Evidence map›Paper›PMID 25861761›Full record

ArticleJournal of molecular biology2015

The response of Greek key proteins to changes in connectivity depends on the nature of their secondary structure.

Katherine R Kemplen, David De Sancho, Jane Clarke

Open access · hybridAbstract read
In one paragraph

Article in Journal of molecular biology, 2015. 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
0.2field-weighted citation impact, top 44% 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

5 citing papers in PubMed, 10 citations in OpenAlex.

  1. Article
  2. Article
  3. Circular permutation at azurin's active site slows down its folding.Journal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry · 2023
    Article
  4. Article
  5. 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

3 authors at 1 institution in 1 country.

Katherine R KemplenUniversity of Cambridge Department of Chemistry, Lensfield Road, Cambridge CB2 1EW, UK.
David De SanchoUniversity of Cambridge Department of Chemistry, Lensfield Road, Cambridge CB2 1EW, UK.
Jane ClarkeUniversity of Cambridge Department of Chemistry, Lensfield Road, Cambridge CB2 1EW, UK. Electronic address: jc162@cam.ac.uk.
University of Cambridge · GB

Funding

Wellcome Trust 095195
6 · The paper itself

Abstract

What governs the balance between connectivity and topology in regulating the mechanism of protein folding? We use circular permutation to vary the order of the helices in the all-α Greek key protein FADD (Fas-associated death domain) to investigate this question. Unlike all-β Greek key proteins, where changes in the order of secondary structure cause a shift in the folding nucleus, the position of the nucleus in FADD is unchanged, even when permutation reduces the complexity significantly. We suggest that this is because local helical contacts are so dominant that permutation has little effect on the entropic cost of forming the folding nucleus whereas, in all-β Greek key proteins, all interactions in the nucleus are long range. Thus, the type of secondary structure modulates the sensitivity of proteins to changes in connectivity.

Indexed as

Protein FoldingFas-Associated Death Domain ProteinModels, MolecularProtein Structure, SecondaryFas-Associated Death Domain Proteindeath domainimmunoglobulin foldphi-valueprotein foldingtopology

Identifiers

PMID25861761
PMCPMC4451459
OpenAlexW2073876360

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.