Evidence map›Paper›PMID 31128780›Full record

ArticleMethods in enzymology2019

Chemical biology of glycoproteins: From chemical synthesis to biological impact.

Yaohao Li, Amy H Tran, Samuel J Danishefsky, Zhongping Tan

Open access · greenAbstract read
In one paragraph

Article in Methods in enzymology, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 31 papers.

0numbers the graph read from it
0cells of the map it votes in
31citing papers in PubMed
7.4field-weighted citation impact, top 2% 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

31 citing papers in PubMed, 46 citations in OpenAlex.

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  4. Assessment of genetically modified maize DAS1131 (application GMFF-2021-1530).EFSA journal. European Food Safety Authority · 2025
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  19. Pathogens (Basel, Switzerland) · 2022
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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

4 authors at 3 institutions in 2 countries.

Yaohao LiInstitute of Materia Medica, Chinese Academy of Medical Sciences and Peking Union Medical College, Beijing, China; Department of Biochemistry and BioFrontiers Institute, University of Colorado, Boulder, CO, United States.
Amy H TranDepartment of Biochemistry and BioFrontiers Institute, University of Colorado, Boulder, CO, United States.
Samuel J DanishefskyChemical Biology Program, Sloan Kettering Institute, Memorial Sloan Kettering Cancer Center, New York, NY, United States. Electronic address: danishes@mskcc.org.
Zhongping TanInstitute of Materia Medica, Chinese Academy of Medical Sciences and Peking Union Medical College, Beijing, China; Department of Biochemistry and BioFrontiers Institute, University of Colorado, Boulder, CO, United States. Electronic address: zhongping.tan@imm.pumc.edu.cn.
University of Colorado Boulder · USChinese Academy of Medical Sciences & Peking Union Medical College · CNMemorial Sloan Kettering Cancer Center · US

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

Recent advances have demonstrated the feasibility and robustness of chemical synthesis for the production of homogeneously glycosylated protein forms (glycoforms). By taking advantage of the unmatchable flexibility and precision provided by chemical synthesis, the quantitative effects of glycosylation were obtained using chemical glycobiology approaches. These findings greatly advanced our fundamental knowledge of glycosylation. More importantly, analysis of these findings has led to the development of glycoengineering guidelines for rationally improving the properties of peptides and proteins. In this chapter, we present the key experimental steps for chemical biology studies of protein glycosylation, with the aim of facilitating and promoting research in this important but significantly underexplored area of biology.

Indexed as

AnimalsChemistry Techniques, SyntheticGlycopeptidesGlycoproteinsGlycosylationHumansModels, MolecularProtein ConformationProtein FoldingProtein StabilitySynthetic BiologyGlycopeptidesGlycoproteinsChemical glycobiologyChemical synthesisGlycoengineeringGlycoproteinsNCL/MFD

Identifiers

PMID31128780
PMCPMC6595224
OpenAlexW2920925486

What OpenQuestion holds

Textmetadata
LicenceTDM
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.