM103450 · NIGMS · UNIVERSITY OF ARKANSAS AT FAYETTEVILLE · PI MILLETT, FRANCIS S · 2012 to 2014
$3.2M
Efficient and Accurate Force Fields for Computer-Aided Drug DesignR01GM120578 · NIGMS · UNIVERSITY OF ARKANSAS AT FAYETTEVILLE · PI Feng Wang · 2017 to 2026
$1.9M
NIGMS NIH HHS P30 GM103450NIGMS NIH HHS R01 GM120578
6 · The paper itself

Abstract

In an effort to examine similarities in the active sites of glycosidases within the GH35 family, we performed a structure-activity-relationship study using our recently described library of galactonoamidines. The kinetic evaluation based on UV/Vis spectroscopy disclosed inhibition of β-galactosidase (bovine liver) in the picomolar concentration range indicating significantly higher inhibitor affinity than previously determined for β-galactosidase (A. oryzae). Possible alterations in the secondary protein structure or folding were excluded after further examination of the inhibitor binding using CD spectroscopy. Molecular dynamics studies suggested loop closing interactions as a rationale for the disparity of the active sites in the β-galactosidases under investigation.

Indexed as

AmidinesAnimalsbeta-GalactosidaseCattleDose-Response Relationship, DrugEnzyme InhibitorsLiverMolecular Dynamics SimulationMolecular StructureStructure-Activity RelationshipAmidinesbeta-GalactosidaseEnzyme InhibitorsAmidineCarbohydrateInhibitionβ-Galactosidase

Identifiers

PMID28844803
PMCPMC5632213
OpenAlexW2735019919

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.