Controlling proteolysis of Clp peptidase: a possible target for combating mitochondrial diseases

Bibliographic Details
Main Author: da Silva, Ronivaldo Rodrigues [UNESP]
Publication Date: 2019
Format: Other
Language: eng
Source: Repositório Institucional da UNESP
Download full: http://dx.doi.org/10.1016/j.biocel.2019.03.007
http://hdl.handle.net/11449/187460
Summary: Some mechanisms of cellular stress, aging, and apoptosis are related to proteolysis. With respect to ClpP, little is known about the mechanical manner in which the substrate is hydrolyzed in and released from the degradation chamber. Furthermore, what would be the real influence of ClpP in mammalian UPR mt ?
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spelling Controlling proteolysis of Clp peptidase: a possible target for combating mitochondrial diseasesCellular functionChaperoneProteaseProteostasisSome mechanisms of cellular stress, aging, and apoptosis are related to proteolysis. With respect to ClpP, little is known about the mechanical manner in which the substrate is hydrolyzed in and released from the degradation chamber. Furthermore, what would be the real influence of ClpP in mammalian UPR mt ?Instituto de Biociências Letras e Ciências Exatas Universidade Estadual Paulista Júlio de Mesquita Filho (UNESP), São José do Rio PretoInstituto de Biociências Letras e Ciências Exatas Universidade Estadual Paulista Júlio de Mesquita Filho (UNESP), São José do Rio PretoUniversidade Estadual Paulista (Unesp)da Silva, Ronivaldo Rodrigues [UNESP]2019-10-06T15:36:47Z2019-10-06T15:36:47Z2019-05-01info:eu-repo/semantics/publishedVersioninfo:eu-repo/semantics/other140-142http://dx.doi.org/10.1016/j.biocel.2019.03.007International Journal of Biochemistry and Cell Biology, v. 110, p. 140-142.1878-58751357-2725http://hdl.handle.net/11449/18746010.1016/j.biocel.2019.03.0072-s2.0-85062893393Scopusreponame:Repositório Institucional da UNESPinstname:Universidade Estadual Paulista (UNESP)instacron:UNESPengInternational Journal of Biochemistry and Cell Biologyinfo:eu-repo/semantics/openAccess2025-04-03T19:00:56Zoai:repositorio.unesp.br:11449/187460Repositório InstitucionalPUBhttp://repositorio.unesp.br/oai/requestrepositoriounesp@unesp.bropendoar:29462025-04-03T19:00:56Repositório Institucional da UNESP - Universidade Estadual Paulista (UNESP)false
dc.title.none.fl_str_mv Controlling proteolysis of Clp peptidase: a possible target for combating mitochondrial diseases
title Controlling proteolysis of Clp peptidase: a possible target for combating mitochondrial diseases
spellingShingle Controlling proteolysis of Clp peptidase: a possible target for combating mitochondrial diseases
da Silva, Ronivaldo Rodrigues [UNESP]
Cellular function
Chaperone
Protease
Proteostasis
title_short Controlling proteolysis of Clp peptidase: a possible target for combating mitochondrial diseases
title_full Controlling proteolysis of Clp peptidase: a possible target for combating mitochondrial diseases
title_fullStr Controlling proteolysis of Clp peptidase: a possible target for combating mitochondrial diseases
title_full_unstemmed Controlling proteolysis of Clp peptidase: a possible target for combating mitochondrial diseases
title_sort Controlling proteolysis of Clp peptidase: a possible target for combating mitochondrial diseases
author da Silva, Ronivaldo Rodrigues [UNESP]
author_facet da Silva, Ronivaldo Rodrigues [UNESP]
author_role author
dc.contributor.none.fl_str_mv Universidade Estadual Paulista (Unesp)
dc.contributor.author.fl_str_mv da Silva, Ronivaldo Rodrigues [UNESP]
dc.subject.por.fl_str_mv Cellular function
Chaperone
Protease
Proteostasis
topic Cellular function
Chaperone
Protease
Proteostasis
description Some mechanisms of cellular stress, aging, and apoptosis are related to proteolysis. With respect to ClpP, little is known about the mechanical manner in which the substrate is hydrolyzed in and released from the degradation chamber. Furthermore, what would be the real influence of ClpP in mammalian UPR mt ?
publishDate 2019
dc.date.none.fl_str_mv 2019-10-06T15:36:47Z
2019-10-06T15:36:47Z
2019-05-01
dc.type.status.fl_str_mv info:eu-repo/semantics/publishedVersion
dc.type.driver.fl_str_mv info:eu-repo/semantics/other
format other
status_str publishedVersion
dc.identifier.uri.fl_str_mv http://dx.doi.org/10.1016/j.biocel.2019.03.007
International Journal of Biochemistry and Cell Biology, v. 110, p. 140-142.
1878-5875
1357-2725
http://hdl.handle.net/11449/187460
10.1016/j.biocel.2019.03.007
2-s2.0-85062893393
url http://dx.doi.org/10.1016/j.biocel.2019.03.007
http://hdl.handle.net/11449/187460
identifier_str_mv International Journal of Biochemistry and Cell Biology, v. 110, p. 140-142.
1878-5875
1357-2725
10.1016/j.biocel.2019.03.007
2-s2.0-85062893393
dc.language.iso.fl_str_mv eng
language eng
dc.relation.none.fl_str_mv International Journal of Biochemistry and Cell Biology
dc.rights.driver.fl_str_mv info:eu-repo/semantics/openAccess
eu_rights_str_mv openAccess
dc.format.none.fl_str_mv 140-142
dc.source.none.fl_str_mv Scopus
reponame:Repositório Institucional da UNESP
instname:Universidade Estadual Paulista (UNESP)
instacron:UNESP
instname_str Universidade Estadual Paulista (UNESP)
instacron_str UNESP
institution UNESP
reponame_str Repositório Institucional da UNESP
collection Repositório Institucional da UNESP
repository.name.fl_str_mv Repositório Institucional da UNESP - Universidade Estadual Paulista (UNESP)
repository.mail.fl_str_mv repositoriounesp@unesp.br
_version_ 1834482573120634880

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