Development of a Glycoform Library-based Strategy to Decipher the Role of Protein Glycosylation.

Yaohao Li, Bo Ma, Xue Li, Shiying Shang, Zhongping Tan

Abstract read

In one paragraph

Article in Methods in molecular biology (Clifton, N.J.), 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.

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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

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3 · Its place in the literature

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4 · The record

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5 · Who and what money

Authors and funding

5 authors.

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.

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.

Xue 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 ShangCenter of Pharmaceutical Technology, School of Pharmaceutical Sciences, Tsinghua University, Beijing, China. shangshiying@mail.tsinghua.edu.cn.

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. zhongping.tan@imm.pumc.edu.cn.

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

Glycoproteins obtained from cell culture supernatants or lysates generally exist as mixtures of over 100 differently glycosylated protein forms (glycoforms). The study of glycosylation is significantly impeded because of the heterogeneous nature of glycoproteins. To overcome this challenge, we developed and optimized a glycoform library-based strategy to investigate the role of protein glycosylation. In this strategy, chemical synthesis was used to prepare individual homogeneous glycoforms and the role of glycosylation was determined by comparing a series of glycoforms with systematic differences in their glycosylation patterns.

Indexed as

GlycoproteinsGlycosylationGlycoproteinsGlycoformsGlycosylationLibraryProteinSynthesis

Identifiers

PMID35761051

DOI10.1021/jo8013897

What OpenQuestion holds

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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.