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cathepsin D
This gene encodes a lysosomal aspartyl protease composed of a dimer of disulfide-linked heavy and light chains, both produced from a single protein precursor. This proteinase, which is a member of the peptidase C1 family, has a specificity similar to but narrower than that of pepsin A. Transcription of this gene is initiated from several sites, including one which is a start site for an estrogen-regulated transcript. Mutations in this gene are involved in the pathogenesis of several diseases, including breast cancer and possibly Alzheimer disease. [provided by RefSeq]
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|---|---|---|---|
| Fat body |
100
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| Set of fingers |
97
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| Epidermis |
94
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| Trigeminal ganglion |
87
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| Urinary bladder |
86
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| Cecum |
84
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|---|---|---|---|
| Meloxicam |
100
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| Fulvestrant |
96
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| Spironolactone |
95
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| Sandoglobulin |
92
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| Nystatin A1 |
90
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| Ethylestrenol |
89
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Individual Studies |
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Authors: Denise Hilfiker-Kleiner, Karol Kaminski, Edith Podewski, Tomasz Bonda, Arnd Schaefer, Karen Sliwa, Olaf Forster, Anja Quint, Ulf Landmesser, Carola Doerries,…
Cell 2007 Feb 9Authors: Hae-Ok Byun, Na-Kyung Han, Hae-June Lee, Ki-Bum Kim, Young-Gyu Ko, Gyesoon Yoon, Yun-Sil Lee, Seok-Il Hong, Jae-Seon Lee
Cancer research 2009 Jun 1Thought leaders and organizations working on research involving CTSD.
conditions: Amino Acid Metabolism, Inborn Errors
interventions: Sodium Benzoate ; Sodium Phenylacetate ; Sodium Phenylbutyrate ; Dietary Intervention
conditions: Relapsed or Refractory Multiple Myeloma
interventions: thymoglobulin
Dir, Scientific Computing
NextBio
PhD Student in Prof. R. Sowdhamini's Computational Biology Lab
National Centre for Biological Sciences - Tata Institute of Fundamental Research
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