A. Fattoum

发表

Interaction of caldesmon with actin subdomain-2.

A. Bartegi, C. Roustan, R. Bertrand, 1998, European journal of biochemistry.

Identification of gelsolin, a Ca2+-dependent regulatory protein of actin gel-sol transformation, and its intracellular distribution in a variety of cells and tissues

J. Albrecht, H. Yin, A. Fattoum, 1981, The Journal of cell biology.

Yeast 3-phosphoglycerate kinase. Essential arginyl residues at the 3-phosphoglycerate binding site.

L. Pradel, C. Roustan, A. Fattoum, 1978, Biochimica et biophysica acta.

Spatial proximity of a tyrosyl and a lysyl residue in the active site region of yeast 3-phosphoglycerate kinase.

L. Pradel, C. Roustan, A. Fattoum, 1979, Biochimie.

Muscle gelsolin: isolation from heart tissue and characterization as an integral myofibrillar protein

J. Gabrion, J. Rouayrenc, R. Kassab, 1984, FEBS letters.

The inhibitory region of troponin-I alters the ability of F-actin to interact with different segments of myosin.

S. Perry, V. Patchell, B. Levine, 2002, European journal of biochemistry.

Calcium‐induced conformational changes in the amino‐terminal half of gelsolin

Y. Benyamin, S. Maciver, C. Roustan, 2007, FEBS letters.

Structural studies on yeast 3-phosphoglycerate kinase. Linear arrangement of the CNBr fragments, partial amino acid sequence of the inner part of the polypeptide chain, and analyses of the N-terminal domain of the protein.

L. Pradel, J. Gregoire, H. Rochat, 2009, International journal of peptide and protein research.

Yeast 3-phosphoglycerate kinase: sulfate and substrate binding, their effect on the conformational state of the enzyme.

L. Pradel, C. Roustan, A. Fattoum, 1980, Biochemistry.

Structural studies on yeast 3-phosphoglycerate kinase. Identification by immuno-affinity chromatography of one glutamyl residue essential for yeast 3-phosphoglycerate kinase activity. Its location in the primary structure.

L. Pradel, G. Desvages, C. Roustan, 1980, European journal of biochemistry.

Isolation and some structural and functional properties of macrophage tropomyosin.

J. Hartwig, T. Stossel, A. Fattoum, 1983, Biochemistry.

Characterization of the Ca2+-induced conformational changes in gelsolin and identification of interaction regions between actin and gelsolin.

J. Rouayrenc, C. Méjean, R. Kassab, 1986, Biochemistry.

The gelsolin:calponin complex nucleates actin filaments with distinct morphologies.

P. Milhiet, B. Seantier, M. Manai, 2010, Biochemical and biophysical research communications.

Calponin binds G‐actin and F‐actin with similar affinity

M. Manai, Y. Benyamin, S. Maciver, 2006, FEBS letters.

Change in the shape and density of dendritic spines caused by overexpression of acidic calponin in cultured hippocampal neurons

O. Caillard, Y. Ben‐Ari, I. Medina, 2006, Hippocampus.

Increased levels of acidic calponin during dendritic spine plasticity after pilocarpine‐induced seizures

A. Represa, T. Shirao, Y. Ben‐Ari, 2003, Hippocampus.

Acidic calponin immunoreactivity in postnatal rat brain and cultures: subcellular localization in growth cones, under the plasma membrane and along actin and glial filaments

Y. Ben-Ari, A. Represa, B. Menn, 1999, The European journal of neuroscience.

The CH-domain of calponin does not determine the modes of calponin binding to F-actin.

Edward H Egelman, Vitold E Galkin, E. Egelman, 2006, Journal of molecular biology.

Co-operation of domain-binding and calcium-binding sites in the activation of gelsolin.

Y. Benyamin, S. Maciver, C. Roustan, 2003, European journal of biochemistry.

Construction, expression and unexpected regulatory properties of a tropomyosin mutant with a 31-residue deletion at the C-terminus (exon 9).

F. Heitz, J. Liautard, A. Bartegi, 1990, European journal of biochemistry.

Spectrophotometric investigations of the interaction of native and chemically modified ATP: guanidinophosphotransferases with their substrates.

N. Thoai, L. Pradel, R. Kassab, 1970, Biochimica et biophysica acta.

The tyrosyl residues in creatine kinase. Modification by iodine.

L. Pradel, R. Kassab, A. Fattoum, 1975, Biochimica et biophysica acta.

The tyrosyl residues of yeast 3‐phosphoglycerate kinase: Reactivity toward iodine

L. Pradel, C. Roustan, A. Fattoum, 1975, FEBS letters.

Effects of iodination and acetylation of tyrosyl residues on the activity and structure of arginine kinase from lobster muscle.

L. Pradel, R. Kassab, A. Fattoum, 1971, European journal of biochemistry.

Characterization of the carboxyl-terminal 10-kDa cyanogen bromide fragment of caldesmon as an actin-calmodulin-binding region.

J. Derancourt, A. Bartegi, R. Kassab, 1990, The Journal of biological chemistry.

Primary structure of lobster-muscle arginine kinase. Isolation and characterization of the fragments produced by cyanogen-bromide cleavage.

R. Kassab, A. Fattoum, F. Regnouf, 1974, European journal of biochemistry.

Cross-linking of smooth muscle caldesmon to the NH2-terminal region of skeletal F-actin.

A. Bartegi, R. Kassab, A. Fattoum, 1990, The Journal of biological chemistry.

Isolation, characterization and immunocytochemical localization of caldesmon-like protein from molluscan striated muscle.

A. Bartegi, J. Gabrion, R. Kassab, 1989, European journal of biochemistry.

Phosphorylation of the minimal inhibitory region at the C-terminus of caldesmon alters its structural and actin binding properties.

A. Vorotnikov, V. Patchell, Steven B Marston, 2002, Biochimica et biophysica acta.

Identification and characterization of a new Leishmania major specific 3'nucleotidase/nuclease protein.

Y. Boublik, Ines Lakhal-Naouar, H. Louzir, 2008, Biochemical and biophysical research communications.

Two distinct regions of calponin share common binding sites on actin resulting in different modes of calponin-actin interaction.

M. Manai, Y. Benyamin, S. Maciver, 2010, Biochimica et biophysica acta.

Characterization of the Regulatory Domain of Gizzard Calponin

C. Mendre, B. Calas, R. Kassab, 1995, The Journal of Biological Chemistry.

Expressing functional domains of mouse calponin: involvement of the region around alanine 145 in the actomyosin ATPase inhibitory activity of calponin.

M. Gimona, P. Strasser, A. Fattoum, 1996, Biochemistry.

Mapping of the functional domains in the amino-terminal region of calponin.

J. Derancourt, R. Kassab, A. Fattoum, 1992, The Journal of biological chemistry.

The activation of gelsolin by low pH: the calcium latch is sensitive to calcium but not pH.

Y. Benyamin, S. Maciver, C. Roustan, 2003, European journal of biochemistry.

Flexibility of actin filaments derived from thermal fluctuations. Effect of bound nucleotide, phalloidin, and muscle regulatory proteins

H. Isambert, P. Venier, A. Maggs, 1995, The Journal of Biological Chemistry.

Isolation and structural properties of a high-molecular-weight actin-binding protein (filamin-like protein) in hog thyroid gland.

L. Pradel, Y. Benyamin, C. Roustan, 1982, European journal of biochemistry.

Biochemical evidence for a low molecular weight protein (profilin‐like protein) in hog thyroid gland and its involvement in actin polymerisation

L. Pradel, C. Roustan, A. Fattoum, 1980, FEBS letters.

Tyrosine phosphorylation of calponins. Inhibition of the interaction with F-actin.

M. Gimona, R. Kassab, C. Benistant, 2004, European journal of biochemistry.

Precise identification of the regulatory F-actin- and calmodulin-binding sequences in the 10-kDa carboxyl-terminal domain of caldesmon.

J. Derancourt, B. Calas, R. Kassab, 1994, The Journal of biological chemistry.

Interaction of yeast 3-phosphoglycerate kinase with negatively charged carriers.

L. Pradel, C. Roustan, D. Schuhmann, 1982, Biophysical chemistry.

Structural Studies on Yeast 3-Phosphoglycerate Kinase

L. Pradel, G. Desvages, C. Roustan, 1978 .

Binding of gelsolin domain 2 to actin. An actin interface distinct from that of gelsolin domain 1 and from ADF/cofilin.

L. Blondin, F. Raynaud, Y. Benyamin, 2001, European journal of biochemistry.

The Identification of a Second Cofilin Binding Site on Actin Suggests a Novel, Intercalated Arrangement of F-actin Binding*

Y. Benyamin, C. Astier, S. Maciver, 1999, The Journal of Biological Chemistry.

Gelsolin binds to polyphosphoinositide-free lipid vesicles and simultaneously to actin microfilaments.

Y. Benyamin, N. Bettache, S. Maciver, 2005, The Biochemical journal.

Two distinct sites of interaction form the calponin: gelsolin complex and two calcium switches control its activity.

M. Manai, Y. Benyamin, S. Maciver, 2007, Biochimica et biophysica acta.

A direct interaction with calponin inhibits the actin-nucleating activity of gelsolin.

M. Manai, Y. Benyamin, S. Maciver, 2006, The Biochemical journal.

Interaction of F-actin with synthetic peptides spanning the loop region of human cardiac beta-myosin heavy chain containing Arg403.

A. Bartegi, A. Chavanieu, C. Roustan, 1997, European journal of biochemistry.

Mapping the microtubule binding regions of calponin.

C. Roustan, R. Kassab, A. Fattoum, 2003, Biochemistry.

A functional tyrosyl residue in arginine kinase, studied by nitration with tetranitromethane.

L. Pradel, R. Kassab, A. Fattoum, 1970, European journal of biochemistry.