Evidence map›Paper›PMID 20959104›Full record

ArticleBiophysical journal2010

Human GLTP: Three distinct functions for the three tryptophans in a novel peripheral amphitropic fold.

Ravi Kanth Kamlekar, Yongguang Gao, Roopa Kenoth, Julian G Molotkovsky, Franklyn G Prendergast, Lucy Malinina, Dinshaw J Patel, William S Wessels, Sergei Y Venyaminov, Rhoderick E Brown

Open access · bronzeAbstract read
In one paragraph

Article in Biophysical journal, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 18 papers.

0numbers the graph read from it
0cells of the map it votes in
18citing papers in PubMed
1.6field-weighted citation impact, top 18% 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

18 citing papers in PubMed, 26 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Article
  5. Review
  6. Article
  7. Review
  8. Article
  9. Sphingolipid transfer proteins defined by the GLTP-fold.Quarterly reviews of biophysics · 2015
    Article
  10. Structural insights into lipid-dependent reversible dimerization of human GLTP.Acta crystallographica. Section D, Biological crystallography · 2013
    Article
  11. Article
  12. Article
  13. Article
  14. Review
  15. Article
  16. Article
  17. Article
  18. 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

10 authors at 6 institutions in 3 countries.

Ravi Kanth KamlekarThe Hormel Institute, University of Minnesota, Austin, USA.
Yongguang Gao
Roopa Kenoth
Julian G Molotkovsky
Franklyn G Prendergast
Lucy Malinina
Dinshaw J Patel
William S Wessels
Sergei Y Venyaminov
Rhoderick E Brown
Mayo Clinic · USHormel (United States) · USUniversity of Minnesota · USCIC bioGUNE · ESMemorial Sloan Kettering Cancer Center · USRussian Academy of Sciences · RU

Funding

GLYCOLIPID TRANSFER--REGULATION BY MEMBRANE INTERFACESR01GM045928 · NIGMS · UNIVERSITY OF MINNESOTA TWIN CITIES · PI BROWN, RHODERICK E · 1992 to 2014
$4.8M
MOLECULAR BASIS OF GLYCOSPHINGOLIPID BINDING SPECIFICITYR01CA121493 · NCI · SLOAN-KETTERING INST CAN RESEARCH · PI PATEL, DINSHAW J · 2006 to 2010
$1.2M
STRUCTURE/LUMINESCENCE CORRELATIONS IN PROTEINSR01GM034847 · NIGMS · MAYO CLINIC COLL OF MEDICINE, ROCHESTER · PI PRENDERGAST, FRANKLYN G · 1985 to 2001
$715k
NCI NIH HHS CA121493NCI NIH HHS R01 CA121493NIGMS NIH HHS GM34847NIGMS NIH HHS GM45928NIGMS NIH HHS R01 GM045928
6 · The paper itself

Abstract

Human glycolipid transfer protein (GLTP) serves as the GLTP-fold prototype, a novel, to our knowledge, peripheral amphitropic fold and structurally unique lipid binding motif that defines the GLTP superfamily. Despite conservation of all three intrinsic Trps in vertebrate GLTPs, the Trp functional role(s) remains unclear. Herein, the issue is addressed using circular dichroism and fluorescence spectroscopy along with an atypical Trp point mutation strategy. Far-ultraviolet and near-ultraviolet circular dichroism spectroscopic analyses showed that W96F-W142Y-GLTP and W96Y-GLTP retain their native conformation and stability, whereas W85Y-W96F-GLTP is slightly altered, in agreement with relative glycolipid transfer activities of >90%, ∼85%, and ∼45%, respectively. In silico three-dimensional modeling and acrylamide quenching of Trp fluorescence supported a nativelike folding conformation. With the Trp⁹⁶-less mutants, changes in emission intensity, wavelength maximum, lifetime, and time-resolved anisotropy decay induced by phosphoglyceride membranes lacking or containing glycolipid and by excitation at different wavelengths along the absorption-spectrum red edge indicated differing functions for W142 and W85. The data suggest that W142 acts as a shallow-penetration anchor during docking with membrane interfaces, whereas the buried W85 indole helps maintain proper folding and possibly regulates membrane-induced transitioning to a glycolipid-acquiring conformation. The findings illustrate remarkable versatility for Trp, providing three distinct intramolecular functions in the novel amphitropic GLTP fold.

Indexed as

TryptophanCarrier ProteinsCell MembraneCircular DichroismFluorescence PolarizationGlycolipidsHumansModels, MolecularMutagenesisMutationProtein Structure, TertiarySolubilitySpectrometry, FluorescenceTime FactorsCarrier ProteinsGLTP protein, humanGlycolipidsTryptophan

Identifiers

PMID20959104
PMCPMC2955354
OpenAlexW1980729214

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.