Evidence map›Paper›PMID 26690112›Full record

ArticleMolecules (Basel, Switzerland)2015

Identification of Hydrophobic Interfaces in Protein-Ligand Complexes by Selective Saturation Transfer NMR Spectroscopy.

Fabien Ferrage, Kaushik Dutta, David Cowburn

Abstract read
In one paragraph

Article in Molecules (Basel, Switzerland), 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.

0numbers the graph read from it
0cells of the map it votes in
0citing papers in PubMed
–field-weighted citation impact
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

0 citing papers in PubMed.

No citing paper in PubMed yet.

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.

Fabien FerrageNew York Structural Biology Center, New York, NY 10027, USA. fabien.ferrage@ens.fr.
Kaushik DuttaNew York Structural Biology Center, New York, NY 10027, USA. kskdutta@gmail.com.
David CowburnNew York Structural Biology Center, New York, NY 10027, USA. david.cowburn@einstein.yu.edu.

Funding

900 MHz NMR Spectrometer for Structural BiologyP41GM066354 · NIGMS · NEW YORK STRUCTURAL BIOLOGY CENTER · PI COWBURN, DAVID · 2002 to 2006
$4.7M
Structural Biology of Protein KinasesR01GM047021 · NIGMS · ROCKEFELLER UNIVERSITY · PI COWBURN, DAVID · 1992 to 2008
$2.4M
NIGMS NIH HHS GM47021NIGMS NIH HHS GM66354NIGMS NIH HHS P41 GM066354NIGMS NIH HHS R01 GM047021
6 · The paper itself

Abstract

The proper characterization of protein-ligand interfaces is essential for structural biology, with implications ranging from the fundamental understanding of biological processes to pharmacology. Nuclear magnetic resonance is a powerful technique for such studies. We propose a novel approach to the direct determination of the likely pose of a peptide ligand onto a protein partner, by using frequency-selective cross-saturation with a low stringency isotopic labeling methods. Our method illustrates a complex of the Src homology 3 domain of C-terminal Src kinase with a peptide from the proline-enriched tyrosine phosphatase.

Indexed as

Amino Acid SequenceBinding SitesCSK Tyrosine-Protein KinaseHydrophobic and Hydrophilic InteractionsLigandsModels, MolecularNuclear Magnetic Resonance, BiomolecularPeptide FragmentsProtein BindingProtein Tyrosine Phosphatasessrc-Family Kinasessrc Homology DomainsCSK Tyrosine-Protein KinaseLigandsPeptide FragmentsProtein Tyrosine Phosphatasessrc-Family Kinasescross-saturationinterface identificationNMRSH3 ligand

Identifiers

PMID26690112
PMCPMC6332028

What OpenQuestion holds

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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.