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J Parello

Showing results (21-30 of 46) with videos related to

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The Journal of Biological Chemistry|February 22, 2000
A minimized human integrin alpha(5)beta(1) that retains ligand recognitionJ L Banères, F Roquet, A Martin, et al.
Biophysical Journal|May 8, 1999
Hydration-coupled dynamics in proteins studied by neutron scattering and NMR: the case of the typical EF-hand calcium-binding parvalbuminJ M Zanotti, M C Bellissent-Funel, J Parello
Protein Science : a Publication of the Protein Society|November 5, 1999
Crystal structure of the EF-hand parvalbumin at atomic resolution (0.91 A) and at low temperature (100 K). Evidence for conformational multistates within the hydrophobic coreJ P Declercq, C Evrard, V Lamzin, et al.
Proceedings of the National Academy of Sciences of the United States of America|November 1, 1976
Superstructure of linear duplex DNAH J Vollenweider, T Koller, J Parello, et al.
FEBS Letters|June 1, 1976
Conformation mobility within the structure of muscular parvalbumins. An NMR study of the aromatic resonances of phenylalanine residuesA Cave, C M Dobson, J Parello, et al.
FEBS Letters|April 1, 1979
Mg2+ binding to parvalbumins studied by 25Mg and 113Cd NMR spectroscopyA Cave, J Parello, T Drakenberg, et al.
FEBS Letters|December 15, 1979
Counterion NMR in polyelectrolyte solutions. 25Mg2+ and 43Ca2+ interaction DNAP Reimarsson, J Parello, T Drakenberg, et al.
Journal of Molecular Biology|February 5, 1992
Crystal structure of the unique parvalbumin component from muscle of the leopard shark (Triakis semifasciata). The first X-ray study of an alpha-parvalbuminF Roquet, J P Declercq, B Tinant, et al.
The Journal of Biological Chemistry|September 12, 1998
The cation-binding domain from the alpha subunit of integrin alpha5 beta1 is a minimal domain for fibronectin recognitionJ L Banères, F Roquet, M Green, et al.
Journal of Molecular Biology|July 20, 1988
Crystal structure determination and refinement of pike 4.10 parvalbumin (minor component from Esox lucius)J P Declercq, B Tinant, J Parello, et al.
Pageof 5

Showing results (21-30 of 46) with videos related to

Sort By:
Pageof 5
The Journal of Biological Chemistry|February 22, 2000
A minimized human integrin alpha(5)beta(1) that retains ligand recognitionJ L Banères, F Roquet, A Martin, et al.
Biophysical Journal|May 8, 1999
Hydration-coupled dynamics in proteins studied by neutron scattering and NMR: the case of the typical EF-hand calcium-binding parvalbuminJ M Zanotti, M C Bellissent-Funel, J Parello
Protein Science : a Publication of the Protein Society|November 5, 1999
Crystal structure of the EF-hand parvalbumin at atomic resolution (0.91 A) and at low temperature (100 K). Evidence for conformational multistates within the hydrophobic coreJ P Declercq, C Evrard, V Lamzin, et al.
Proceedings of the National Academy of Sciences of the United States of America|November 1, 1976
Superstructure of linear duplex DNAH J Vollenweider, T Koller, J Parello, et al.
FEBS Letters|June 1, 1976
Conformation mobility within the structure of muscular parvalbumins. An NMR study of the aromatic resonances of phenylalanine residuesA Cave, C M Dobson, J Parello, et al.
FEBS Letters|April 1, 1979
Mg2+ binding to parvalbumins studied by 25Mg and 113Cd NMR spectroscopyA Cave, J Parello, T Drakenberg, et al.
FEBS Letters|December 15, 1979
Counterion NMR in polyelectrolyte solutions. 25Mg2+ and 43Ca2+ interaction DNAP Reimarsson, J Parello, T Drakenberg, et al.
Journal of Molecular Biology|February 5, 1992
Crystal structure of the unique parvalbumin component from muscle of the leopard shark (Triakis semifasciata). The first X-ray study of an alpha-parvalbuminF Roquet, J P Declercq, B Tinant, et al.
The Journal of Biological Chemistry|September 12, 1998
The cation-binding domain from the alpha subunit of integrin alpha5 beta1 is a minimal domain for fibronectin recognitionJ L Banères, F Roquet, M Green, et al.
Journal of Molecular Biology|July 20, 1988
Crystal structure determination and refinement of pike 4.10 parvalbumin (minor component from Esox lucius)J P Declercq, B Tinant, J Parello, et al.
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