A gated channel into the proteasome core particle
By M. Groll, M. Bajorek, A. Köhler, L. Moroder, D. Rubin, R. Huber, M. Glickman, D. Finley. Nature Structural Biology, 2000
850 citations recorded by the source corpus.
Subfields: Cell Biology, Molecular Biology
View Paper: https://www.semanticscholar.org/paper/60c1efa793dfa01d47e382b51fadcd22b9dcea3d
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Citations in the corpus
- Protein degradation by the ubiquitin-proteasome pathway in normal and disease states. (2006, background): “The outer subunits of the 20S particle surround a narrow, central, and gated pore through which substrates enter and products exit (41).”
- Recognition and Processing of Ubiquitin-Protein Conjugates by the Proteasome (2009, background): “The process of channel opening can be evaluated by monitoring the hydrolysis of peptide substrates (6).”
- Complete subunit architecture of the proteasome regulatory particle (2012, neutral): “The tails of Rpt1, 4, and 6 lack this motif and were not observed to statically interact with 20S in our holoenzyme structure.”
- Multiple associated proteins regulate proteasome structure and function. (2002, background): “…such as polymerases, molecular of the N-terminal tails of the subunits (Whitby et al., chaperones, ribosomes, cytoskeletal fibers, and nuclear 2000; Groll et al., 2000; Köhler et al., 2001). pores, loosely associated cofactors are critical for func- An eight-subunit subcomplex of the RP, the lid,…”
- Computational approaches for detecting protein complexes from protein interaction networks: a survey (2010, background): “It is involved in the degradation of proteins, which is an essential process within the cell [7]; the nuclear pore complex is responsible for the protected exchange of components between the nucleus and cytoplasm and for preventing the transport of material not destined to cross the nuclear membrane”
- The Logic of the 26S Proteasome. (2017, neutral): “Non-selective entry and destruction of cell proteins in the 20S particle are prevented by N termini of the 20S a-subunits, which protrude into this central channel to formagate (Groll et al., 2000).”