Literature DB >> 24703183

No stress--Hsp90 and signal transduction in Leishmania.

A Hombach1, J Clos1.   

Abstract

SUMMARY Hsp90 (a.k.a. Hsp83) plays a significant role in the life cycle control of the protozoan parasite Leishmania donovani. Rather than protecting Leishmania spp. against adverse and stressful environs, Hsp90 is required for the maintenance of the motile, highly proliferative insect stage, the promastigote. However, Hsp90 is also essential for survival and proliferation of the intracellular mammalian stage, the amastigote. Moreover, recent evidence shows Hsp90 and other components of large multi-chaperone complexes as substrates of stage-specific protein phosphorylation pathways, and thus as likely effectors of the signal transduction pathways in Leishmania spp. Future efforts should be directed towards the identification of the protein kinases and the critical phosphorylation sites as targets for novel therapeutic approaches.

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Year:  2014        PMID: 24703183     DOI: 10.1017/S0031182013002151

Source DB:  PubMed          Journal:  Parasitology        ISSN: 0031-1820            Impact factor:   3.234


  13 in total

Review 1.  Heat Shock Proteins as the Druggable Targets in Leishmaniasis: Promises and Perils.

Authors:  Pragya Prasanna; Arun Upadhyay
Journal:  Infect Immun       Date:  2021-01-19       Impact factor: 3.441

2.  Unraveling of interacting protein network of chaperonin TCP1 gamma subunit of Leishmania donovani.

Authors:  Shailendra Yadav; Apeksha Anand; Karthik Ramalingam; Deep Chandra Balodi; Jaswinder Singh Maras; Neena Goyal
Journal:  Cell Stress Chaperones       Date:  2022-02-23       Impact factor: 3.827

Review 3.  Molecular Chaperones of Leishmania: Central Players in Many Stress-Related and -Unrelated Physiological Processes.

Authors:  Jose M Requena; Ana M Montalvo; Jorge Fraga
Journal:  Biomed Res Int       Date:  2015-06-18       Impact factor: 3.411

4.  Simultaneous transcriptional profiling of Leishmania major and its murine macrophage host cell reveals insights into host-pathogen interactions.

Authors:  Laura A L Dillon; Rahul Suresh; Kwame Okrah; Hector Corrada Bravo; David M Mosser; Najib M El-Sayed
Journal:  BMC Genomics       Date:  2015-12-29       Impact factor: 3.969

5.  Modeling Immune Response to Leishmania Species Indicates Adenosine As an Important Inhibitor of Th-Cell Activation.

Authors:  Henrique A L Ribeiro; Tatiani U Maioli; Leandro M de Freitas; Paolo Tieri; Filippo Castiglione
Journal:  Front Cell Infect Microbiol       Date:  2017-07-20       Impact factor: 5.293

6.  The heat shock protein 90 of Toxoplasma gondii is essential for invasion of host cells and tachyzoite growth.

Authors:  Hongchao Sun; Xunhui Zhuo; Xianfeng Zhao; Yi Yang; Xueqiu Chen; Chaoqun Yao; Aifang Du
Journal:  Parasite       Date:  2017-06-19       Impact factor: 3.000

7.  Biophysical analysis of Plasmodium falciparum Hsp70-Hsp90 organising protein (PfHop) reveals a monomer that is characterised by folded segments connected by flexible linkers.

Authors:  Stanley Makumire; Tawanda Zininga; Juha Vahokoski; Inari Kursula; Addmore Shonhai
Journal:  PLoS One       Date:  2020-04-28       Impact factor: 3.240

8.  A small heat shock protein is essential for thermotolerance and intracellular survival of Leishmania donovani.

Authors:  Antje Hombach; Gabi Ommen; Andrea MacDonald; Joachim Clos
Journal:  J Cell Sci       Date:  2014-09-01       Impact factor: 5.285

9.  MAPK1 of Leishmania donovani interacts and phosphorylates HSP70 and HSP90 subunits of foldosome complex.

Authors:  Pavneet Kaur; Mansi Garg; Antje Hombach-Barrigah; Joachim Clos; Neena Goyal
Journal:  Sci Rep       Date:  2017-08-31       Impact factor: 4.379

10.  Discovery of small molecule inhibitors of Leishmania braziliensis Hsp90 chaperone.

Authors:  Fernanda A H Batista; Sérgio L Ramos; Giusy Tassone; Andrei Leitão; Carlos A Montanari; Maurizio Botta; Mattia Mori; Júlio C Borges
Journal:  J Enzyme Inhib Med Chem       Date:  2020-12       Impact factor: 5.051

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