Zobrazeno 1 - 10
of 54
pro vyhledávání: '"Abdellatif Fattoum"'
Autor:
Jeanne Feinberg, Dalila Karoui, Hervé Rochat, Claude Roustan, Jana Gregoire, Louise-Anne Pradel, Abdellatif Fattoum
Publikováno v:
International Journal of Peptide and Protein Research. 17:393-400
The purpose of this work was to contribute to the study of the covalent struc ture of yeast 3-phosphoglycerate kinase. First, we undertook the complete align ment of the four fragments produced by cyanogen-bromide cleavage and which constitute the in
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::3b679dd0e5b4584d87491b44262bcadf
https://doi.org/10.1111/j.1399-3011.1981.tb02006.x
https://doi.org/10.1111/j.1399-3011.1981.tb02006.x
Autor:
Yvan Boublik, Mehdi Chenik, Hechmi Louzir, Yosser Ben Achour-Chenik, Ahlem Aamouri, Inès Lakhal-Naouar, Abdellatif Fattoum, Mounira Meddeb
Publikováno v:
Biochemical and Biophysical Research Communications
Biochemical and Biophysical Research Communications, Elsevier, 2008, 375 (1), pp.54-8. ⟨10.1016/j.bbrc.2008.07.099⟩
Biochemical and Biophysical Research Communications, Elsevier, 2008, 375 (1), pp.54-8. ⟨10.1016/j.bbrc.2008.07.099⟩
International audience; We report the characterization of a new Leishmania major gene, lmaj3'nt/nu, encoding a 382 amino acids protein, Lmaj3'NT/NU, that belongs to the 3'nucleotidase/nuclease family. Interestingly, sequence and phylogenetic analysis
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::b8e0627ed4351123d5f69a48e90eff24
https://doi.org/10.1016/j.bbrc.2008.07.099
https://doi.org/10.1016/j.bbrc.2008.07.099
Autor:
Sutherland K. Maciver, Abdellatif Fattoum, Claude Roustan, Bertrand Rebiere, Imen Ferjani, Yves Benyamin
Publikováno v:
FEBS Letters
FEBS Letters, Wiley, 2007, 581 (4), pp.681-6. ⟨10.1016/j.febslet.2007.01.031⟩
FEBS Letters, Wiley, 2007, 581 (4), pp.681-6. ⟨10.1016/j.febslet.2007.01.031⟩
Gelsolin is an actin-binding protein that is regulated by the occupancy of multiple calcium-binding sites. We have studied calcium induced conformational changes in the G1-2 and G1-3 sub-domains, and report the binding affinities for the three type I
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::019bdcc8113e3b314b7c0cb625d4fa1a
https://doi.org/10.1016/j.febslet.2007.01.031
https://doi.org/10.1016/j.febslet.2007.01.031
Autor:
Sutherland K. Maciver, Claude Roustan, Abdellatif Fattoum, Yves Benyamin, Mohamed Manai, Imen Ferjani
Publikováno v:
FEBS Letters. 580:4801-4806
Calponins are actin-binding proteins that are implicated in the regulation of actomyosin. Calponin binds filamentous actin (F-actin) through two distinct sites ABS1 and ABS2, with an affinity in the low micromolar range. We report that smooth muscle
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::c250971226dc32c6c769b38a72bbff94
https://doi.org/10.1016/j.febslet.2006.07.065
https://doi.org/10.1016/j.febslet.2006.07.065
Publikováno v:
Journal of Molecular Biology. 359:478-485
Many actin-binding proteins have been observed to have a modular architecture. One of the most abundant modules is the calponin-homology (CH) domain, found as tandem repeats in proteins that cross-link actin filaments (such as fimbrin, spectrin and a
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::1b66a2214286ce7d8da62f5a18f28e9d
https://doi.org/10.1016/j.jmb.2006.03.044
https://doi.org/10.1016/j.jmb.2006.03.044
Autor:
Sutherland K. Maciver, Nadir Bettache, Anne Chahinian, Jocelyn Méré, Claude Roustan, Yves Benyamin, Abdellatif Fattoum
Publikováno v:
Biochemical Journal. 386:47-56
Gelsolin is a calcium-, pH- and lipid-dependent actin filament severing/capping protein whose main function is to regulate the assembly state of the actin cytoskeleton. Gelsolin is associated with membranes in cells, and it is generally assumed that
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::6b968c21ee6054f1178528d6f6775411
https://doi.org/10.1042/bj20041054
https://doi.org/10.1042/bj20041054
Autor:
Abdellatif Fattoum, Mario Gimona, Julien Abouzaglou, Christine Benistant, Claude Roustan, Rhida Kassab
Publikováno v:
European Journal of Biochemistry. 271:2615-2623
The phosphorylation-dephosphorylation of serine and threonine residues of calponin is known to modulate in vitro its interaction with F-actin and is thought to regulate several biological processes in cells, involving either of the calponin isoforms.
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::c34299d5d7e2556f27315bd0929e23e2
https://doi.org/10.1111/j.1432-1033.2004.04190.x
https://doi.org/10.1111/j.1432-1033.2004.04190.x
Autor:
Ridha Kassab, Abdellatif Fattoum, Claude Roustan, Elisabeth Der Terrossian, Cybelle Smyczynski
Publikováno v:
Biochemistry. 42:1274-1282
The smooth muscle basic calponin interacts with F-actin and inhibits the actomyosin ATPase in a calmodulin or phosphorylation modulated manner. It also binds in vitro to microtubules and its acidic isoform, present in nonmuscle cells, and co-localize
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::7ec64eca19f2f67d4d0c0f551de2f43a
https://doi.org/10.1021/bi020336g
https://doi.org/10.1021/bi020336g
Autor:
S. Victor Perry, Clare E. Gallon, Abdellatif Fattoum, Barry A. Levine, Matthew A. Hodgkin, Valerie B. Patchell
Publikováno v:
European Journal of Biochemistry. 269:5088-5100
Peptides corresponding to the N-terminus of skeletal myosin light chain 1 (rsMLC1 1–37) and the short loop of human cardiac β-myosin (hcM398–414) have been shown to interact with skeletal F-actin by NMR and fluorescence measurements. Skeletal tr
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::727479e5ee0800baf860972e42364d60
https://doi.org/10.1046/j.1432-1033.2002.03227.x
https://doi.org/10.1046/j.1432-1033.2002.03227.x
Autor:
Yuan Gao, Mohammed El-Mezgueldi, Steven B. Marston, Abdellatif Fattoum, James S. Evans, Douglas G. Low, Valerie B. Patchell, Barry A. Levine, Alexander V. Vorotnikov
Publikováno v:
Biochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology. 1596:121-130
Caldesmon is an inhibitory protein believed to be involved in the regulation of thin filament activity in smooth muscles and is a major cytoplasmic substrate for MAP kinase. NMR spectroscopy shows that the actin binding properties of the minimal inhi
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::4d36b2e2b05fed8d503164c51b12ca18
https://doi.org/10.1016/s0167-4838(02)00210-8
https://doi.org/10.1016/s0167-4838(02)00210-8