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J Schleucher

Showing results (11-20 of 14) with videos related to

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Journal of Molecular Biology|May 18, 1999
The solution structure of the homeodomain of the rat insulin-gene enhancer protein isl-1. Comparison with other homeodomainsH Ippel, G Larsson, G Behravan, et al.
Journal of Biomolecular NMR|March 1, 1994
A general enhancement scheme in heteronuclear multidimensional NMR employing pulsed field gradientsJ Schleucher, M Schwendinger, M Sattler, et al.
Molecular and Cellular Biology|November 14, 2000
Mutational and structural analyses of the ribonucleotide reductase inhibitor Sml1 define its Rnr1 interaction domain whose inactivation allows suppression of mec1 and rad53 lethalityX Zhao, B Georgieva, A Chabes, et al.
Biochemistry|February 20, 2003
Global structure and dynamics of human apolipoprotein CII in complex with micelles: evidence for increased mobility of the helix involved in the activation of lipoprotein lipaseJ Zdunek, G V Martinez, J Schleucher, et al.
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Showing results (11-20 of 14) with videos related to

Sort By:
Pageof 2
You have reached the last page of results.This site can display upto 14 results.
Journal of Molecular Biology|May 18, 1999
The solution structure of the homeodomain of the rat insulin-gene enhancer protein isl-1. Comparison with other homeodomainsH Ippel, G Larsson, G Behravan, et al.
Journal of Biomolecular NMR|March 1, 1994
A general enhancement scheme in heteronuclear multidimensional NMR employing pulsed field gradientsJ Schleucher, M Schwendinger, M Sattler, et al.
Molecular and Cellular Biology|November 14, 2000
Mutational and structural analyses of the ribonucleotide reductase inhibitor Sml1 define its Rnr1 interaction domain whose inactivation allows suppression of mec1 and rad53 lethalityX Zhao, B Georgieva, A Chabes, et al.
Biochemistry|February 20, 2003
Global structure and dynamics of human apolipoprotein CII in complex with micelles: evidence for increased mobility of the helix involved in the activation of lipoprotein lipaseJ Zdunek, G V Martinez, J Schleucher, et al.
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