Evidence map›Paper›PMID 27642006›Full record

ArticleScientific reports2016

Full-length model of the human galectin-4 and insights into dynamics of inter-domain communication.

Joane K Rustiguel, Ricardo O S Soares, Steve P Meisburger, Katherine M Davis, Kristina L Malzbender, Nozomi Ando, Marcelo Dias-Baruffi, Maria Cristina Nonato

Open access · goldAbstract read
In one paragraph

Article in Scientific reports, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 14 papers.

0numbers the graph read from it
0cells of the map it votes in
14citing papers in PubMed
0.5field-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

14 citing papers in PubMed, 24 citations in OpenAlex.

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  13. Exploring functional pairing between surface glycoconjugates and human galectins using programmable glycodendrimersomes.Proceedings of the National Academy of Sciences of the United States of America · 2018
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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 2 institutions in 2 countries.

Joane K RustiguelLaboratório de Cristalografia de Proteínas, Faculdade de Ciências Farmacêuticas de Ribeirão Preto, Universidade de São Paulo, SP, Brazil.
Ricardo O S SoaresLaboratório de Cristalografia de Proteínas, Faculdade de Ciências Farmacêuticas de Ribeirão Preto, Universidade de São Paulo, SP, Brazil.
Steve P MeisburgerDepartment of Chemistry, Princeton University, Princeton, NJ, USA.
Katherine M DavisDepartment of Chemistry, Princeton University, Princeton, NJ, USA.
Kristina L MalzbenderDepartment of Chemistry, Princeton University, Princeton, NJ, USA.
Nozomi AndoDepartment of Chemistry, Princeton University, Princeton, NJ, USA.
Marcelo Dias-BaruffiDepartamento de Análises Clínicas, Toxicológicas e Bromatológicas, Faculdade de Ciências Farmacêuticas de Ribeirão Preto, Universidade de São Paulo, SP, Brazil.
Maria Cristina NonatoLaboratório de Cristalografia de Proteínas, Faculdade de Ciências Farmacêuticas de Ribeirão Preto, Universidade de São Paulo, SP, Brazil.
Princeton University · USUniversidade de São Paulo · BR

Funding

Overall (pp. 40-62)P41GM103485 · NIGMS · CORNELL UNIVERSITY · PI CERIONE, RICHARD A. · 2012 to 2018
$15.5M
Structural Characterizations of Transient and Heterogeneous Protein ComplexesR00GM100008 · NIGMS · PRINCETON UNIVERSITY · PI ANDO, NOZOMI · 2014 to 2016
$747k
Structural Characterizations of Transient and Heterogeneous Protein ComplexesK99GM100008 · NIGMS · MASSACHUSETTS INSTITUTE OF TECHNOLOGY · PI ANDO, NOZOMI · 2012 to 2013
$176k
NIGMS NIH HHS K99 GM100008NIGMS NIH HHS P41 GM103485NIGMS NIH HHS R00 GM100008
6 · The paper itself

Abstract

Galectins are proteins involved in diverse cellular contexts due to their capacity to decipher and respond to the information encoded by β-galactoside sugars. In particular, human galectin-4, normally expressed in the healthy gastrointestinal tract, displays differential expression in cancerous tissues and is considered a potential drug target for liver and lung cancer. Galectin-4 is a tandem-repeat galectin characterized by two carbohydrate recognition domains connected by a linker-peptide. Despite their relevance to cell function and pathogenesis, structural characterization of full-length tandem-repeat galectins has remained elusive. Here, we investigate galectin-4 using X-ray crystallography, small- and wide-angle X-ray scattering, molecular modelling, molecular dynamics simulations, and differential scanning fluorimetry assays and describe for the first time a structural model for human galectin-4. Our results provide insight into the structural role of the linker-peptide and shed light on the dynamic characteristics of the mechanism of carbohydrate recognition among tandem-repeat galectins.

Indexed as

Models, MolecularProtein Interaction Domains and MotifsAmino Acid SequenceCrystallography, X-RayGalectin 4HumansMolecular Dynamics SimulationProtein ConformationProtein StabilitySolubilityStructure-Activity RelationshipThermodynamicsGalectin 4

Identifiers

PMID27642006
PMCPMC5027518
OpenAlexW2522276088

What OpenQuestion holds

Textmetadata
LicenceCC BY
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.