Understanding the mechanism of proteasome 20S core particle gating (original) (raw)

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A Tetrahedral Transition State at the Active Sites of the 20S Proteasome Is Coupled to Opening of the α-Ring Channel

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Probing Structural Determinants Distal to the Site of Hydrolysis that Control Substrate Specificity of the 20S Proteasome

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Structural Models for Interactions between the 20S Proteasome and Its PAN/19S Activators

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Conformational constraints for protein self-cleavage in the proteasome

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Dependence of Proteasome Processing Rate on Substrate Unfolding

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Allosteric coupling between α-rings of the 20S proteasome

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2010

Conformational constraints for protein self-cleavage in the proteasome1

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Observing Protein Degradation by the PAN-20S Proteasome by Time-Resolved Neutron Scattering

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PACemakers of Proteasome Core Particle Assembly

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The Direction of Protein Entry into the Proteasome Determines the Variety of Products and Depends on the Force Needed to Unfold Its Two Termini

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Molecular architecture of the 26S proteasome holocomplex determined by an integrative approach

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Gyre and gimble in the proteasome

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Docking of the Proteasomal ATPases' Carboxyl Termini in the 20S Proteasome's α Ring Opens the Gate for Substrate Entry

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The catalytic sites of 20S proteasomes and their role in subunit maturation: A mutational and crystallographic study

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Proteasome Channel Opening as a Rate-Limiting Step in the Ubiquitin-Proteasome System

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Israel Journal of Chemistry, 2006

Redox Control of 20S Proteasome Gating

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An unstructured initiation site is required for efficient proteasome-mediated degradation

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A role for the proteasome alpha2 subunit N-tail in substrate processing