Evidence map›Paper›PMID 7816856›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America1995

Conformational implications of asparagine-linked glycosylation.

B Imperiali, K W Rickert

Open access · greenAbstract readComparative Study
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 1995. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 45 papers.

0numbers the graph read from it
0cells of the map it votes in
45citing papers in PubMed
4.5field-weighted citation impact, top 4% 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

45 citing papers in PubMed, 171 citations in OpenAlex.

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  4. UniqueJournal of biological engineering · 2019
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  14. Profile of Barbara Imperiali.Proceedings of the National Academy of Sciences of the United States of America · 2013
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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

2 authors at 1 institution in 1 country.

B ImperialiDivision of Chemistry and Chemical Engineering, California Institute of Technology, Pasadena 91125.
K W Rickert
California Institute of Technology · US

Funding

SPECIFICITY IN CO- AND POST-TRANSLATIONAL MODIFICATIONR01GM039334 · NIGMS · MASSACHUSETTS INSTITUTE OF TECHNOLOGY · PI ALLEN, KAREN N., IMPERIALI, BARBARA · 1993 to 2025
$8.0M
SPECIFICITY IN CO POST TRANSLATION MODIFICATIONR29GM039334 · NIGMS · CARNEGIE-MELLON UNIVERSITY · PI IMPERIALI, BARBARA · 1988 to 1992
–
NIGMS NIH HHS GM39334
6 · The paper itself

Abstract

The effects of cotranslational protein modification on the process of protein folding are poorly understood. Time-resolved fluorescence energy transfer has been used to assess the impact of glycosylation on the conformational dynamics of flexible oligopeptides. The peptide sequences examined are selected from glycoproteins of known three-dimensional structure. The energy transfer modulation associated with N-linked glycosylation is consistent with the glycopeptides sampling different conformational profiles in water. Results show that glycosylation causes the modified peptides to adopt a different ensemble of conformations, and for some peptides this change may lead to conformations that are more compact and better approximate the conformation of these peptides in the final folded protein. This result further implies that cotranslational glycosylation can trigger the timely formation of structural nucleation elements and thus assist in the complex process of protein folding.

Indexed as

AsparagineHexosyltransferasesMembrane ProteinsProtein ConformationProtein FoldingAmino Acid SequenceFluorescent DyesGlycopeptidesGlycoproteinsGlycosylationHemagglutininsImmunoglobulin AImmunoglobulin Fab FragmentsIndicators and ReagentsKineticsMolecular Sequence DataAsparaginedolichyl-diphosphooligosaccharide - protein glycotransferaseFluorescent DyesGlycopeptidesGlycoproteinsHemagglutininsHexosyltransferasesImmunoglobulin AImmunoglobulin Fab FragmentsIndicators and ReagentsMembrane ProteinsOligopeptidesSolventsTransferases

Identifiers

PMID7816856
PMCPMC42824
OpenAlexW1994172525

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.