Evidence map›Paper›PMID 24601557›Full record

ReviewJournal of medicinal chemistry2014

Hydrocarbon-stapled peptides: principles, practice, and progress.

Loren D Walensky, Gregory H Bird

Abstract readReview
In one paragraph

Review in Journal of medicinal chemistry, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 350 papers.

0numbers the graph read from it
0cells of the map it votes in
350citing 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

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

350 citing papers in PubMed.

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290 more citing papers are in PubMed but not listed here.

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

2 authors.

Loren D WalenskyDepartment of Pediatric Oncology, Dana-Farber Cancer Institute , Boston, Massachusetts 02215, United States.
Gregory H Bird

Funding

YAC TECHNOLOGY IN THE REGULATION OF A LARGE GENE, BCL2R01CA050239 · NCI · WASHINGTON UNIVERSITY · PI WALENSKY, LOREN DAVID · 1989 to 2014
$4.3M
Stapled Antigens for HIV-1 VaccinationR01AI084102 · NIAID · DANA-FARBER CANCER INST · PI WALENSKY, LOREN DAVID · 2009 to 2012
$1.7M
NCI NIH HHS 5R01CA050239NCI NIH HHS R01 CA050239NIAID NIH HHS R01 AI084102NIAID NIH HHS R01AI084102NIGMS NIH HHS 5R01GM0902995
6 · The paper itself

Abstract

Protein structure underlies essential biological processes and provides a blueprint for molecular mimicry that drives drug discovery. Although small molecules represent the lion's share of agents that target proteins for therapeutic benefit, there remains no substitute for the natural properties of proteins and their peptide subunits in the majority of biological contexts. The peptide α-helix represents a common structural motif that mediates communication between signaling proteins. Because peptides can lose their shape when taken out of context, developing chemical interventions to stabilize their bioactive structure remains an active area of research. The all-hydrocarbon staple has emerged as one such solution, conferring α-helical structure, protease resistance, cellular penetrance, and biological activity upon successful incorporation of a series of design and application principles. Here, we describe our more than decade-long experience in developing stapled peptides as biomedical research tools and prototype therapeutics, highlighting lessons learned, pitfalls to avoid, and keys to success.

Indexed as

AlanineAnimalsBiomedical ResearchCross-Linking ReagentsHumansHydrocarbonsPeptide FragmentsPeptidesProtein Structure, SecondaryProtein UnfoldingProteolysisProto-Oncogene ProteinsStructure-Activity RelationshipAlanineBax protein (53-86)Cross-Linking ReagentsHydrocarbonsPeptide FragmentsPeptidesProto-Oncogene Proteins

Identifiers

PMID24601557
PMCPMC4136684

What OpenQuestion holds

Textmetadata
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.