Evidence map›Paper›PMID 37768271›Full record

ArticleProtein science : a publication of the Protein Society2023

CC

Prasun Kumar, Rokas Petrenas, William M Dawson, Hugo Schweke, Emmanuel D Levy, Derek N Woolfson

Abstract read
In one paragraph

Article in Protein science : a publication of the Protein Society, 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 5 papers.

0numbers the graph read from it
0cells of the map it votes in
5citing 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

5 citing papers in PubMed.

  1. Designability of α-Helical Protein Filaments.Sub-cellular biochemistry · 2026
    Review
  2. Chemical science · 2025
    Article
  3. Article
  4. Article
  5. CCProtein science : a publication of the Protein Society · 2023
    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.

Prasun KumarSchool of Chemistry, University of Bristol, Bristol, UK.ORCID 0000-0002-2008-3347
Rokas PetrenasSchool of Chemistry, University of Bristol, Bristol, UK.
William M DawsonSchool of Chemistry, University of Bristol, Bristol, UK.
Hugo SchwekeDepartment of Chemical and Structural Biology, Weizmann Institute of Science, Rehovot, Israel.
Emmanuel D LevyDepartment of Chemical and Structural Biology, Weizmann Institute of Science, Rehovot, Israel.
Derek N WoolfsonSchool of Chemistry, University of Bristol, Bristol, UK.ORCID 0000-0002-0394-3202

Funding

Biotechnology and Biological Sciences Research Council BB/L01386X/1Biotechnology and Biological Sciences Research Council BB/R00661X/1European Research Council 340764European Research Council 787173European Research Council 819318
6 · The paper itself

Abstract

α-Helical coiled coils are common tertiary and quaternary elements of protein structure. In coiled coils, two or more α helices wrap around each other to form bundles. This apparently simple structural motif can generate many architectures and topologies. Coiled coil-forming sequences can be predicted from heptad repeats of hydrophobic and polar residues, hpphppp, although this is not always reliable. Alternatively, coiled-coil structures can be identified using the program SOCKET, which finds knobs-into-holes (KIH) packing between side chains of neighboring helices. SOCKET also classifies coiled-coil architecture and topology, thus allowing sequence-to-structure relationships to be garnered. In 2009, we used SOCKET to create a relational database of coiled-coil structures, CC

Indexed as

ProteomeSoftwareProtein Conformation, alpha-HelicalProtein DomainsProtein Structure, SecondaryProteomeAlphaFold2bioinformaticscoiled coilprotein assemblyprotein designprotein engineeringprotein-structure analysis and modelingSOCKETSocket2structural biologyα helix

Identifiers

PMID37768271
PMCPMC10588367

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.