Evidence map›Paper›PMID 18201565›Full record

ArticleFEBS letters2008

The role of conserved residues of chagasin in the inhibition of cysteine peptidases.

Flavia C G dos Reis, Brian O Smith, Camila C Santos, Tatiana F R Costa, Julio Scharfstein, Graham H Coombs, Jeremy C Mottram, Ana Paula C A Lima

Open access · hybridAbstract read
In one paragraph

Article in FEBS letters, 2008. 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
1.8field-weighted citation impact, top 15% 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, 20 citations in OpenAlex.

  1. Article
  2. Investigations into PoyH, a promiscuous protease from polytheonamide biosynthesis.Journal of industrial microbiology & biotechnology · 2019
    Article
  3. Article
  4. Review
  5. Article
  6. 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

8 authors at 4 institutions in 2 countries.

Flavia C G dos ReisInstituto de Biofísica Carlos Chagas Filho, Universidade Federal do Rio de Janeiro, Bloco G, C.C.S., Cidade Universitária, Ilha do Fundão, Rio de Janeiro, 21949-900 RJ, Brazil.
Brian O Smith
Camila C Santos
Tatiana F R Costa
Julio Scharfstein
Graham H Coombs
Jeremy C Mottram
Ana Paula C A Lima
Universidade Federal do Rio de Janeiro · BRWellcome Centre for Molecular Parasitology · GBUniversity of Glasgow · GBUniversity of Strathclyde · GB

Funding

Medical Research Council G9722968Medical Research Council G9722968(65078)Wellcome Trust 081877
6 · The paper itself

Abstract

We have evaluated the roles of key amino acids to the action of the natural inhibitor chagasin of papain-family cysteine peptidases. A W93A substitution decreased inhibitor affinity for human cathepsin L 100-fold, while substitutions of T31 resulted in 10-100-fold increases in the K(i) for cruzipain of Trypanosoma cruzi. A T31A/T32A double mutant had increased affinity for cathepsin L but not for cruzipain, while the T31-T32 deletion drastically affected inhibition of both human and parasite peptidases. These differential effects reflect the occurrence of direct interactions between chagasin and helix 8 of cathepsin L, interactions that do not occur with cruzipain.

Indexed as

Conserved SequenceAmino Acid SequenceAnimalsBase SequenceCysteine Proteinase InhibitorsDNA PrimersMolecular Sequence DataMutagenesis, Site-DirectedProtozoan ProteinsSequence Homology, Amino AcidTrypanosoma cruzichagasin, TrypanosomaCysteine Proteinase InhibitorsDNA PrimersProtozoan Proteins

Identifiers

PMID18201565
PMCPMC2607524
OpenAlexW2120472021

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.