Evidence map›Paper›PMID 27580482›Full record

ReviewCurrent opinion in chemical biology2016

How PEGylation influences protein conformational stability.

Paul B Lawrence, Joshua L Price

Abstract readReview
In one paragraph

Review in Current opinion in chemical biology, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 57 papers.

0numbers the graph read from it
0cells of the map it votes in
57citing 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

57 citing papers in PubMed.

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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.

Paul B LawrenceDepartment of Chemistry and Biochemistry, Brigham Young University, Provo, UT 84602, United States.
Joshua L PriceDepartment of Chemistry and Biochemistry, Brigham Young University, Provo, UT 84602, United States.

Funding

Predictive Structure-based Guidelines for Identifying Optimal PEGylation Sites within Proteins and Understanding the Context-Dependence of Non-covalent Interaction StrengthR15GM116055 · NIGMS · BRIGHAM YOUNG UNIVERSITY · PI PRICE, JOSHUA L · 2015 to 2020
$781k
NIGMS NIH HHS R15 GM116055
6 · The paper itself

Abstract

PEGylation is an important strategy for enhancing the pharmacokinetic properties of protein therapeutics. The development of chemoselective side-chain modification reactions has enabled researchers to PEGylate proteins with high selectivity at defined locations. However, aside from avoiding active sites and binding interfaces, there are few guidelines for the selection of optimal PEGylation sites. Because conformational stability is intimately related to the ability of a protein to avoid proteolysis, aggregation, and immune responses, it is possible that PEGylating a protein at sites where PEG enhances conformational stability will result in PEG-protein conjugates with enhanced pharmacokinetic properties. However, the impact of PEGylation on protein conformational stability is incompletely understood. This review describes recent advances toward understanding the impact of PEGylation on protein conformational stability, along with the development of structure-based guidelines for selecting stabilizing PEGylation sites.

Indexed as

Protein StabilityPharmacokineticsPolyethylene GlycolsProtein ConformationPolyethylene Glycols

Identifiers

PMID27580482
PMCPMC5107330

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.