Evidence map›Paper›PMID 27054066›Full record

ArticleInternational journal for parasitology. Drugs and drug resistance2016

Scaffold proteins LACK and TRACK as potential drug targets in kinetoplastid parasites: Development of inhibitors.

Nir Qvit, Deborah Schechtman, Darlene Aparecida Pena, Denise Aparecida Berti, Chrislaine Oliveira Soares, Qianqian Miao, Liying Annie Liang, Lauren A Baron, Christian Teh-Poot, Pedro Martínez-Vega and 12 more

Open access · goldAbstract read
In one paragraph

Article in International journal for parasitology. Drugs and drug resistance, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 4 papers.

0numbers the graph read from it
0cells of the map it votes in
4citing papers in PubMed
1.5field-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

4 citing papers in PubMed, 16 citations in OpenAlex.

  1. Review
  2. Article
  3. Review
  4. Review
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

22 authors at 7 institutions in 4 countries.

Nir QvitDepartment of Chemical and Systems Biology, Stanford University, School of Medicine, Stanford, CA 94305, USA. Electronic address: nirqvit@stanford.edu.
Deborah SchechtmanDepartment of Chemical and Systems Biology, Stanford University, School of Medicine, Stanford, CA 94305, USA; Departamento de Bioquímica, Instituto de Química, Universidade de São Paulo, SP, Brazil.
Darlene Aparecida PenaDepartamento de Bioquímica, Instituto de Química, Universidade de São Paulo, SP, Brazil.
Denise Aparecida BertiDepartamento de Bioquímica, Instituto de Química, Universidade de São Paulo, SP, Brazil.
Chrislaine Oliveira SoaresDepartamento de Bioquímica, Instituto de Química, Universidade de São Paulo, SP, Brazil.
Qianqian MiaoNational Reference Centre for Parasitology, Research Institute of the McGill University, Montreal, Canada.
Liying Annie LiangNational Reference Centre for Parasitology, Research Institute of the McGill University, Montreal, Canada.
Lauren A BaronLaboratorio de Parasitología, Centro de Investigaciones Regionales "Dr. Hideyo Noguchi", Universidad Autónoma de Yucatán, Mérida, Yucatán, Mexico.
Christian Teh-PootLaboratorio de Parasitología, Centro de Investigaciones Regionales "Dr. Hideyo Noguchi", Universidad Autónoma de Yucatán, Mérida, Yucatán, Mexico.
Pedro Martínez-VegaLaboratorio de Parasitología, Centro de Investigaciones Regionales "Dr. Hideyo Noguchi", Universidad Autónoma de Yucatán, Mérida, Yucatán, Mexico.
Maria Jesus Ramirez-SierraLaboratorio de Parasitología, Centro de Investigaciones Regionales "Dr. Hideyo Noguchi", Universidad Autónoma de Yucatán, Mérida, Yucatán, Mexico.
Eric ChurchillDepartment of Chemical and Systems Biology, Stanford University, School of Medicine, Stanford, CA 94305, USA.
Anna D CunninghamDepartment of Chemical and Systems Biology, Stanford University, School of Medicine, Stanford, CA 94305, USA.
Andrey V MalkovskiyBiomaterials and Advanced Drug Delivery Laboratory, Stanford University, Stanford, CA 94305, USA.
Nancy A FederspielDepartment of Chemical and Systems Biology, Stanford University, School of Medicine, Stanford, CA 94305, USA.
Fabio Cesar GozzoInstitute of Chemistry, University of Campinas, Campinas, SP, Brazil.
Ana Claudia TorrecilhasDepartamento de Ciências Biológicas, Campus Diadema, UNIFESP, Brazil.
Maria Julia Manso AlvesDepartamento de Bioquímica, Instituto de Química, Universidade de São Paulo, SP, Brazil.
Armando JardimInstitute of Parasitology and Centre for Host-Parasite Interactions, McGill University, Québec, Canada.
Ndao MomarNational Reference Centre for Parasitology, Research Institute of the McGill University, Montreal, Canada.
Eric DumonteilLaboratorio de Parasitología, Centro de Investigaciones Regionales "Dr. Hideyo Noguchi", Universidad Autónoma de Yucatán, Mérida, Yucatán, Mexico.
Daria Mochly-RosenDepartment of Chemical and Systems Biology, Stanford University, School of Medicine, Stanford, CA 94305, USA.
Stanford University · USAutonomous University of Yucatán · MXUniversidade de São Paulo · BRMcGill University · CAMcGill University Health Centre · CAUniversidade Estadual de Campinas (UNICAMP) · BRUniversidade Federal de São Paulo · BR

Funding

Protein Kinase C Isozymes in Ischemic HeartR01HL052141 · NHLBI · STANFORD UNIVERSITY · PI MOCHLY-ROSEN, DARIA · 1996 to 2021
$8.5M
Stanford Global Health Consortium: Innovation, Design, Evaluation, and ActionRC4TW008781 · FIC · STANFORD UNIVERSITY · PI BARRY, MICHELE · 2010 to 2010
$8.1M
Interfering with Protein-Protein Interaction for the Treatment of LeishmaniasisR21AI078505 · NIAID · STANFORD UNIVERSITY · PI MOCHLY-ROSEN, DARIA · 2008 to 2009
$442k
FIC NIH HHS RC4 TW008781NHLBI NIH HHS R01 HL052141NIAID NIH HHS AI078505NIAID NIH HHS R21 AI078505PHS HHS TW008781-01C-IDEA
6 · The paper itself

Abstract

Parasitic diseases cause ∼ 500,000 deaths annually and remain a major challenge for therapeutic development. Using a rational design based approach, we developed peptide inhibitors with anti-parasitic activity that were derived from the sequences of parasite scaffold proteins LACK (Leishmania's receptor for activated C-kinase) and TRACK (Trypanosoma receptor for activated C-kinase). We hypothesized that sequences in LACK and TRACK that are conserved in the parasites, but not in the mammalian ortholog, RACK (Receptor for activated C-kinase), may be interaction sites for signaling proteins that are critical for the parasites' viability. One of these peptides exhibited leishmanicidal and trypanocidal activity in culture. Moreover, in infected mice, this peptide was also effective in reducing parasitemia and increasing survival without toxic effects. The identified peptide is a promising new anti-parasitic drug lead, as its unique features may limit toxicity and drug-resistance, thus overcoming central limitations of most anti-parasitic drugs.

Indexed as

Amino Acid SequenceAnimalsAntigens, ProtozoanDrug DesignLeishmaniaLeishmaniasisMiceParasitemiaPeptidesProtozoan ProteinsReceptors, Cell SurfaceReceptors for Activated C KinaseSequence AlignmentTrypanocidal AgentsTrypanosomaTrypanosomiasisAntigens, ProtozoanLACK antigen, LeishmaniaPeptidesProtozoan ProteinsReceptors, Cell SurfaceReceptors for Activated C KinaseTrypanocidal AgentsChagas diseaseLACKLeishmaniasisPeptideScaffold proteinTRACK

Identifiers

PMID27054066
PMCPMC4805777
OpenAlexW2280492033

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC-ND
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.