Evidence map›Paper›PMID 33231438›Full record

ArticleBiochemistry2020

Binding of a Soluble

Yossef López de Los Santos, David N Bernard, Philippe Egesborg, Myriam Létourneau, Clara Lafortune, Matthew J Cuneo, Agathe Urvoas, David Chatenet, Jean-Pierre Mahy, Yves St-Pierre and 2 more

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 4 papers.

0numbers the graph read from it
0cells of the map it votes in
4citing papers in PubMed
0.3field-weighted citation impact, top 42% 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

4 citing papers in PubMed, 6 citations in OpenAlex.

  1. Article
  2. Article
  3. Review
  4. 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

12 authors at 3 institutions in 3 countries.

Yossef López de Los SantosCentre Armand-Frappier Santé Biotechnologie, Institut national de la recherche scientifique (INRS), Université du Québec, Laval, QC H7V 1B7, Canada.
David N BernardCentre Armand-Frappier Santé Biotechnologie, Institut national de la recherche scientifique (INRS), Université du Québec, Laval, QC H7V 1B7, Canada.
Philippe EgesborgCentre Armand-Frappier Santé Biotechnologie, Institut national de la recherche scientifique (INRS), Université du Québec, Laval, QC H7V 1B7, Canada.
Myriam LétourneauCentre Armand-Frappier Santé Biotechnologie, Institut national de la recherche scientifique (INRS), Université du Québec, Laval, QC H7V 1B7, Canada.
Clara LafortuneCentre Armand-Frappier Santé Biotechnologie, Institut national de la recherche scientifique (INRS), Université du Québec, Laval, QC H7V 1B7, Canada.
Matthew J CuneoDepartment of Structural Biology, St. Jude Children's Research Hospital, Memphis, Tennessee 38105, United States.ORCID 0000-0002-1475-6656
Agathe UrvoasInstitut de biologie intégrative de la cellule (I2BC), CNRS, Université Paris-Saclay, 91190 Orsay, France.
David ChatenetCentre Armand-Frappier Santé Biotechnologie, Institut national de la recherche scientifique (INRS), Université du Québec, Laval, QC H7V 1B7, Canada.ORCID 0000-0002-7270-4328
Jean-Pierre MahyLaboratoire de chimie bioorganique et bioinorganique, Institut de chimie moléculaire et des matériaux d'Orsay (ICMMO), CNRS, Université Paris-Saclay, 91190 Orsay, France.ORCID 0000-0001-6502-7923
Yves St-PierreCentre Armand-Frappier Santé Biotechnologie, Institut national de la recherche scientifique (INRS), Université du Québec, Laval, QC H7V 1B7, Canada.
Rémy RicouxLaboratoire de chimie bioorganique et bioinorganique, Institut de chimie moléculaire et des matériaux d'Orsay (ICMMO), CNRS, Université Paris-Saclay, 91190 Orsay, France.ORCID 0000-0002-3464-7895
Nicolas DoucetCentre Armand-Frappier Santé Biotechnologie, Institut national de la recherche scientifique (INRS), Université du Québec, Laval, QC H7V 1B7, Canada.ORCID 0000-0002-1952-9380
Institut National de la Recherche Scientifique · CACentre National de la Recherche Scientifique · FRSt. Jude Children's Research Hospital · US

Funding

Conformational sub-states in enzyme catalysis: Applications to ribonucleaseR01GM105978 · NIGMS · UNIVERSITY OF PITTSBURGH AT PITTSBURGH · PI AGARWAL, PRATUL K, CHENNUBHOTLA, SRINIVAS CHAKRA · 2014 to 2018
$2.8M
NIGMS NIH HHS R01 GM105978
6 · The paper itself

Abstract

The selective targeting of protein-protein interactions remains a significant determinant for the proper modulation and regulation of cell apoptosis. Prototypic galectins such as human galectin-7 (GAL-7) are characterized by their ability to form homodimers that control the molecular fate of a cell by mediating subtle yet critical glycan-dependent interactions between pro- and anti-apoptotic molecular partners. Altering the structural architecture of GAL-7 can therefore result in resistance to apoptosis in various human cancer cells, further illustrating its importance in cell survival. In this study, we used a combination of biophysical and cellular assays to illustrate that binding of a water-soluble

Indexed as

ApoptosisBinding SitesGalectinsHumansIn Vitro TechniquesJurkat CellsMesoporphyrinsMolecular Docking SimulationNuclear Magnetic Resonance, BiomolecularProtein BindingProtein Interaction Domains and MotifsProtein MultimerizationProtein Structure, QuaternaryRecombinant ProteinsScattering, Small AngleSolubilityGalectinsLGALS7 protein, humanMesoporphyrinsRecombinant Proteins

Identifiers

PMID33231438
PMCPMC7890795
OpenAlexW3108141885

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.