Evidence map›Paper›PMID 32250593›Full record

ArticleBiochemistry2020

Ndr/Lats Kinases Bind Specific Mob-Family Coactivators through a Conserved and Modular Interface.

Benjamin W Parker, Gergo Gogl, Mónika Bálint, Csaba Hetényi, Attila Reményi, Eric L Weiss

Open access · greenAbstract read
In one paragraph

Article in Biochemistry, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 6 papers.

0numbers the graph read from it
0cells of the map it votes in
6citing papers in PubMed
0.8field-weighted citation impact, top 33% 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

6 citing papers in PubMed, 9 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Article
  5. The STK38-XPO1 axis, a new actor in physiology and cancer.Cellular and molecular life sciences : CMLS · 2021
    Review
  6. Review
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

6 authors at 5 institutions in 3 countries.

Benjamin W ParkerDepartment of Biochemistry, University of Illinois Urbana-Champaign, Urbana, Illinois 61801, United States.ORCID 0000-0002-1464-1189
Gergo GoglInstitute of Organic Chemistry, Research Center for Natural Sciences, Magyar Tudósok körútja, 1117 Budapest, Hungary.
Mónika BálintDepartment of Pharmacology and Pharmacotherapy, Medical School, University of Pécs, Szigeti út 12, 7624 Pécs, Hungary.
Csaba HetényiDepartment of Pharmacology and Pharmacotherapy, Medical School, University of Pécs, Szigeti út 12, 7624 Pécs, Hungary.
Attila ReményiInstitute of Organic Chemistry, Research Center for Natural Sciences, Magyar Tudósok körútja, 1117 Budapest, Hungary.
Eric L WeissMolecular Biosciences, Northwestern University, Evanston, Illinois 60208, United States.
University of Pecs · HUCentre National de la Recherche Scientifique · FRInstitute of Organic Chemistry · HUNorthwestern University · USUniversity of Illinois Urbana-Champaign · US

Funding

Tumor Environment and Metastasis (TEAM) Research ProgramP30CA060553 · NCI · NORTHWESTERN UNIVERSITY AT CHICAGO · PI Daniela E Matei · 1993 to 2026
$153.9M
Control and function of the yeast RAM networkR01GM084223 · NIGMS · NORTHWESTERN UNIVERSITY · PI WEISS, ERIC LYLE · 2008 to 2017
$2.9M
Cytokinesis staging mechanismsR01GM137133 · NIGMS · NORTHWESTERN UNIVERSITY · PI WEISS, ERIC LYLE · 2020 to 2023
$1.6M
NCI NIH HHS P30 CA060553NIGMS NIH HHS R01 GM084223NIGMS NIH HHS R01 GM137133
6 · The paper itself

Abstract

Ndr/Lats kinases bind Mob coactivator proteins to form complexes that are essential and evolutionarily conserved components of "Hippo" signaling pathways, which control cell proliferation and morphogenesis in eukaryotes. All Ndr/Lats kinases have a characteristic N-terminal regulatory (NTR) region that binds a specific Mob cofactor: Lats kinases associate with Mob1 proteins, and Ndr kinases associate with Mob2 proteins. To better understand the significance of the association of Mob protein with Ndr/Lats kinases and selective binding of Ndr and Lats to distinct Mob cofactors, we determined crystal structures of

Indexed as

Conserved SequenceAmino Acid SequenceAnimalsHumansIntracellular Signaling Peptides and ProteinsModels, MolecularNerve Tissue ProteinsProtein BindingProtein ConformationProtein Serine-Threonine KinasesSaccharomyces cerevisiae ProteinsSubstrate SpecificityCBK1 protein, S cerevisiaeIntracellular Signaling Peptides and ProteinsMOB2 protein, humanNerve Tissue ProteinsProtein Serine-Threonine KinasesSaccharomyces cerevisiae Proteins

Identifiers

PMID32250593
PMCPMC8341033
OpenAlexW3014782306

What OpenQuestion holds

Textmetadata
LicenceTDM
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.