The lysosomal protein cathepsin L is a progranulin protease

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Location: Deutsche Nationalbibliothek Frankfurt am Main

ISSN: 1750-1326

Extent: Online-Ressource

Language: Englisch

Notes: online resource.

Bibliographic citation: The lysosomal protein cathepsin L is a progranulin protease ; volume:12 ; number:1 ; day:25 ; month:7 ; year:2017 ; pages:1-9 ; date:12.2017
Molecular neurodegeneration ; 12, Heft 1 (25.7.2017), 1-9, 12.2017

Keyword: Histologie
Cytologie

Creator: Lee, Chris W.

Contributor: Stankowski, Jeannette N.
Chew, Jeannie
Cook, Casey N.
Lam, Ying-Wai
Almeida, Sandra
Carlomagno, Yari
Lau, Kwok-Fai
Prudencio, Mercedes
Gao, Fen-Biao
Bogyo, Matthew
Dickson, Dennis W.
Petrucelli, Leonard
SpringerLink (Online service)

DOI: 10.1186/s13024-017-0196-6

URN: urn:nbn:de:1111-201710067005

Rights: Der Zugriff auf das Objekt ist unbeschränkt möglich.

Last update: 15.08.2025, 7:28 AM CEST

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Associated

Lee, Chris W.
Stankowski, Jeannette N.
Chew, Jeannie
Cook, Casey N.
Lam, Ying-Wai
Almeida, Sandra
Carlomagno, Yari
Lau, Kwok-Fai
Prudencio, Mercedes
Gao, Fen-Biao
Bogyo, Matthew
Dickson, Dennis W.
Petrucelli, Leonard
SpringerLink (Online service)

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The lysosomal protein cathepsin L is a progranulin protease

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Other Objects (12)

The neuropathological diagnosis of Alzheimer’s disease

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Cellular and pathological heterogeneity of primary tauopathies

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Neuropathology and molecular diagnosis of Synucleinopathies

Altered microRNA expression in frontotemporal lobar degeneration with TDP-43 pathology caused by progranulin mutations

Lysosomal dysfunction and microglial hyperactivation in models of progranulin deficiency

Genetic dissection of cell-type specific functions of the lysosomal protease Cathepsin L in breast cancer progression

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Cellular and pathological heterogeneity of primary tauopathies

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Altered microRNA expression in frontotemporal lobar degeneration with TDP-43 pathology caused by progranulin mutations

Lysosomal dysfunction and microglial hyperactivation in models of progranulin deficiency

Genetic dissection of cell-type specific functions of the lysosomal protease Cathepsin L in breast cancer progression

Proaggregant nuclear factor(s) trigger rapid formation of α-synuclein aggregates in apoptotic neurons

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C-terminal and full length TDP-43 specie differ according to FTLD-TDP lesion type but not genetic mutation

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Pathogenic functions of the lysosomal protease cathepsin B in murine invasive breast cancer

Inhibition of cysteine protease cathepsin Lincreases the level and activity of lysosomal glucocerebrosidase

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