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Articles
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MEROPS: the database of proteolytic enzymes, their substrates and inhibitors 2014
https://ncsu.summon.serialssolutions.com/2.0.0/link/0/eLvHCXMwnV1LS8QwEB7Ui17EF7q-iCierG03r1ZEkEXxIoqPc0mT1C26WXH1sP56J-lWXL15bhrCl2nnm8zkG4ADK1hZGlVF3CgesdTYKDeqjIyWViaGKynN9GEO8PYuTCja12V97F4Gx67uh9rK14GO2zqx-Pa6R3OBRD2NZ2FWUtaG6JPUAXqkRjMqSGyyrNUkzWns1Fv89Pyec989x7sumfn-5z8d0h-W-btY8of3uVyCxQltJOfN8pZhxroVWD13GDIPxuSQhELOcEK-AvO9tonbKtxfX9zd3N6fEOR5xFeDeq9FhhU57Z8FiYbhyxinJNZ9jgd2dBr3z45ISB6QEf5SgnTtiChnSO36dVn73jxr8Hh58dC7iiZ9FCJNKaORTrvSYCClONKpVDFZ0cykJYbFXcW7ShpqqkQJySwzyAeY1Al-jLlNtFAWGQjdAJJQzcvMWGWFYFpUmaVJJaznP0aLPO3Afoti8droZBRNfpsWCHvRwN6BvRbgAoHwuQnl7PBjhBEILofjnuGY9Qbw73naneqAnNqK7wFeInv6CVpOkMqeWMrmv9_cggUPSXPosg1z728fdgfm_P2K3WB3X6wP4C4
Nucleic Acids Research, Vol. 42, Issue Database issue.
Peptidases, their substrates and inhibitors are of great relevance to biology, medicine and biotechnology. The MEROPS database (http://merops.sanger.ac.uk) aims to fulfill the need for an integrate... Read more
Peptidases, their substrates and inhibitors are of great relevance to biology, medicine and biotechnology. The MEROPS database (http://merops.sanger.ac.uk) aims to fulfill the need for an integrated source of information about these. The database has hierarchical classifications in which homologous sets of peptidases and protein inhibitors are grouped into protein species, which are grouped into families, which are in turn grouped into clans. Recent developments include the following. A community annotation project has been instigated in which acknowledged experts are invited to contribute summaries for peptidases. Software has been written to provide an Internet-based data entry form. Contributors are acknowledged on the relevant web page. A new display showing the intron/exon structures of eukaryote peptidase genes and the phasing of the junctions has been implemented. It is now possible to filter the list of peptidases from a completely sequenced bacterial genome for a particular strain of the organism. The MEROPS filing pipeline has been altered to circumvent the restrictions imposed on non-interactive blastp searches, and a HMMER search using specially generated alignments to maximize the distribution of organisms returned in the search results has been added. Read less
Journal Article | Full Text Online
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Endogenous proteolytic enzymes – A study of their impact on cod (Gadus morhua) muscle proteins... 2015
https://ncsu.summon.serialssolutions.com/2.0.0/link/0/eLvHCXMwpV3NTtwwEB5V9FAulAKCbQHNoarKIdqE_EsrpOVnS1WJExxR5Hhs7SI2QWT3sD31HSr1AfskHdtrRKtKCHFM4kxszcSesb_5BuCjypK6JqGDlEQaJBGpoCRRByRzlYeUijynvzdzIPK5MP8e4Vsolm5b4iGYxPHI0ZIWhmQ7TnNTrGF0evww93KDwp0bFHZz61FO8P_FPLEcOVCkXWtGb-Ha99JCTExhg8dY-77lN7SkFp7L8VkjWoe1pROKQ2c17-CVajbgzYmv_bYBvdOJmuEnXLKG3uKFJ-3ndj6XuduEX2cNtY7mFQfjI0v60N4uWCyq5vtiqrpBf3yEv3_8xCFaJltsNdrDCXT5mdg2KFvCz18EsZBpez-eiwOczjvuGVqBk6ZD0RAajIohCTF37wwcXHU4aVCg5tXFUIuSeWL4a7fganR2eXIeLCs9BDKO01nAbkpiYlGR8ZSjeBbioFOWWiYqFIeSiC2G3dTyUHB8loQqTouaw1ap86SmLA91vAMYxjKtC1JCZVkiM12oONSZMh4ayayMetD3mq7uHJNH5SFuN5VXSGUUUoVlxQrpQekNolr6I87PqFihT7677Szo4VuGC45jzej9C6R-gFW-Sh1yaBdWZvdztQcrxgL34fXw67fzi337Q_wBbewNbA
Food Chemistry, Vol. 172, pp. 551 - 558.
•Endogenous proteolytic activities in a fermented cod product were investigated.•Effect of endogenous proteases on proteins at different pHs was investigated.•Effect of proteases on gel strength in... Read more
•Endogenous proteolytic activities in a fermented cod product were investigated.•Effect of endogenous proteases on proteins at different pHs was investigated.•Effect of proteases on gel strength in fermentation and storage was investigated.•Cathepsin B showed the highest activities during fermentation and storage.•The product showed a firm texture despite high catheptic activities. The aim of this study was to investigate endogenous proteolytic activities in a cod product and their impact on muscle proteins and textural properties during fermentation and storage. The result of specific proteolytic activities showed that cathepsins, especially cathepsin B, had the highest activities during fermentation and storage. SDS–PAGE indicated more degradation of myofibrillar proteins by cathepsin L than other proteases and that the hydrolysis by cathepsins was pronounced in the last stage of fermentation. Texture analysis showed that cathepsins had a negative impact on gel strength and this impact increased in the last stage of fermentation. However the product still had a firm texture. During storage (4°C) for one week, no significant changes were seen in the gel strength. In conclusion, cathepsins had more impact on muscle proteins and textural properties than other proteases during fermentation but had little impact on gel strength during storage at 4°C. Read less
Journal Article | Full Text Online
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Proteolytic Enzymes Clustered in Specialized Plasma-Membrane Domains Drive Endothelial Cells'... 2016
https://ncsu.summon.serialssolutions.com/2.0.0/link/0/eLvHCXMwnV3NbtNAEF7R9MIFUUA0UIJBSMDBiZ21vYlUVUrchhaIsGipWi7WenedWPJPFDeH9sRr8Ho8CTNrO5JRT1wmsne8cnZ-dsae-UzIO-U5USR5bLqSu6ZjS2WOJY9MKZhilnQ5Y7L9MIe4TS-MLtoXUdLP06yfJ0tdW7nKxKCpExsEc98ZIcjIcLBDdhh1mhS9cr9gwJ5X98hRZg9qkfRXRa76GDAwC5FChww2Lsemre1Io_ZvfXNnlRblfYHnv_WTFbqU3pBmj8mjOpI0JtUd75EHKn9C9mpbLY0PNaD0x6dkdbg8ChCPoUhvgdk4ye9uM1UeDpZHhp9uECpBSSPJjfpj9MkdHAYQVmfcnKsM8ulcGcdFxpO8NI7X4B9hComtWylwG75K0_LPr9_GPFlU-vSM_JidXPinZv2lBVPAZnVjClgKHg9pFHsC8o0xJGZjW7lSRkyMxjZ3BXhBiE04dSjFd4vx0JPccgRzhEVVTPeJYVHhRiOpODA6wotHilqxpzBCkgKm6xKzWelwVSFphPp1GoMMpFqyEIUU1kLqkimKY8uLONj6RLFehLU2hJRGQng2grYJ7M-OYsQv8yAOii0-VDDJaxRmWDWVbq05nDgQ5jLMhrvkreZALIwci20WfFOW4dm3yxbT-5opLkDigte9C3C7CJ_V4jxocYKxitbwPmpV84fL0AaHCVEnpI1wZaNp9w-_2Q7jpFgbl6tiU_GMNRBjlzyvFHO7aI2adwlrqWxrVdsjYHQaZbw2shf_feVL8hCiS09Xh3oHpHOz3qhXpIOtKT0w3O-XSC8-Ib1imk6Bjny7R3Yn08_-DH8v_OC8px-UAJ0FX-HcqX82-wlHX6b9HpbqBpoiV-DC-d3g2j-_7mmn8Bfb1For
Plo S One, Vol. 11, Issue 5.
In vitro cultured endothelial cells forming a continuous monolayer establish stable cell-cell contacts and acquire a "resting" phenotype; on the other hand, when growing in sparse conditions these ... Read more
In vitro cultured endothelial cells forming a continuous monolayer establish stable cell-cell contacts and acquire a "resting" phenotype; on the other hand, when growing in sparse conditions these cells acquire a migratory phenotype and invade the empty area of the culture. Culturing cells in different conditions, we compared expression and clustering of proteolytic enzymes in cells having migratory versus stationary behavior. In order to observe resting and migrating cells in the same microscopic field, a continuous cell monolayer was wounded. Increased expression of proteolytic enzymes was evident in cell membranes of migrating cells especially at sprouting sites and in shed membrane vesicles. Gelatin zymography and western blotting analyses confirmed that in migrating cells, expression of membrane-bound and of vesicle-associated proteolytic enzymes are increased. The enzymes concerned include MMP-2, MMP-9, MT1-MMP, seprase, DPP4 (DiPeptidyl Peptidase 4) and uPA. Shed membrane vesicles were shown to exert degradative activity on ECM components and produce substrates facilitating cell migration. Vesicles shed by migrating cells degraded ECM components at an increased rate; as a result their effect on cell migration was amplified. Inhibiting either Matrix Metallo Proteases (MMPs) or Serine Integral Membrane Peptidases (SIMPs) caused a decrease in the stimulatory effect of vesicles, inhibiting the spontaneous migratory activity of cells; a similar result was also obtained when a monoclonal antibody acting on DPP4 was tested. We conclude that proteolytic enzymes have a synergistic stimulatory effect on cell migration and that their clustering probably facilitates the proteolytic activation cascades needed to produce maximal degradative activity on cell substrates during the angiogenic process. Read less
Journal Article | Full Text Online
Books & Media
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Proteolytic enzymes
https://catalog.lib.ncsu.edu/catalog/NCSU3342209
Online Resources QP601 .M49 V.19 EBOOK | Book
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Proteolytic enzymes
https://catalog.lib.ncsu.edu/catalog/NCSU3342210
Online Resources QP601 .M49 V.45 EBOOK | Book
Other Ways to Find Articles
Journals
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Journal of enzyme inhibition and medicinal chemistry
https://www.lib.ncsu.edu/journals/more_info.php?id=40071
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