ArticleThe EMBO journal1993
Two crystal structures for cathepsin D: the lysosomal targeting signal and active site.
Article in The EMBO journal, 1993. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 35 papers.
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Who cites it
35 citing papers in PubMed, 160 citations in OpenAlex.
- Broadening Horizons: Exploring the Cathepsin Family as Therapeutic Targets for Alzheimer's Disease.Aging and disease · 2024Review
- Oxidation of Cathepsin D by Hydroxy Radical: Its Effect on Enzyme Structure and Activity against Myofibrillar Proteins Extracted fromMolecules (Basel, Switzerland) · 2023Article
- New multienzymatic complex formed between human cathepsin D and snake venom phospholipase AThe journal of venomous animals and toxins including tropical diseases · 2022Article
- Autophagy in the Neuronal Ceroid Lipofuscinoses (Batten Disease).Frontiers in cell and developmental biology · 2022Review
- Quantitative N-glycoproteome analysis of bovine milk and yogurt.Current research in food science · 2022Article
- Cathepsin D-Managing the Delicate Balance.Pharmaceutics · 2021Review
- Low-density lipoprotein receptor-related protein 6 regulates cardiomyocyte-derived paracrine signaling to ameliorate cardiac fibrosis.Theranostics · 2021Article
- The role of cathepsin D in the pathophysiology of heart failure and its potentially beneficial properties: a translational approach.European journal of heart failure · 2020Article
- Partial Characterization of Two Cathepsin D Family Aspartic Peptidases of Clonorchis sinensis.The Korean journal of parasitology · 2019Article
- Extraction of Cathepsin D-Like Protease from Neon Flying Squid (Biomolecules · 2019Article
- Genome Wide Mapping of Peptidases inFrontiers in physiology · 2017Article
- Trehalose Alters Subcellular Trafficking and the Metabolism of the Alzheimer-associated Amyloid Precursor Protein.The Journal of biological chemistry · 2016Article
- Alteration of cathepsin-D expression in atrophied muscles and apoptotic myofibers by hindlimb unloading in a low-temperature environment.Journal of physical therapy science · 2015Article
- New tools for NTD vaccines: A case study of quality control assays for product development of the human hookworm vaccine Na-APR-1M74.Human vaccines & immunotherapeutics · 2015Article
- Cold-adapted digestive aspartic protease of the clawed lobsters Homarus americanus and Homarus gammarus: biochemical characterization.Marine biotechnology (New York, N.Y.) · 2013Article
- Characterization of gut-associated cathepsin D hemoglobinase from tick Ixodes ricinus (IrCD1).The Journal of biological chemistry · 2012Article
- Procathepsin D and cancer: From molecular biology to clinical applications.World journal of clinical oncology · 2010Article
- Pro-cathepsin D interacts with the extracellular domain of the beta chain of LRP1 and promotes LRP1-dependent fibroblast outgrowth.Journal of cell science · 2010Article
- Heat shock cognate 70 protein secretion as a new growth arrest signal for cancer cells.Oncogene · 2010Article
- Cathepsin D--many functions of one aspartic protease.Critical reviews in oncology/hematology · 2008Review
Corrections and comments
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Authors and funding
2 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Two crystal structures are described for the lysosomal aspartic protease cathepsin D (EC 3.4.23.5). The molecular replacement method was used with X-ray diffraction data to 3 A resolution to produce structures for human spleen cathepsin D and for bovine liver cathepsin D complexed with the 6-peptide inhibitor pepstatin A. The lysosomal targeting region of cathepsin D defined by previous expression studies [Barnaski et al. (1990) Cell, 63, 281-219] is located in well defined electron density on the surface of the molecules. This region includes the putative binding site of the cis-Golgi phosphotransferase which is responsible for the initial sorting step for soluble proteins destined for lysosomes by phosphorylating the carbohydrates on these molecules. Carbohydrate density is visible at both expected positions on the cathepsin D molecules and, at the best defined position, four sugar residues extend towards the lysosomal targeting region. The active site of the protease and the active site cleft substrate binding subsites are described using the pepstatin inhibited structure. The model geometry for human cathepsin D has rms deviations from ideal of bonds and angles of 0.013 A and 3.2 degrees respectively. For bovine cathepsin D the corresponding figures are 0.014 A and 3.3 degrees. The crystallographic residuals (R factors) are 16.1% and 15.8% for the human and inhibited bovine cathepsin D models respectively. The free R factors, calculated with 10% of the data reserved for testing the models and not used for refinement, are 25.1% and 24.1% respectively.
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