Zobrazeno 1 - 10
of 29
pro vyhledávání: '"Isabelle Durussel"'
Publikováno v:
Journal of Biological Chemistry. 281:38905-38917
S100A16 protein is a new and unique member of the EF-hand Ca(2+)-binding proteins. S100 proteins are cell- and tissue-specific and are involved in many intra- and extracellular processes through interacting with specific target proteins. In the centr
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::5096738be998bc9bcbdcf20c77b70537
https://doi.org/10.1074/jbc.m605798200
https://doi.org/10.1074/jbc.m605798200
Autor:
Isabelle Durussel, Claudia Firanescu, Patricia Duchambon, Constantin T. Craescu, Yves Blouquit, Fabiana Tirone, Jos A. Cox
Publikováno v:
Biochemistry. 44:840-850
There are four isoforms of centrin in mammals, with variable sequence, tissue expression, and functional properties. We have recently characterized a number of structural, ion, and target binding properties of human centrin isoform HsCen2. This paper
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::45e0213a645b46ab912fe29c4832ba57
https://doi.org/10.1021/bi048294e
https://doi.org/10.1021/bi048294e
Autor:
Patricia Duchambon, Yves Blouquit, Jos A. Cox, Simona Miron, Isabelle Durussel, Elena Matei, Constantin T. Craescu
Publikováno v:
Biochemistry. 42:1439-1450
Human centrin 2 (HsCen2) is an EF-hand protein that plays a critical role in the centrosome duplication and separation during cell division. We studied the structural and Ca(2+)-binding properties of two C-terminal fragments of this protein: SC-HsCen
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::882f2177056ffef12832c99ccb0a56d2
https://doi.org/10.1021/bi0269714
https://doi.org/10.1021/bi0269714
Publikováno v:
Biochemistry. 41:5439-5448
Human CLSP, a new Ca(2+)-binding protein specifically expressed in differentiated keratinocytes, is a 15.9 kDa, four EF-hand containing protein with 52% sequence identity to calmodulin (CaM). The protein binds four Ca(2+) ions at two pairs of sites w
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::ff861ae02ae13d926d9e17aedb1f219f
https://doi.org/10.1021/bi016062z
https://doi.org/10.1021/bi016062z
Publikováno v:
Journal of Biological Chemistry. 276:17762-17769
Grancalcin is a recently described Ca(2+)-binding protein especially abundant in human neutrophils. Grancalcin belongs to the penta-EF-hand subfamily of EF-hand proteins, which also comprises calpain, sorcin, peflin, and ALG-2. Penta-EF-hand members
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::ba62cc481339b37f33f9866dba6365fd
https://doi.org/10.1074/jbc.m100965200
https://doi.org/10.1074/jbc.m100965200
Autor:
Beat W. Schäfer, Jos A. Cox, Jean-Marc Fritschy, Heinz Troxler, Claus W. Heizmann, Petra Murmann, Isabelle Durussel
Publikováno v:
Journal of Biological Chemistry. 275:30623-30630
S100A5 is a novel member of the EF-hand superfamily of calcium-binding proteins that is poorly characterized at the protein level. Immunohistochemical analysis demonstrates that it is expressed in very restricted regions of the adult brain. Here we c
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::ac07834e374f3f00d99ffbe9be86f369
https://doi.org/10.1074/jbc.m002260200
https://doi.org/10.1074/jbc.m002260200
Publikováno v:
FEBS Letters. 472:208-212
Centrin and calmodulin (CaM) are closely related four-EF-hand Ca(2+)-binding proteins. While CaM is monomeric, centrin 2 is dimeric and binds only two Ca(2+) per dimer, likely to site IV in each monomer. Ca(2+) binding to centrin 2 displays pronounce
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::f0a3629bf61fc0f50ccd23ec2be9fe3c
https://doi.org/10.1016/s0014-5793(00)01452-6
https://doi.org/10.1016/s0014-5793(00)01452-6
Publikováno v:
Journal of Biological Chemistry. 275:8686-8694
S100 proteins became of major interest because of their divergent cell- and tissue-specific expression, their close association with a number of human diseases, and their importance for clinical diagnostics. Here, we report for the first time the pur
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::9ca0052c128fa17f19221e3e923a20a3
https://doi.org/10.1074/jbc.275.12.8686
https://doi.org/10.1074/jbc.275.12.8686
Publikováno v:
Journal of Biological Chemistry. 273:31145-31152
In the Sdr family of Staphylococcus aureus cell surface proteins, three recently cloned members (Josefsson, E., McCrea, K., Ni Eidhin, D., O'Connell, D., Cox, J. A., Hook, M., and Foster, T. (1998) Microbiology, in press) display variable numbers of
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::d6ad5cbcd52afa513fc431a5df1dfe9a
https://doi.org/10.1074/jbc.273.47.31145
https://doi.org/10.1074/jbc.273.47.31145
Publikováno v:
Journal of Biological Chemistry. 273:18826-18834
The Ca2+-binding protein S100A2 is an unusual member of the S100 family, characterized by its nuclear localization and down-regulated expression in tumorigenic cells. In this study, we investigated the properties of human recombinant S100A2 (wtS100A2
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::3f2310612bd9e8eb1698ec3c75404700
https://doi.org/10.1074/jbc.273.30.18826
https://doi.org/10.1074/jbc.273.30.18826