Results 271 to 280 of about 20,002 (295)
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Maspin: A Tumor Suppressing Serpin
1996Maspin, a serpin found in mammary epithelial cells, has been shown to have tumor suppressor activity. The gene is expressed in normal human mammary epithelial cells but down-regulated in invasive breast carcinomas. Similar patterns of expression at the RNA and protein levels are seen by Northern analysis with cells grown in culture and by ...
Mary J.C. Hendrix+3 more
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Evolutionary history of the uterine serpins
Journal of Experimental Zoology, 2000A bioinformatics analysis was conducted on the four members of the uterine serpin (US) family of serpins. Evolutionary analysis of the protein sequences and 86 homologous serpins by maximum parsimony and distance methods indicated that the uterine serpins proteins form a clade distinct from other serpins.
Steven A. Benner+4 more
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Biochemistry, 1989
Article synthese sur l'α1-antitrypsine: caracteristiques structurales et fonctionnelles (capacite de liaison a des modulateurs); utilisation de l'α1-antitrypsine en tant que modele pour toutes les ...
R. Huber, Carrell Rw
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Article synthese sur l'α1-antitrypsine: caracteristiques structurales et fonctionnelles (capacite de liaison a des modulateurs); utilisation de l'α1-antitrypsine en tant que modele pour toutes les ...
R. Huber, Carrell Rw
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Conformational pathology of the serpins: themes, variations, and therapeutic strategies.
Annual Review of Biochemistry, 2009Point mutations cause members of the serine protease inhibitor (serpin) superfamily to undergo a novel conformational transition, forming ordered polymers. These polymers characterize a group of diseases termed the serpinopathies.
B. Gooptu, D. Lomas
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The FEBS Journal, 2005
Much of the basic biochemistry of antiplasmin was described more than 20 years ago and yet it remains an enigmatic member of the serine protease inhibitor (serpin) family. It possesses all of the characteristics of other inhibitory serpins but in addition it has unique N‐ and C‐terminal extensions which significantly modify its activities.
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Much of the basic biochemistry of antiplasmin was described more than 20 years ago and yet it remains an enigmatic member of the serine protease inhibitor (serpin) family. It possesses all of the characteristics of other inhibitory serpins but in addition it has unique N‐ and C‐terminal extensions which significantly modify its activities.
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Science Translational Medicine, 2014
Serpins help breast and lung cancer cells metastasize to the brain by annulling stromal defenses and co-opting capillaries.
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Serpins help breast and lung cancer cells metastasize to the brain by annulling stromal defenses and co-opting capillaries.
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Cystatins, serpins and other families of protease inhibitors in plants.
Current protein and peptide science, 2011Plant protease inhibitors (PIs) are generally small proteins present in high concentrations in storage tissues (tubers and seeds), and to a lower level in leaves.
M. Volpicella+5 more
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Serpins in plants and green algae
Functional & Integrative Genomics, 2007Control of proteolysis is important for plant growth, development, responses to stress, and defence against insects and pathogens. Members of the serpin protein family are likely to play a critical role in this control through irreversible inhibition of endogenous and exogenous target proteinases. Serpins have been found in diverse species of the plant
Jørn Hejgaard, Thomas H. Roberts
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Serpin Structure, Mechanism, and Function
Chemical Reviews, 2002AbstractFor Abstract see ChemInform Abstract in Full Text.
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Serpins in Caenorhabditis elegans
2015C. elegans is an extremely powerful model organism to study gene function and biology. The nematodes’ genetic tractability and high degree of genetic similarity with humans make it ideal to study the biologic role of serpins. The endogenous C. elegans serpins are most similar to the human clade B or intracellular serpin family and have a predominantly ...
Cliff J. Luke+6 more
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