Evidence map›Paper›PMID 12142442›Full record

ArticleProtein science : a publication of the Protein Society2002

Crucial stages of protein folding through a solvable model: predicting target sites for enzyme-inhibiting drugs.

Cristian Micheletti, Fabio Cecconi, Alessandro Flammini, Amos Maritan

Open access · greenAbstract read
In one paragraph

Article in Protein science : a publication of the Protein Society, 2002. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 6 papers.

0numbers the graph read from it
0cells of the map it votes in
6citing papers in PubMed
0.9field-weighted citation impact, top 26% 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

6 citing papers in PubMed, 22 citations in OpenAlex.

  1. Article
  2. Temperature dependence of fluctuations in HIV1-protease.European biophysics journal : EBJ · 2010
    Article
  3. Article
  4. Article
  5. Article
  6. Protein flexibility prediction by an all-atom mean-field statistical theory.Protein science : a publication of the Protein Society · 2005
    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

4 authors at 1 institution in 1 country.

Cristian MichelettiInternational School for Advanced Studies (SISSA/ISAS), I-34014 Trieste, Italy. michelet@sissa.it
Fabio Cecconi
Alessandro Flammini
Amos Maritan
Scuola Internazionale Superiore di Studi Avanzati · IT

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

An exactly solvable model based on the topology of a protein native state is applied to identify bottlenecks and key sites for the folding of human immunodeficiency virus type 1 (HIV-1) protease. The predicted sites are found to correlate well with clinical data on resistance to Food and Drug Administration-approved drugs. It has been observed that the effects of drug therapy are to induce multiple mutations on the protease. The sites where such mutations occur correlate well with those involved in folding bottlenecks identified through the deterministic procedure proposed in this study. The high statistical significance of the observed correlations suggests that the approach may be promisingly used in conjunction with traditional techniques to identify candidate locations for drug attacks.

Indexed as

Protein FoldingAmino AcidsDrug DesignHIV-1HIV ProteaseHIV Protease InhibitorsHumansModels, MolecularPoint MutationProtein ConformationStatistics as TopicThermodynamicsAmino AcidsHIV ProteaseHIV Protease Inhibitors

Identifiers

PMID12142442
PMCPMC2373687
OpenAlexW2160276969

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.