Evidence map›Paper›PMID 32793559›Full record

ReviewFrontiers in chemistry2020

Protein Glycoengineering: An Approach for Improving Protein Properties.

Bo Ma, Xiaoyang Guan, Yaohao Li, Shiying Shang, Jing Li, Zhongping Tan

Abstract readReview
In one paragraph

Review in Frontiers in chemistry, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 34 papers.

0numbers the graph read from it
0cells of the map it votes in
34citing 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

34 citing papers in PubMed.

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  19. Recombinant mucin biotechnology and engineering.Advanced drug delivery reviews · 2023
    Review
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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

6 authors.

Bo MaState Key Laboratory of Bioactive Substance and Function of Natural Medicines, Institute of Materia Medica, Chinese Academy of Medical Sciences and Peking Union Medical College, Beijing, China.
Xiaoyang GuanDepartment of Chemistry and Biochemistry and BioFrontiers Institute, University of Colorado, Boulder, CO, United States.
Yaohao LiState Key Laboratory of Bioactive Substance and Function of Natural Medicines, Institute of Materia Medica, Chinese Academy of Medical Sciences and Peking Union Medical College, Beijing, China.
Shiying ShangSchool of Pharmaceutical Sciences, Tsinghua University, Beijing, China.
Jing LiBeijing Key Laboratory of DNA Damage Response and College of Life Sciences, Capital Normal University, Beijing, China.
Zhongping TanState Key Laboratory of Bioactive Substance and Function of Natural Medicines, Institute of Materia Medica, Chinese Academy of Medical Sciences and Peking Union Medical College, Beijing, China.

Funding

Glycoengineering of Therapeutic Peptides for Improved Treatment of Human DiseasesR01EB025892 · NIBIB · UNIVERSITY OF COLORADO · PI SAMMAKIA, TAREK · 2018 to 2021
$1.3M
NIBIB NIH HHS R01 EB025892
6 · The paper itself

Abstract

Natural proteins are an important source of therapeutic agents and industrial enzymes. While many of them have the potential to be used as highly effective medical treatments for a wide range of diseases or as catalysts for conversion of a range of molecules into important product types required by modern society, problems associated with poor biophysical and biological properties have limited their applications. Engineering proteins with reduced side-effects and/or improved biophysical and biological properties is therefore of great importance. As a common protein modification, glycosylation has the capacity to greatly influence these properties. Over the past three decades, research from many disciplines has established the importance of glycoengineering in overcoming the limitations of proteins. In this review, we will summarize the methods that have been used to glycoengineer proteins and briefly discuss some representative examples of these methods, with the goal of providing a general overview of this research area.

Indexed as

biological methodchemical methodenzymeglycoengineeringtherapeutic protein

Identifiers

PMID32793559
PMCPMC7390894

What OpenQuestion holds

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Registered trials

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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.