نتایج جستجو برای: serpin

تعداد نتایج: 1326  

Journal: :Clinical and Developmental Immunology 2004
Imre Szabo Miklos Simon Janos Hunyadi

Keratinocytes were shown to induce the activation of plasminogen activator resulting in the formation of plasmin and the initiation of proteolysis in vitro. Activation of surface bound plasminogen may localize protease activity in the pericellular microenvironment and play a role in inducing both a conformational change and cell locomotion. Plasmin, however, can induce non-proteolytic effects o...

Journal: :Thrombosis and haemostasis 2010
Ganesh Munuswamy-Ramanujam Erbin Dai Liying Liu Mira Shnabel Yun Ming Sun Mee Bartee David A Lomas Alexandra R Lucas

Thrombolytic serine proteases not only initiate fibrinolysis, but also are up-regulated in vascular disease and acute inflammatory responses. Although the serine protease inhibitor (serpin) plasminogen activator inhibitor-1 (PAI-1) is considered a main regulator of thrombolysis, PAI-1 is also associated with vascular inflammation. The role of other serpins that target thrombolytic proteases, PA...

Journal: :Journal of experimental botany 2005
Mette la Cour Petersen Jørn Hejgaard Gary A Thompson Alexander Schulz

Serpins are unique inhibitors of serine proteases that are located in various plant tissues and organs. An orthologue of the pumpkin (Cucurbita maxima) phloem serpin CmPS-1 was amplified from cucumber (Cucumis sativus) RNA by RT-PCR, cloned, and designated as CsPS-1 (GenBank accession no. AJ866989). Alternative amino acid sequences in the reactive centre loop suggest distinct inhibitory specifi...

Journal: :The Biochemical journal 1998
I Björk K Nordling E Raub-Segall U Hellman S T Olson

Cross-class inhibition of cysteine proteinases by serpins differs from serpin inhibition of serine proteinases primarily in that no stable serpin-cysteine proteinase complex can be demonstrated. This difference in reaction mechanism was elucidated by studies of the inactivation of the cysteine proteinases, papain and cathepsin L, by the serpin antithrombin. The two proteinases were inactivated ...

Journal: :Proceedings of the National Academy of Sciences 1997

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