Evidence map›Paper›PMID 21030291›Full record

ReviewCurrent opinion in chemical biology2010

Chemoenzymatic methods for site-specific protein modification.

David Rabuka

Open access · greenAbstract readReview
In one paragraph

Review in Current opinion in chemical biology, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 37 papers.

0numbers the graph read from it
0cells of the map it votes in
37citing papers in PubMed
3.9field-weighted citation impact, top 6% 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

37 citing papers in PubMed, 121 citations in OpenAlex.

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  15. Engineered control of enzyme structural dynamics and function.Protein science : a publication of the Protein Society · 2018
    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

1 author at 1 institution in 1 country.

David RabukaRedwood Bioscience, Burlingame, CA 94010, USA. drabuka@redwoodbioscience.com
Redwood Scientific (United States) · US

Funding

Universal Protein Carrier Scaffold for Small Molecules and Peptide TherapeuticsRC1AA019619 · NIAAA · REDWOOD BIOSCIENCE, INC. · PI RABUKA, DAVID IAN · 2009 to 2010
$1000k
NIAAA NIH HHS RC1 AA019619NIBIB NIH HHS 1RC1EB010344-01
6 · The paper itself

Abstract

In the past decade, numerous chemical technologies have been developed to allow the site-specific post-translational modification of proteins. Traditionally covalent chemical protein modification has been accomplished by the attachment of synthetic groups to nucleophilic amino acids on protein surfaces. These chemistries, however, are rarely sufficiently selective to distinguish one residue within a literal sea of chemical functionality. One solution to this problem is to introduce a unique chemical handle into the target protein that is orthogonal to the remainder of the proteome. In practice, this handle can be a novel peptide sequence, which forms a 'tag' that is selectively and irreversibly modified by enzymes. Furthermore, if the enzymes can tolerate substrate analogs, it becomes possible to engineer chemically modified proteins in a site-specific fashion. This review details the significant progress in creating techniques for the chemoenzymatic generation of protein-small molecule constructs and provides examples of novel applications of these methodologies.

Indexed as

Protein Processing, Post-TranslationalAnimalsHumansProtein EngineeringProteinsSmall Molecule LibrariesProteinsSmall Molecule Libraries

Identifiers

PMID21030291
PMCPMC2997875
OpenAlexW2092014932

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.