Evidence map›Paper›PMID 18393823›Full record

ReviewCurrent drug targets2008

Structure and function of beta -1,4-galactosyltransferase.

Pradman K Qasba, Boopathy Ramakrishnan, Elizabeth Boeggeman

Open access · greenAbstract readReview
In one paragraph

Review in Current drug targets, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 79 papers.

0numbers the graph read from it
0cells of the map it votes in
79citing papers in PubMed
2.9field-weighted citation impact, top 9% 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

79 citing papers in PubMed, 127 citations in OpenAlex.

  1. MBPBERT: A Large Language Model for Metal-Binding Peptide Discovery.Interdisciplinary sciences, computational life sciences · 2026
    Article
  2. Article
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  4. Review
  5. Loss of sialic acid side-chainProceedings of the National Academy of Sciences of the United States of America · 2025
    Article
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  7. Article
  8. Review
  9. Review
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  11. UnderstandingCell surface (Amsterdam, Netherlands) · 2023
    Review
  12. Article
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  14. Article
  15. Article
  16. Article
  17. Review
  18. Review
  19. B4GALT1 as a New Biomarker of Idiopathic Pulmonary Fibrosis.International journal of molecular sciences · 2022
    Article
  20. Article

19 more citing papers are in PubMed but not listed here.

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 1 institution in 1 country.

Pradman K QasbaStructural Glycobiology Section, CCRNP, NCI-Frederick, Building 469, Room 221, Frederick, Maryland 21702, USA. qasba@helix.nih.gov
Boopathy Ramakrishnan
Elizabeth Boeggeman
Frederick National Laboratory for Cancer Research · US

Funding

Structure-Function Studies and Design of Novel GlycosyltransferasesZIABC009304 · NCI · DIVISION OF BASIC SCIENCES - NCI · PI QASBA, PRADMAN K · 2009 to 2013
$1.2M
Utilizing Glycosyltransferases for BioconjugationZ01BC010742 · NCI · DIVISION OF BASIC SCIENCES - NCI · PI QASBA, PRADMAN K · 2006 to 2008
$678k
Structure-Function Studies and Design of Novel GlycosyltransferasesZ01BC009304 · NCI · DIVISION OF BASIC SCIENCES - NCI · PI QASBA, PRADMAN K · 1996 to 2008
$631k
Oligosaccharide substrate interactions with beta-1,4-GalZ01BC010041 · NCI · DIVISION OF BASIC SCIENCES - NCI · PI QASBA, PRADMAN K · 1996 to 2008
$216k
Intramural NIH HHS Z01 BC009304Intramural NIH HHS Z01 BC010041Intramural NIH HHS Z01 BC010742Intramural NIH HHS Z99 CA999999PHS HHS N01-C0-12400
6 · The paper itself

Abstract

Beta-1,4-galactosylransferase (beta4Gal-T1) participates in the synthesis of Galbeta1-4-GlcNAc-disaccharide unit of glycoconjugates. It is a trans-Golgi glycosyltransferase (Glyco-T) with a type II membrane protein topology, a short N-terminal cytoplasmic domain, a membrane-spanning region, as well as a stem and a C-terminal catalytic domain facing the trans-Golgi-lumen. Its hydrophobic membrane-spanning region, like that of other Glyco-T, has a shorter length compared to plasma membrane proteins, an important feature for its retention in the trans-Golgi. The catalytic domain has two flexible loops, a long and a small one. The primary metal binding site is located at the N-terminal hinge region of the long flexible loop. Upon binding of metal ion and sugar-nucleotide, the flexible loops undergo a marked conformational change, from an open to a closed conformation. Conformational change simultaneously creates at the C-terminal region of the flexible loop an oligosaccharide acceptor binding site that did not exist before. The loop acts as a lid covering the bound donor substrate. After completion of the transfer of the glycosyl unit to the acceptor, the saccharide product is ejected; the loop reverts to its native conformation to release the remaining nucleotide moiety. The conformational change in beta4Gal-T1 also creates the binding site for a mammary gland-specific protein, alpha-lactalbumin (LA), which changes the acceptor specificity of the enzyme toward glucose to synthesize lactose during lactation. The specificity of the sugar donor is generally determined by a few residues in the sugar-nucleotide binding pocket of Glyco-T, conserved among the family members from different species. Mutation of these residues has allowed us to design new and novel glycosyltransferases, with broader or requisite donor and acceptor specificities, and to synthesize specific complex carbohydrates as well as specific inhibitors for these enzymes.

Indexed as

Protein ConformationBinding SitesHumansModels, MolecularMutationN-Acetyllactosamine SynthaseN-Acetyllactosamine Synthase

Identifiers

PMID18393823
PMCPMC2365515
OpenAlexW2095997872

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.