| DOI | Resolve DOI: https://doi.org/10.1136/ard.2004.030429 |
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| Author | Search for: Rocken, C.; Search for: Menard, R.1; Search for: Buhling, F.; Search for: Vockler, S.; Search for: Raynes, J.; Search for: Stix, B.; Search for: Kruger, S.; Search for: Roessner, A.; Search for: Kahne, T. |
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| Affiliation | - National Research Council of Canada. NRC Biotechnology Research Institute
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| Format | Text, Article |
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| Subject | Cathepsin B; Cysteine; pathology; pharmaceutical; Protease; Protein; Proteins |
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| Abstract | Background: AA amyloidosis develops in patients with chronic inflammatory diseases. The AA amyloid proteins are proteolytic fragments obtained from serum amyloid A (SAA). Previous studies have provided evidence that endosomes or lysosomes might be involved in the processing of SAA, and contribute to the pathology of AA amyloidosis |
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| Publication date | 2005 |
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| In | |
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| NRC number | 47475 |
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| NPARC number | 3539900 |
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| Export citation | Export as RIS |
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| Report a correction | Report a correction (opens in a new tab) |
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| Record identifier | ac215f7b-bfbc-4f34-9665-a09caa96df44 |
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| Record created | 2009-03-01 |
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| Record modified | 2020-04-07 |
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