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Plant Physiology|March 1, 1995
Phytochrome A overexpression in transgenic tobacco. Correlation of dwarf phenotype with high concentrations of phytochrome in vascular tissue and attenuated gibberellin levelsE T Jordan, P M Hatfield, D Hondred, et al.
The Journal of Biological Chemistry|January 27, 1998
Multiubiquitin chain binding and protein degradation are mediated by distinct domains within the 26 S proteasome subunit Mcb1H Fu, S Sadis, D M Rubin, et al.
The Plant Cell|May 1, 1993
Carboxy-terminal deletion analysis of oat phytochrome A reveals the presence of separate domains required for structure and biological activityJ R Cherry, D Hondred, J M Walker, et al.
The Journal of Biological Chemistry|May 5, 1987
Comparison of the three-dimensional structures of human, yeast, and oat ubiquitinS Vijay-Kumar, C E Bugg, K D Wilkinson, et al.
Molecular Biology Reports|June 11, 1999
Structure and functional analysis of the 26S proteasome subunits from plantsH Fu, P A Girod, J H Doelling, et al.
The Plant Journal : for Cell and Molecular Biology|March 13, 1999
Sequences within both the N- and C-terminal domains of phytochrome A are required for PFR ubiquitination and degradationR C Clough, E T Jordan-Beebe, K N Lohman, et al.
Molecular and Cellular Biology|November 1, 1996
The multiubiquitin-chain-binding protein Mcb1 is a component of the 26S proteasome in Saccharomyces cerevisiae and plays a nonessential, substrate-specific role in protein turnoverS van Nocker, S Sadis, D M Rubin, et al.
Molecular Biology of the Cell|February 17, 2001
The cellular level of PR500, a protein complex related to the 19S regulatory particle of the proteasome, is regulated in response to stresses in plantsZ Peng, J M Staub, G Serino, et al.
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