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          Institute: MPI für Biochemie     Collection: Structural Biology (W. Baumeister)     Display Documents



ID: 318770.0, MPI für Biochemie / Structural Biology (W. Baumeister)
Proteasome: from structure to function
Authors:Stock, D.; Nederlof, P. M.; Seemüller, E.; Baumeister, W.; Huber, R.; Löwe, J.
Date of Publication (YYYY-MM-DD):1996
Title of Journal:Current Opinion in Biotechnology.
Volume:7
Issue / Number:4
Start Page:376
End Page:385
Audience:Not Specified
Abstract / Description:During the past two years, significant progress has been made in understanding the structure and function of the proteasome. Recent work has revealed the three-dimensional structure of the 700 kDa proteolytic complex at atomic resolution and elucidated its novel catalytic mechanism. Close relationships to a number of other amino-terminal hydrolases have emerged, making the proteasomal subunits the prototype of this newly discovered structural superfamily. [References: 75]
Free Keywords:Animal; *Cysteine Endopeptidases/ch [Chemistry]; Cysteine Endopeptidases/im [Immunology]; *Cysteine Endopeptidases/ph [Physiology]; Human; Models, Biological; Models, Immunological; Models, Molecular; *Multienzyme Complexes/ch [Chemistry]; Multienzyme Complexes/im [Immunology]; *Multienzyme Complexes/ph [Physiology]; Protein Conformation; Protein Folding
External Publication Status:published
Document Type:Article
Communicated by:Anton Hillebrand
Affiliations:MPI für Biochemie/Structural Biology (W. Baumeister)/
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