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CATHEPSIN D
Known as:
CTSD
, Cathepsin D [Chemical/Ingredient]
, Cathepsin D (Lysosomal Aspartyl Protease)
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An intracellular proteinase found in a variety of tissue. It has specificity similar to but narrower than that of pepsin A. The enzyme is involved in…
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National Institutes of Health
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Related topics
Related topics
30 relations
Angiogenic Process
Aspartic Acid Proteases
Breast Carcinoma
CTSD gene
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Broader (1)
Aspartic Acid Endopeptidases
Narrower (5)
Ctsd protein, mouse
NEURONAL CEROID LIPOFUSCINOSIS DUE TO CATHEPSIN D DEFICIENCY
procathepsin D
short recombinant human pseudocathepsin D
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Papers overview
Semantic Scholar uses AI to extract papers important to this topic.
Highly Cited
2017
Highly Cited
2017
Progranulin functions as a cathepsin D chaperone to stimulate axonal outgrowth in vivo
S. Beel
,
M. Moisse
,
+5 authors
P. van Damme
Human Molecular Genetics
2017
Corpus ID: 205104247
Abstract Loss of function mutations in progranulin (GRN) cause frontotemporal dementia, but how GRN haploinsufficiency causes…
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Highly Cited
2011
Highly Cited
2011
AGR2 is a novel surface antigen that promotes the dissemination of pancreatic cancer cells through regulation of cathepsins B and D.
Laurent Dumartin
,
Hannah J. Whiteman
,
+10 authors
T. Crnogorac-Jurcevic
Cancer Research
2011
Corpus ID: 1410896
Pancreatic ductal adenocarcinoma (PDAC) remains one of the most lethal cancers largely due to disseminated disease at the time of…
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Highly Cited
2010
Highly Cited
2010
Osteopontin Is Cleaved at Multiple Sites Close to Its Integrin-binding Motifs in Milk and Is a Novel Substrate for Plasmin and Cathepsin D*
B. Christensen
,
L. Schack
,
E. Kläning
,
E. S. Sørensen
Journal of Biological Chemistry
2010
Corpus ID: 205297204
Osteopontin (OPN) is a highly modified integrin-binding protein present in most tissues and body fluids where it has been…
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Highly Cited
2006
Highly Cited
2006
Cathepsin D deficiency is associated with a human neurodegenerative disorder.
R. Steinfeld
,
K. Reinhardt
,
+5 authors
J. Gartner
American Journal of Human Genetics
2006
Corpus ID: 41201738
Cathepsin D is a ubiquitously expressed lysosomal protease that is involved in proteolytic degradation, cell invasion, and…
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Highly Cited
2004
Highly Cited
2004
Cathepsin D links TNF-induced acid sphingomyelinase to Bid-mediated caspase-9 and -3 activation
M. Heinrich
,
J. Neumeyer
,
+8 authors
S. Schütze
Cell Death and Differentiation
2004
Corpus ID: 20449746
AbstractAcidic noncaspase proteases-like cathepsins have been introduced as novel mediators of apoptosis. A clear role for these…
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Highly Cited
2000
Highly Cited
2000
Ceramide as an activator lipid of cathepsin D.
M. Heinrich
,
M. Wickel
,
+9 authors
S. Schütze
Advances in Experimental Medicine and Biology
2000
Corpus ID: 44906439
We have identified the aspartic protease cathepsin D as a novel intracellular target protein for the lipid second messenger…
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Highly Cited
1998
Highly Cited
1998
Mutant Rab7 Causes the Accumulation of Cathepsin D and Cation-independent Mannose 6–Phosphate Receptor in an Early Endocytic Compartment
B. Press
,
Yan Feng
,
B. Hoflack
,
A. Wandinger-Ness
Journal of Cell Biology
1998
Corpus ID: 3070038
Stable BHK cell lines inducibly expressing wild-type or dominant negative mutant forms of the rab7 GTPase were isolated and used…
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Highly Cited
1994
Highly Cited
1994
Characterization of the proximal estrogen-responsive element of human cathepsin D gene.
P. Augereau
,
F. Miralles
,
V. Cavaillès
,
C. Gaudelet
,
M. Parker
,
H. Rochefort
Molecular Endocrinology
1994
Corpus ID: 2205105
Cathepsin D, a lysosomal proteinase, is induced by estrogens in mammary cancer cells where its concentration is correlated with a…
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Highly Cited
1976
Highly Cited
1976
The effects of proteolytic enzymes on the mechanical properties of adult human articular cartilage.
G. Kempson
,
M. Tuke
,
J. Dingle
,
A. J. Barrett
,
P. Horsfield
Biochimica et Biophysica Acta
1976
Corpus ID: 36999387
Highly Cited
1971
Highly Cited
1971
Cathepsin D. Characteristics of immunoinhibition and the confirmation of a role in cartilage breakdown.
J. Dingle
,
A. J. Barrett
,
P. Weston
Biochemical Journal
1971
Corpus ID: 24394470
1. Antisera were raised against lysosomal cathepsin D of man, chicken and rabbit. 2. The antisera were found to be specific and…
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