For Publishers
DiscoveryMetadataPeer reviewHostingPublishing
For Researchers
JoinPublishReviewCollect
Register
Blog
About
Search
Advanced search
My ScienceOpen
Search
For Publishers
For Researchers
Blog
About
9
views
107
references
 Top references
cited by
8
    
0 reviews
 Review
0
comments
 Comment
0
recommends
+1 Recommend
0 collections
    0
    shares
      175
      similar
       All similar
      • Record: found
      • Abstract: found
      • Article: found
      Is Open Access

      Challenges in the chemotherapy of Chagas disease: Looking for possibilities related to the differences and similarities between the parasite and host

      review-article

      Read this article at

      ScienceOpenPublisherPMC
      Bookmark
          There is no author summary for this article yet. Authors can add summaries to their articles on ScienceOpen to make them more accessible to a non-specialist audience.

          Abstract

          Almost 110 years after the first studies by Dr. Carlos Chagas describing an infectious disease that was named for him, Chagas disease remains a neglected illness and a death sentence for infected people in poor countries. This short review highlights the enormous need for new studies aimed at the development of novel and more specific drugs to treat chagasic patients. The primary tool for facing this challenge is deep knowledge about the similarities and differences between the parasite and its human host.

          Related collections

          Most cited references107

          • Record: found
          • Abstract: found
          • Article: not found

          Tracking the ends: a dynamic protein network controls the fate of microtubule tips.

          Anna Akhmanova, Michel Steinmetz (2008)
          Microtubule plus-end tracking proteins (+TIPs) are a diverse group of evolutionarily conserved cellular factors that accumulate at the ends of growing microtubules. They form dynamic networks through the interaction of a limited set of protein modules, repeat sequences and linear motifs that bind to each other with moderate affinities. +TIPs regulate different aspects of cell architecture by controlling microtubule dynamics, microtubule interactions with cellular structures and signalling factors, and the forces that are exerted on microtubule networks.
          Article 0 comments Cited 301 times – based on 0 reviews     Review now
            Bookmark
            • Record: found
            • Abstract: found
            • Article: not found

            Regulatory circuitry governing fungal development, drug resistance, and disease.

            Rebecca S. Shapiro, Nicole Robbins, Leah E. Cowen (2011)
            Pathogenic fungi have become a leading cause of human mortality due to the increasing frequency of fungal infections in immunocompromised populations and the limited armamentarium of clinically useful antifungal drugs. Candida albicans, Cryptococcus neoformans, and Aspergillus fumigatus are the leading causes of opportunistic fungal infections. In these diverse pathogenic fungi, complex signal transduction cascades are critical for sensing environmental changes and mediating appropriate cellular responses. For C. albicans, several environmental cues regulate a morphogenetic switch from yeast to filamentous growth, a reversible transition important for virulence. Many of the signaling cascades regulating morphogenesis are also required for cells to adapt and survive the cellular stresses imposed by antifungal drugs. Many of these signaling networks are conserved in C. neoformans and A. fumigatus, which undergo distinct morphogenetic programs during specific phases of their life cycles. Furthermore, the key mechanisms of fungal drug resistance, including alterations of the drug target, overexpression of drug efflux transporters, and alteration of cellular stress responses, are conserved between these species. This review focuses on the circuitry regulating fungal morphogenesis and drug resistance and the impact of these pathways on virulence. Although the three human-pathogenic fungi highlighted in this review are those most frequently encountered in the clinic, they represent a minute fraction of fungal diversity. Exploration of the conservation and divergence of core signal transduction pathways across C. albicans, C. neoformans, and A. fumigatus provides a foundation for the study of a broader diversity of pathogenic fungi and a platform for the development of new therapeutic strategies for fungal disease.
            Article 0 comments Cited 193 times – based on 0 reviews     Review now
              Bookmark
              • Record: found
              • Abstract: found
              • Article: not found

              An overview of tubulin inhibitors that interact with the colchicine binding site.

              Wei Li, David S Miller, Yan Lu … (2012)
              Tubulin dynamics is a promising target for new chemotherapeutic agents. The colchicine binding site is one of the most important pockets for potential tubulin polymerization destabilizers. Colchicine binding site inhibitors (CBSI) exert their biological effects by inhibiting tubulin assembly and suppressing microtubule formation. A large number of molecules interacting with the colchicine binding site have been designed and synthesized with significant structural diversity. CBSIs have been modified as to chemical structure as well as pharmacokinetic properties, and tested in order to find a highly potent, low toxicity agent for treatment of cancers. CBSIs are believed to act by a common mechanism via binding to the colchicine site on tubulin. The present review is a synopsis of compounds that have been reported in the past decade that have provided an increase in our understanding of the actions of CBSIs.
              Article 0 comments Cited 161 times – based on 0 reviews     Review now
                Bookmark
                All references

                Author and article information

                Journal
                Journal ID (nlm-ta): World J Biol Chem
                Journal ID (publisher-id): WJBC
                Title: World Journal of Biological Chemistry
                Publisher: Baishideng Publishing Group Inc
                ISSN (Electronic): 1949-8454
                Publication date (Print): 26 February 2017
                Publication date (Electronic): 26 February 2017
                Volume: 8
                Issue: 1
                Pages: 57-80
                Affiliations
                Vitor Sueth-Santiago, Instituto Federal de Educação, Ciência e Tecnologia do Rio de Janeiro, Campus São Gonçalo, Rua José Augusto Pereira dos Santos, São Gonçalo, CEP 24425-004, Brazil
                Vitor Sueth-Santiago, Marco Edilson Freire Lima, Universidade Federal Rural do Rio de Janeiro, Instituto de Ciências Exatas, Departamento de Química, Seropédica, CEP 23890-000, Brazil
                Debora Decote-Ricardo, Universidade Federal Rural do Rio de Janeiro, Instituto de Veterinária, Departamento de Microbiologia e Imunologia Veterinária, Seropédica, CEP 23890-000, Brazil
                Alexandre Morrot, Celio Geraldo Freire-de-Lima, Universidade Federal do Rio de Janeiro, Rio de Janeiro, CEP 21941-902, Brazil
                Author notes

                Author contributions: Sueth-Santiago V and Lima MEF wrote the paper; Decote-Ricardo D, Morrot A and Freire-de-Lima CG perfomed the collected the data.

                Correspondence to: Dr. Marco Edilson Freire Lima, Universidade Federal Rural do Rio de Janeiro, Instituto de Ciências Exatas, Departamento de Química, Rodovia BR 465, Km 7, Seropédica, CEP 23890-000, Brazil. marco@ 123456ufrrj.br

                Telephone: +55-21-25626523 Fax: +55-21-22808193

                Article
                Other ID: jWJBC.v8.i1.pg57
                DOI: 10.4331/wjbc.v8.i1.57
                PMC ID: 5329715
                PubMed ID: 28289519
                SO-VID: a36e1a48-4e39-48f5-a5cd-1be6119058b9
                Copyright © ©The Author(s) 2017. Published by Baishideng Publishing Group Inc. All rights reserved.
                License:

                This article is an open-access article which was selected by an in-house editor and fully peer-reviewed by external reviewers. It is distributed in accordance with the Creative Commons Attribution Non Commercial (CC BY-NC 4.0) license, which permits others to distribute, remix, adapt, build upon this work non-commercially, and license their derivative works on different terms, provided the original work is properly cited and the use is non-commercial.

                History
                Date received : 27 August 2016
                Date revision received : 30 December 2016
                Date accepted : 11 January 2017
                Categories
                Subject: Review

                Keywords: trypanosoma cruzi,trans-sialidase,trypanothione reductase,cyp51,cruzipain,tubulin
                Data availability:
                Keywords: trypanosoma cruzi, trans-sialidase, trypanothione reductase, cyp51, cruzipain, tubulin

                Comments

                Comment on this article

                scite_

                Similar content175

                See all similar

                Cited by8

                See all cited by

                Most referenced authors1,727

                See all reference authors