Evidence map›Paper›PMID 32306515›Full record

ArticleProtein science : a publication of the Protein Society2020

Comparison of metal-bound and unbound structures of aminopeptidase B proteins from Escherichia coli and Yersinia pestis.

George Minasov, Matthew R Lam, Monica Rosas-Lemus, Joanna Sławek, Magdalena Woinska, Ivan G Shabalin, Ludmilla Shuvalova, Bernhard Ø Palsson, Adam Godzik, Wladek Minor and 1 more

Open access · bronzeAbstract read
PubMed Full text at PMC Publisher
In one paragraph

Article in Protein science : a publication of the Protein Society, 2020. 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
0.1field-weighted citation impact, top 57% 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, 4 citations in OpenAlex.

  1. Article
  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

11 authors at 3 institutions in 1 country.

George MinasovDepartment of Microbiology-Immunology, Feinberg School of Medicine, Northwestern University, Chicago, Illinois, USA.
Matthew R LamDepartment of Molecular Biosciences, Weinberg School of Arts and Sciences, Northwestern University, Evanston, Illinois, USA.
Monica Rosas-LemusDepartment of Microbiology-Immunology, Feinberg School of Medicine, Northwestern University, Chicago, Illinois, USA.
Joanna SławekCenter for Structural Genomics of Infectious Diseases, Northwestern University, Chicago, Illinois, USA.
Magdalena WoinskaCenter for Structural Genomics of Infectious Diseases, Northwestern University, Chicago, Illinois, USA.
Ivan G ShabalinCenter for Structural Genomics of Infectious Diseases, Northwestern University, Chicago, Illinois, USA.
Ludmilla ShuvalovaDepartment of Microbiology-Immunology, Feinberg School of Medicine, Northwestern University, Chicago, Illinois, USA.
Bernhard Ø PalssonDepartment of Bioengineering and Pediatrics, University of California, San Diego, California, USA.
Adam GodzikCenter for Structural Genomics of Infectious Diseases, Northwestern University, Chicago, Illinois, USA.
Wladek MinorCenter for Structural Genomics of Infectious Diseases, Northwestern University, Chicago, Illinois, USA.
Karla J F SatchellDepartment of Microbiology-Immunology, Feinberg School of Medicine, Northwestern University, Chicago, Illinois, USA.ORCID 0000-0003-3274-7611
Northwestern University · USUniversity of California, Riverside · USUniversity of California San Diego · US

Funding

Systems Biology Approach to Redefine Susceptibility Testing and Treatment of MDR Pathogens in the Context of Host ImmunityU01AI124316 · NIAID · UNIVERSITY OF CALIFORNIA, SAN DIEGO · PI PALSSON, BERNHARD O · 2016 to 2020
$10.2M
NIAID NIH HHS HHSN272201200026CNIAID NIH HHS HHSN272201700060CNIAID NIH HHS U01 AI124316NIAID NIH HHS U01AI124316
6 · The paper itself

Abstract

Protein degradation by aminopeptidases is involved in bacterial responses to stress. Escherichia coli produces two metal-dependent M17 family leucine aminopeptidases (LAPs), aminopeptidase A (PepA) and aminopeptidase B (PepB). Several structures have been solved for PepA as well as other bacterial M17 peptidases. Herein, we report the first structures of a PepB M17 peptidase. The E. coli PepB protein structure was determined at a resolution of 2.05 and 2.6 Å. One structure has both Zn

Indexed as

AminopeptidasesCrystallography, X-RayEscherichia coliEscherichia coli ProteinsManganeseProtein DomainsYersinia pestisZincAminopeptidasesEscherichia coli ProteinsManganeseZincaminopeptidaseEscherichia colihexamermetalloproteasePepBX-ray crystallographyYersinia pestis

Identifiers

PMID32306515
PMCPMC7314395
OpenAlexW3016583921

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.