Evidence map›Paper›PMID 25805144›Full record

ReviewTopics in current chemistry2015

Total synthesis of glycosylated proteins.

Alberto Fernández-Tejada, John Brailsford, Qiang Zhang, Jae-Hung Shieh, Malcolm A S Moore, Samuel J Danishefsky

Abstract readReview
In one paragraph

Review in Topics in current chemistry, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 22 papers.

0numbers the graph read from it
0cells of the map it votes in
22citing papers in PubMed
260.7field-weighted citation impact, top 1% 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

22 citing papers in PubMed, 51 citations in OpenAlex.

  1. Article
  2. Identification and comparison ofFood chemistry: X · 2025
    Article
  3. Review
  4. Review
  5. Article
  6. Article
  7. Review
  8. Cell-free systems for accelerating glycoprotein expression and biomanufacturing.Journal of industrial microbiology & biotechnology · 2020
    Review
  9. Review
  10. Article
  11. Review
  12. Review
  13. Review
  14. Oligosaccharide Synthesis and Translational Innovation.Journal of the American Chemical Society · 2019
    Review
  15. Article
  16. Article
  17. Review
  18. Article
  19. Review
  20. Article
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 at 1 institution in 1 country.

Alberto Fernández-TejadaLaboratory for Bioorganic Chemistry, Molecular Pharmacology and Chemistry Program, 1275 York Avenue, New York, NY, 10065, USA, aftejada@cib.csic.es.
John Brailsford
Qiang Zhang
Jae-Hung Shieh
Malcolm A S Moore
Samuel J Danishefsky
Kettering University · US

Funding

X-RAY CRYSTALLOGRAPHYP30CA008748 · NCI · SLOAN-KETTERING INSTITUTE FOR CANCER RES · PI Nicholas D Socci · 1985 to 2026
$347.4M
CANCER PHARMACOLOGYT32CA062948 · NCI · WEILL MEDICAL COLL OF CORNELL UNIV · PI LORRAINE J GUDAS · 1994 to 2026
$12.1M
THE SYNTHESIS OF ANTITUMOR NATURAL PRODUCTSR01CA028824 · NCI · YALE UNIVERSITY · PI CHIOSIS, GABRIELA · 1985 to 2016
$2.7M
Synthesis Directed Toward Therapeutic AgentsR01GM102872 · NIGMS · SLOAN-KETTERING INST CAN RESEARCH · PI TAN, DEREK S · 2012 to 2015
$2.3M
New Synthetic Reactions to Reach Bioactive ProteinsR01GM109760 · NIGMS · SLOAN-KETTERING INST CAN RESEARCH · PI LUO, MINKUI · 2014 to 2017
$1.7M
NCI NIH HHS P30 CA008748NCI NIH HHS R01 CA028824NCI NIH HHS T32 CA062948NIGMS NIH HHS R01 GM102872NIGMS NIH HHS R01 GM109760
6 · The paper itself

Abstract

Glycoproteins are an important class of naturally occurring biomolecules which play a pivotal role in many biological processes. They are biosynthesized as complex mixtures of glycoforms through post-translational protein glycosylation. This fact, together with the challenges associated with producing them in homogeneous form, has hampered detailed structure-function studies of glycoproteins as well as their full exploitation as potential therapeutic agents. By contrast, chemical synthesis offers the unique opportunity to gain access to homogeneous glycoprotein samples for rigorous biological evaluation. Herein, we review recent methods for the assembly of complex glycopeptides and glycoproteins and present several examples from our laboratory towards the total chemical synthesis of clinically relevant glycosylated proteins that have enabled synthetic access to full-length homogeneous glycoproteins.

Indexed as

GlycoproteinsGlycosylationMolecular StructureProtein EngineeringGlycoproteins

Identifiers

PMID25805144
PMCPMC5079620
OpenAlexW235194763

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.