Výsledky vyhledávání - "Cell Surface Enzymes"

The Dimer Interface of the Membrane Type 1 Matrix Metalloproteinase Hemopexin Domain

Autor: Anna Tochowicz, Klaus Richter, Hideaki Nagase, Wolfram Bode, Robert Visse, Klaus Maskos, Richard Evans, Peter Goettig, Noriko Ito, Yoshifumi Itoh, Daniel Franke, Ralf Palmisano, Yasuyuki Shitomi, Dmitri I. Svergun

Publikováno v: The journal of biological chemistry 286, 7587-7600 (2011). doi:10.1074/jbc.M110.178434
The Journal of Biological Chemistry

Homodimerization is an essential step for membrane type 1 matrix metalloproteinase (MT1-MMP) to activate proMMP-2 and to degrade collagen on the cell surface. To uncover the molecular basis of the hemopexin (Hpx) domain-driven dimerization of MT1-MMP

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::326609ab62d10c9d41e7d089cdcb19c8
https://doi.org/10.1074/jbc.m110.178434

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Structural and computational studies of the Staphylococcus aureus sortase B-substrate complex reveal a substrate-stabilized oxyanion hole

Autor: Brendan R. Amer, Michael E. Jung, Robert T. Clubb, Sung Wook Yi, Grace L. Huang, Michael R. Sawaya, Alex W. Jacobitz, Angelyn V. Nguyen, Jeff Wereszczynski, J. Andrew McCammon

Publikováno v: Jacobitz, AW; Wereszczynski, J; Yi, SW; Amer, BR; Huang, GL; Nguyen, AV; et al.(2014). Structural and computational studies of the Staphylococcus aureus sortase B-substrate complex reveal a substrate-stabilized oxyanion hole. Journal of Biological Chemistry, 289(13), 8891-8902. doi: 10.1074/jbc.M113.509273. UC San Diego: Retrieved from: http://www.escholarship.org/uc/item/2928d1bp
The Journal of biological chemistry, vol 289, iss 13

Sortase cysteine transpeptidases covalently attach proteins to the bacterial cell wall or assemble fiber-like pili that promote bacterial adhesion. Members of this enzyme superfamily are widely distributed in Gram-positive bacteria that frequently ut

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::9f639b8657cd310f75deeb8965d79773
http://www.escholarship.org/uc/item/2928d1bp

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Small angle X-ray scattering analysis of Clostridium thermocellum cellulosome N-terminal complexes reveals a highly dynamic structure

Autor: Edward A. Bayer, Holly L. Spencer, Carlos M. G. A. Fontes, Zongchao Jia, Kate Cameron, Fernando M. V. Dias, Mark A. Currie, Steven P. Smith

Publikováno v: Repositório Científico de Acesso Aberto de Portugal
Repositório Científico de Acesso Aberto de Portugal (RCAAP)
instacron:RCAAP

Articles in International Journals Clostridium thermocellum produces the prototypical cellulosome, a large multienzyme complex that efficiently hydrolyzes plant cell wall polysaccharides into fermentable sugars. This ability has garnered great intere

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::aca509cedab9ab6eb8646ce658a73cfb
https://hdl.handle.net/10400.5/7135

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The CD38/CD157 mammalian gene family: An evolutionary paradigm for other leukocyte surface enzymes

Autor: Fabio Malavasi, Silvia Deaglio

Publikováno v: Purinergic Signalling

Human CD38 is the mammalian prototype of a family of phylogenetically conserved proteins which share structural similarities and enzymatic activities involved in the production of an intracellular second messenger with calcium mobilizing effects. Eng

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