Evidence map›Paper›PMID 31488542›Full record

ArticleThe Journal of biological chemistry2019

Exploring the molecular basis for substrate specificity in homologous macrolide biosynthetic cytochromes P450.

Matthew D DeMars, Nathan L Samora, Song Yang, Marc Garcia-Borràs, Jacob N Sanders, K N Houk, Larissa M Podust, David H Sherman

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 papers.

0numbers the graph read from it
0cells of the map it votes in
7citing papers in PubMed
0.9field-weighted citation impact, top 26% 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

7 citing papers in PubMed, 13 citations in OpenAlex.

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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

8 authors at 3 institutions in 1 country.

Matthew D DeMarsLife Sciences Institute, University of Michigan, Ann Arbor, Michigan 48109.ORCID 0000-0002-7268-5286
Nathan L SamoraSkaggs School of Pharmacy and Pharmaceutical Sciences, University of California, San Diego, California 92093.ORCID 0000-0003-4158-552X
Song YangDepartment of Chemistry and Biochemistry, University of California, Los Angeles, California 90095.
Marc Garcia-BorràsDepartment of Chemistry and Biochemistry, University of California, Los Angeles, California 90095.ORCID 0000-0001-9458-1114
Jacob N SandersDepartment of Chemistry and Biochemistry, University of California, Los Angeles, California 90095.
K N HoukDepartment of Chemistry and Biochemistry, University of California, Los Angeles, California 90095.ORCID 0000-0002-8387-5261
Larissa M PodustSkaggs School of Pharmacy and Pharmaceutical Sciences, University of California, San Diego, California 92093.ORCID 0000-0002-8537-8760
David H ShermanLife Sciences Institute, University of Michigan, Ann Arbor, Michigan 48109 davidhs@umich.edu.ORCID 0000-0001-8334-3647
University of California, Los Angeles · USUniversity of California San Diego · USUniversity of Michigan · US

Funding

Cellular Biotechnology Training Program (CBTP)T32GM008353 · NIGMS · UNIVERSITY OF MICHIGAN AT ANN ARBOR · PI SCHWENDEMAN, ANNA · 1991 to 2021
$9.3M
Discovery and Characterization of Natural Product Systems-Research Supplement to Promote DiversityR35GM118101 · NIGMS · UNIVERSITY OF MICHIGAN AT ANN ARBOR · PI SHERMAN, DAVID H · 2016 to 2025
$3.3M
Cellular Biotechnology Training Program (CBTP) - Years 31-35T32GM145304 · NIGMS · UNIVERSITY OF MICHIGAN AT ANN ARBOR · PI Guizhi Zhu · 2022 to 2026
$2.6M
NIGMS NIH HHS R35 GM118101NIGMS NIH HHS T32 GM008353NIGMS NIH HHS T32 GM145304
6 · The paper itself

Abstract

Cytochromes P450 (P450s) are nature's catalysts of choice for performing demanding and physiologically vital oxidation reactions. Biochemical characterization of these enzymes over the past decades has provided detailed mechanistic insight and highlighted the diversity of substrates P450s accommodate and the spectrum of oxidative transformations they catalyze. Previously, we discovered that the bacterial P450 MycCI from the mycinamicin biosynthetic pathway in

Indexed as

Amino Acid SubstitutionBacterial ProteinsBinding SitesCytochrome P-450 Enzyme SystemMolecular Dynamics SimulationProtein BindingStreptomycesSubstrate SpecificityTylosinBacterial ProteinsCytochrome P-450 Enzyme SystemTylosincytochrome P450enzyme structuremacrolide antibioticsmolecular dynamicsnatural product biosynthesisprotein chimeraStreptomycessubstrate specificity

Identifiers

PMID31488542
PMCPMC6827315
OpenAlexW2971810481

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.