Evidence map›Paper›PMID 19292456›Full record

ArticleBiochemistry2009

Thermodynamics of multivalent carbohydrate-lectin cross-linking interactions: importance of entropy in the bind and jump mechanism.

Tarun K Dam, Thomas A Gerken, C Fred Brewer

Open access · greenAbstract read
In one paragraph

Article in Biochemistry, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 40 papers.

0numbers the graph read from it
0cells of the map it votes in
40citing papers in PubMed
3.1field-weighted citation impact, top 8% 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

40 citing papers in PubMed, 105 citations in OpenAlex.

  1. Article
  2. Afil, a Lectin fromMicroorganisms · 2025
    Article
  3. Article
  4. Review
  5. Article
  6. Review
  7. Article
  8. LectinOracle: A Generalizable Deep Learning Model for Lectin-Glycan Binding Prediction.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2022
    Article
  9. Review
  10. Article
  11. Article
  12. Article
  13. Article
  14. Article
  15. Article
  16. Article
  17. Article
  18. Article
  19. Following sugar patterns in search of galectin function.Proceedings of the National Academy of Sciences of the United States of America · 2018
    Article
  20. 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

3 authors at 2 institutions in 1 country.

Tarun K DamDepartment of Molecular Pharmacology, Albert Einstein College of Medicine, Bronx, New York 10461, USA.
Thomas A Gerken
C Fred Brewer
Albert Einstein College of Medicine · USUniversity School · US

Funding

WORD PROCESSORP30CA013330 · NCI · YESHIVA UNIVERSITY · PI ALYSON B MOADEL · 1985 to 2026
$111.2M
Translational Research in Cystic FibrosisP30DK027651 · NIDDK · CASE WESTERN RESERVE UNIVERSITY · PI DRUMM, MITCHELL L · 1986 to 2014
$15.6M
MUCIN SITE SPECIFIC O-GLYCOSYLATIONR01CA078834 · NCI · CASE WESTERN RESERVE UNIVERSITY · PI GERKEN, THOMAS A · 1999 to 2012
$3.4M
CAROHYDRATE AND GLYCOPROTEIN INTERACTIONS WITH LECTINSR01CA016054 · NCI · YESHIVA UNIVERSITY · PI BREWER, CURTIS FRED · 1987 to 2006
$3.1M
NCI NIH HHS CA-16054NCI NIH HHS CA-78834NCI NIH HHS P30 CA013330NCI NIH HHS P30 CA-13330NCI NIH HHS R01 CA016054NCI NIH HHS R01 CA078834NIDDK NIH HHS P30 DK027651
6 · The paper itself

Abstract

The high affinity (K(d) = 0.2 nM) of the soybean agglutinin (SBA), a tetrameric GalNAc specific lectin, for a modified form of porcine submaxillary mucin, a linear glycoprotein, with a molecular mass of approximately 10(6) Da and approximately 2300 GalNAcalpha1-O-Ser/Thr residues (Tn-PSM) has been ascribed to an internal diffusion mechanism that involves binding and jumping of the lectin from GalNAc to GalNAc residue of the mucin [Dam, T. K., et al. (2007) J. Biol. Chem. 282, 28256-28263]. Hill plot analysis of the raw ITC data shows increasing negative cooperativity, which correlates with an increasing number of lectin-mucin cross-linking interactions and decreasing favorable binding entropies. However, the affinity of bound SBA for other Tn-PSM molecules during cross-linking is much higher than that of free SBA for GalNAcalpha1-O-Ser, a monovalent analogue. The high affinity of bound SBA for GalNAc residues on other Tn-PSM molecules appears to be due to the favorable entropy of binding associated with the internal diffusion mechanism. Furthermore, the increasing negative cooperativity of SBA binding to Tn-PSM correlates with a decreasing level of internal diffusion of the lectin on the mucin as cross-linking occurs. These findings indicate the importance of the internal diffusion mechanism in generating large, favorable entropies of binding that drive lectin-mucin cross-linking interactions. The results are important for understanding the energetics of lectin-mucin cross-linking interactions that are associated with biological signaling on the surface of cells and the role of the internal diffusion mechanism in ligand-biopolymer interactions in general.

Indexed as

ThermodynamicsBinding SitesCarbohydrate ConformationCarbohydratesDiffusionLectinsCarbohydratesLectins

Identifiers

PMID19292456
PMCPMC2691598
OpenAlexW2019209704

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.