Evidence map›Paper›PMID 26911284›Full record

ArticleGlycobiology2016

Intra- and intermolecular interactions of human galectin-3: assessment by full-assignment-based NMR.

Hans Ippel, Michelle C Miller, Sabine Vértesy, Yi Zheng, F Javier Cañada, Dennis Suylen, Kimiko Umemoto, Cecilia Romanò, Tilman Hackeng, Guihua Tai and 8 more

Open access · bronzeAbstract read
In one paragraph

Article in Glycobiology, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 46 papers.

0numbers the graph read from it
0cells of the map it votes in
46citing papers in PubMed
4.8field-weighted citation impact, top 5% 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

46 citing papers in PubMed, 83 citations in OpenAlex.

  1. Galectin-3 Mediates TGF-β-Controlled Migration in Müller Glial Cells.International journal of molecular sciences · 2026
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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

18 authors at 11 institutions in 8 countries.

Hans IppelDepartment of Biochemistry, Molecular Biology and Biophysics, University of Minnesota, Minneapolis, MN 55455, USA.
Michelle C MillerDepartment of Biochemistry, Molecular Biology and Biophysics, University of Minnesota, Minneapolis, MN 55455, USA.
Sabine VértesyInstitute of Physiological Chemistry, Faculty of Veterinary Medicine, Ludwig-Maximilians-University Munich, 80539 Munich, Germany.
Yi ZhengSchool of Life Science, Northeast Normal University, 130024 Changchun, People's Republic of China.
F Javier CañadaChemical and Physical Biology, Centro de Investigaciones Biológicas, CSIC, 28040 Madrid, Spain.
Dennis SuylenDepartment of Biochemistry and CARIM, Maastricht University, Maastricht, The Netherlands.
Kimiko UmemotoDepartment of Chemistry, International Christian University, Tokyo, Japan.
Cecilia RomanòCenter for Synthesis and Chemical Biology, University College Dublin, Belfield, Dublin 4, Ireland.
Tilman HackengDepartment of Biochemistry and CARIM, Maastricht University, Maastricht, The Netherlands.
Guihua TaiSchool of Life Science, Northeast Normal University, 130024 Changchun, People's Republic of China.
Hakon LefflerDepartment of Laboratory Medicine, Microbiology, Immunology, Glycobiology Section, 22362 Lund, Sweden.
Jürgen KopitzInstitute of Pathology, Applied Tumor Biology, Ruprecht-Karls-University, 69120 Heidelberg, Germany.
Sabine AndréInstitute of Physiological Chemistry, Faculty of Veterinary Medicine, Ludwig-Maximilians-University Munich, 80539 Munich, Germany.
Dieter KüblerMechanismen Biomolekularer Interaktionen, Deutsches Krebsforschungszentrum, 69120 Heidelberg, Germany.
Jesús Jiménez-BarberoCIC bioGUNE, Bizkaia Technological Park, 48160 Derio, Spain.
Stefan OscarsonCenter for Synthesis and Chemical Biology, University College Dublin, Belfield, Dublin 4, Ireland.
Hans-Joachim GabiusInstitute of Physiological Chemistry, Faculty of Veterinary Medicine, Ludwig-Maximilians-University Munich, 80539 Munich, Germany.
Kevin H MayoDepartment of Biochemistry, Molecular Biology and Biophysics, University of Minnesota, Minneapolis, MN 55455, USA.
Ludwig-Maximilians-Universität München · DEUniversity of Minnesota · USMaastricht University · NLNortheast Normal University · CNUniversity College Dublin · IECentro de Investigaciones Biológicas Margarita Salas · ESCIC bioGUNE · ESGerman Cancer Research Center · DEHeidelberg University · DEInternational Christian University · JPLund University · SE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Galectin-3 is an adhesion/growth-regulatory protein with a modular design comprising an N-terminal tail (NT, residues 1-111) and the conserved carbohydrate recognition domain (CRD, residues 112-250). The chimera-type galectin interacts with both glycan and peptide motifs. Complete (13)C/(15)N-assignment of the human protein makes NMR-based analysis of its structure beyond the CRD possible. Using two synthetic NT polypeptides covering residues 1-50 and 51-107, evidence for transient secondary structure was found with helical conformation from residues 5 to 15 as well as proline-mediated, multi-turn structure from residues 18 to 32 and around PGAYP repeats. Intramolecular interactions occur between the CRD F-face (the 5-stranded β-sheet behind the canonical carbohydrate-binding 6-stranded β-sheet of the S-face) and NT in full-length galectin-3, with the sequence P(23)GAW(26)…P(37)GASYPGAY(45) defining the primary binding epitope within the NT. Work with designed peptides indicates that the PGAX motif is crucial for self-interactions between NT/CRD. Phosphorylation at position Ser6 (and Ser12) (a physiological modification) and the influence of ligand binding have minimal effect on this interaction. Finally, galectin-3 molecules can interact weakly with each other via the F-faces of their CRDs, an interaction that appears to be assisted by their NTs. Overall, our results add insight to defining binding sites on galectin-3 beyond the canonical contact area for β-galactosides.

Indexed as

Amino Acid SequenceBinding SitesBlood ProteinsCarbon IsotopesCloning, MolecularEscherichia coliGalectin 3GalectinsGene ExpressionGenetic VectorsHumansModels, MolecularNitrogen IsotopesNuclear Magnetic Resonance, BiomolecularPeptidesPhosphorylationBlood ProteinsCarbon IsotopesGalectin 3GalectinsLGALS3 protein, humanNitrogen IsotopesPeptidesRecombinant Proteinsadhesionapoptosislectinphosphorylationself-association

Identifiers

PMID26911284
PMCPMC5018044
OpenAlexW2289049983

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.