Proteases as Targets for Therapy, Выпуск 146
M. Abdel-Meguid, Klaus von der Helm, Bruce D. Korant, John Chris Dion Cheronis
Springer Science & Business Media, 2000 - Всего страниц: 410
This volume is the first to combine latest information on viral, microbial and cellular proteolytic enzymes as potential targets for human therapeutics. Proteases control a large array of physiological reactions, and are involved in a variety of pathological processes for which effective medications are currently needed and/or being sought after. Although protease inhibitors have been investigated for many years, few have been employed therapeutically. Recent break- through by HIV protease inhibitors as therapeutic drugs has re-encouraged the search for inhibitors of other proteolytic enzymes. Klaus von der Helm, who described the first viral protease has brought leading experts together to discuss not only the success and problems of clinical use and continuing prospects, but to review further potential drug targets. This volume provides detailed information and evaluations of key viral, bacterial, fungal, and cellular proteases as potential future drug candidates.
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TANAKA K The Tokyo Metropolitan Institute of Medical Science
Early Clinical Studies
Clinical Experience with Human Immunodeficiency Virus Protease
Biochemical Basis for Resistance
Two Strategies to Reduce Viral Resistance to
Designing Drugs to Inhibit PIResistant Viruses
Inhibitors of TACE and TNFα Secretion
B Serine Elastases and Inflammation
Suggestions for Future Therapeutic Strategies
The NS23 Proteinase
E The 3C Proteinases
F Inhibition of 3C Proteinases
Potential InhibitorBinding Sites
E Summary and Prospects
E Paradigms for Testing Proteinase Inhibitors as Therapeutic
F Bacterial Proteinases to the Rescue
General Considerations in the Development of MMPIS
Potential Clinical Targets for SerineElastase Inhibition
Cystatins in Cancer
Potential Transcriptional Regulation
G Potential for Caspase Inhibitor Therapy
Regulatory Control of Ub and the Proteasome in Apoptosis
F The UbProteasome System and Cancer Therapy
Role of Mutant Presenilins in Amyloid Generation
E Proteolytic Degradation of PSs
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Стр. 393 - Scheuner D, Eckman C, Jensen M, Song X, Citron M, Suzuki N, Bird TD, Hardy J, Hutton M, Kukull W, Larson E, LevyLahad E, Viitanen M, Peskind E, Poorkaj P, Schellenberg G, Tanzi R, Wasco W, Lannfelt L, Selkoe D...
Стр. 371 - J. (1991 ). Segregation of a missense mutation in the amyloid precursor protein gene with familial Alzheimer's disease.
Стр. 393 - Secreted amyloid beta-protein similar to that in the senile plaques of Alzheimer's disease is increased in vivo by the presenilin 1 and 2 and APP mutations linked to familial Alzheimer's disease.
Стр. 393 - Seubert, P., Vigo-Pelfrey, C., Esch, F., Lee. M., Dovey, H., Davis, D.. Sinha, S., Schlossmacher, M.. Whaley, J., Swindlehurst, C., McCormack, R., Wolfert, R., Selkoe, D., Lieberburg, I., and Schenk D., Isolation and quantification of soluble Alzheimer's p-peptide from biological fluids.