Zobrazeno 1 - 8
of 8
pro vyhledávání: '"Jill R. Beyette"'
Publikováno v:
Biochemical Journal. 332:315-320
The induction of apoptosis in thymocytes by the glucocorticoid dexamethasone was used as a model system to investigate whether there are changes in 20 S and 26 S proteasome activities during apoptosis. We observed that thymocytes contain high concent
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::13e376f43f2b99c9ad32e93c402a7d49
https://doi.org/10.1042/bj3320315
https://doi.org/10.1042/bj3320315
Autor:
Donald L. Mykles, Jill R. Beyette
Publikováno v:
The Journal of Experimental Zoology. 277:106-119
Lobster skeletal muscle contains four Ca 2+ -dependent cysteine proteinases that completely degrade myofibrillar proteins to acid-soluble products and may be involved in molt- induced claw muscle atrophy. One of the four enzymes, designated Ca 2+ -de
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::ddb5f5a53244a751ea90719755339057
https://doi.org/10.1002/(sici)1097-010x(19970201)277:2<106::aid-jez3>3.0.co
https://doi.org/10.1002/(sici)1097-010x(19970201)277:2<106::aid-jez3>3.0.co
Publikováno v:
Archives of Biochemistry and Biophysics. 337:232-238
Lobster skeletal muscles contain four Ca2+-dependent cysteine proteinases (CDPs I, IIa, IIb, and III) that degrade myofibrillar proteins. Lobster CDPs share many properties with calpains from vertebrate tissues, but differ in native mass and subunit
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::d4cd42272dd63e2a9e9c4e183cf065f6
https://doi.org/10.1006/abbi.1996.9758
https://doi.org/10.1006/abbi.1996.9758
Publikováno v:
Comparative Biochemistry and Physiology Part B: Comparative Biochemistry. 104:95-99
1. 1. A Ca 2+ -dependent proteinase (CDP) was purified from claw and abdominal muscles of the American lobster, Homarus americanus . It is one of four CDP activities previously identified in lobster striated muscles and designated CDP IIb (Mykles D.L
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::432a98a65179207d75fa91d72bdcdb9c
https://doi.org/10.1016/0305-0491(93)90343-4
https://doi.org/10.1016/0305-0491(93)90343-4
Proteasomes are large multicatalytic proteinases located in the nuclei and cytoplasm of all eukaryotic cells. Proteasomes are composed of four heptameric rings stacked to form a hollow cylinder (length 16–20 nm, diameter 11–12 nm). The outer two
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::8239e8d47a65e03e512e6d721de060f7
https://doi.org/10.1385/1-59259-062-4:1
https://doi.org/10.1385/1-59259-062-4:1
Autor:
Jill R. Beyette, Grant G. F. Mason
Publisher Summary This chapter discusses the major classes of proteases that have been ascribed roles in apoptosis and presents the evidence for their involvement in programmed cell death. Apoptosis or programmed cell death is a genetically controlle
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::cbb1cac750597ed48b2342a116fc5cd7
https://doi.org/10.1016/s1569-2558(08)60464-6
https://doi.org/10.1016/s1569-2558(08)60464-6
Publikováno v:
Biochemical and biophysical research communications. 199(3)
The presence of calcium-dependent proteinase in plants was investigated using soluble proteins from Arabidopsis root cultures. Calcium increased the proteolytic activity by two to three fold. Calcium-stimulated proteolytic activity was inhibited by d
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::27b9e1bc0e207c4a4bb7dd2046503aad
https://pubmed.ncbi.nlm.nih.gov/8147850
https://pubmed.ncbi.nlm.nih.gov/8147850
Publikováno v:
Applied Microbiology and Biotechnology. 30
Ethanol was produced from xylose by converting the sugar to xylulose, using commercial xylose isomerases, and simultaneously converting the xylulose to ethanol by anaerobic fermentation using different yeast strains. The process was optimized with th
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::a25a1f5dfa7fd8898173e43b672dad37
https://doi.org/10.1007/bf00255362
https://doi.org/10.1007/bf00255362