Evidence map›Paper›PMID 33770486›Full record

ReviewCell chemical biology2021

Degradation from the outside in: Targeting extracellular and membrane proteins for degradation through the endolysosomal pathway.

Green Ahn, Steven M Banik, Carolyn R Bertozzi

Open access · bronzeAbstract readReview
In one paragraph

Review in Cell chemical biology, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 36 papers.

0numbers the graph read from it
0cells of the map it votes in
36citing papers in PubMed
4.2field-weighted citation impact, top 4% 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

36 citing papers in PubMed, 84 citations in OpenAlex.

  1. Article
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  5. Dynamic reprogramming of the tumor immune network via multicycle checkpoint degradation for cancer immunotherapy.Proceedings of the National Academy of Sciences of the United States of America · 2026
    Article
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  15. Induced proximity at the cell surface.Nature biotechnology · 2025
    Review
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  17. Article
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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

3 authors at 2 institutions in 1 country.

Green AhnDepartment of Chemistry and Stanford ChEM-H, Stanford University, Stanford, CA 94305, USA.
Steven M BanikDepartment of Chemistry and Stanford ChEM-H, Stanford University, Stanford, CA 94305, USA.
Carolyn R BertozziDepartment of Chemistry and Stanford ChEM-H, Stanford University, Stanford, CA 94305, USA; Howard Hughes Medical Institute, Stanford, CA 94305, USA. Electronic address: bertozzi@stanford.edu.
Stanford University · USHoward Hughes Medical Institute · US

Funding

METABOLIC OLIGOSACCHARIDE ENGINEERINGR01GM058867 · NIGMS · UNIVERSITY OF CALIFORNIA BERKELEY · PI Carolyn Bertozzi · 1999 to 2026
$5.6M
Howard Hughes Medical InstituteNIGMS NIH HHS R01 GM058867
6 · The paper itself

Abstract

Targeted protein degradation (TPD) is a promising strategy to remove deleterious proteins for therapeutic benefit and to probe biological pathways. The past two decades have witnessed a surge in the development of technologies that rely on intracellular machinery to degrade challenging cytosolic targets. However, these TPD platforms leave the majority of extracellular and membrane proteins untouched. To enable degradation of these classes of proteins, internalizing receptors can be co-opted to traffic extracellular proteins to the lysosome. Sweeping antibodies and Seldegs use Fc receptors in conjunction with engineered antibodies to degrade soluble proteins. Recently, lysosome-targeting chimeras (LYTACs) have emerged as a strategy to degrade both secreted and membrane-anchored targets. Together with other newcomer technologies, including antibody-based proteolysis-targeting chimeras, modalities that degrade extracellular proteins have promising translational potential. This perspective will give an overview of TPD platforms that degrade proteins via outside-in approaches and focus on the recent development of LYTACs.

Indexed as

LysosomesMembrane ProteinsMembrane ProteinsAbTACsextracellular and membrane protein degradationlysosomeLYTACsMoDE-AsSeldegsSweeping antibodiestargeted protein degradation

Identifiers

PMID33770486
PMCPMC8286304
OpenAlexW3137806971

What OpenQuestion holds

Textmetadata
LicenceCC BY
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.