Activity and expression of Candida glabrata vacuolar proteases in autophagy-like conditions-Reference-Cited by-同舟云学术

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Activity and expression of Candida glabrata vacuolar proteases in autophagy-like conditions

Published:2018-01-29 Issue:2 Volume:18 Page:
ISSN:1567-1364
Container-title:FEMS Yeast Research
language:en
Short-container-title:

Author:

Cortez-Sánchez J Luis¹,Cortés-Acosta Elías¹,Cueto-Hernández V Mónica¹,Reyes-Maldonado Elba²,Hernández-Rodríguez César¹,Villa-Tanaca Lourdes¹,Ibarra J Antonio¹

Affiliation:

1. Departamento de Microbiología, Escuela Nacional de Ciencias Biológicas, Instituto Politécnico Nacional, Delegación Miguel Hidalgo, Ciudad de México CP 11340, México

2. Departamento de Morfología, Escuela Nacional de Ciencias Biológicas, Instituto Politécnico Nacional, Delegación Miguel Hidalgo, Ciudad de México CP 11340, México

Funder

CONACYT

SIP-IPN

Publisher

Oxford University Press (OUP)

Subject

Applied Microbiology and Biotechnology,General Medicine,Microbiology

Link

http://academic.oup.com/femsyr/article-pdf/18/2/foy006/24341597/foy006.pdf

Reference45 articles.

1. Yeast vacuoles: more than a model lysosome;Armstrong;Trends Cell Biol,2010

2. Ultrastrucmral analysis of the autophagic process in yeast: detection of autophagosomes and their characterization;Baba;J Cell Biol,1994

3. Nitrogen source and growth stage of Candida albicans influence expression level of vacuolar aspartic protease Apr1p and carboxypeptidase Cpy1p;Bauerová;Can J Microbiol,2012

4. A large-scale analysis of autophagy-related gene expression identifies new regulators of autophagy;Bernard;Autophagy,2015

5. Biology of the pathogenic yeastCandida glabrata;Bialková;Folia Microbiol,2006

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1. Vacuolar proteases and autophagy in phytopathogenic fungi: A review;Frontiers in Fungal Biology;2022-10-26

2. The Salmonella Typhimurium InvF-SicA complex is necessary for the transcription of sopB in the absence of the repressor H-NS;PLOS ONE;2020-10-29

3. Heterologous expression and characterization of the aspartic endoprotease Pep4um from Ustilago maydis, a homolog of the human Chatepsin D, an important breast cancer therapeutic target;Molecular Biology Reports;2018-08-03

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