Mutational and Combinatorial Control of Self-Assembling and Disassembling of Human Proteasome α Subunits.

scientific article published on 9 May 2019

Mutational and Combinatorial Control of Self-Assembling and Disassembling of Human Proteasome α Subunits. is …
instance of (P31):
scholarly articleQ13442814

External links are
P356DOI10.3390/IJMS20092308
P953full work available at URLhttps://www.mdpi.com/1422-0067/20/9/2308
P932PMC publication ID6539845
P698PubMed publication ID31075988

P50authorHiroki WatanabeQ64214420
Tadashi SatohQ73227431
Kazuyoshi MurataQ87703418
Chihong SongQ89454812
Hirokazu YagiQ40409305
Kentaro IshiiQ42323737
Takayuki UchihashiQ55856636
Susumu UchiyamaQ56285607
Koichi KatoQ57030726
Saeko YanakaQ57644596
P2093author name stringKoichi Kato
Hirokazu Yagi
Susumu Uchiyama
Tadashi Satoh
Kazuyoshi Murata
Hiroki Watanabe
Takayuki Uchihashi
Saeko Yanaka
Chihong Song
Kentaro Ishii
Eiji Kurimoto
Toshiya Kozai
Taichiro Sekiguchi
P2860cites workQuantitative dynamics and binding studies of the 20S proteasome by NMRQ59082478
PAC1-PAC2 proteasome assembly chaperone retains the core α4-α7 assembly intermediates in the cytoplasmQ64166841
Molecular and Structural Basis of the Proteasome α Subunit Assembly Mechanism Mediated by the Proteasome-Assembling Chaperone PAC3-PAC4 Heterodimer.Q64997430
Proteasome assembly from 15S precursors involves major conformational changes and recycling of the Pba1-Pba2 chaperoneQ86573364
The structure of the mammalian 20S proteasome at 2.75 A resolutionQ27638997
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Crystal structure of a chaperone complex that contributes to the assembly of yeast 20S proteasomesQ27649865
The inhibition mechanism of human 20S proteasomes enables next-generation inhibitor designQ27725464
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RELION: implementation of a Bayesian approach to cryo-EM structure determinationQ29547673
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AAA+ proteins: diversity in function, similarity in structureQ34738695
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Kinetic asymmetry of subunit exchange of homooligomeric protein as revealed by deuteration-assisted small-angle neutron scatteringQ35342400
Gates, Channels, and Switches: Elements of the Proteasome MachineQ35862786
Symmetries throughout organic evolutionQ36246323
Disassembly of the self-assembled, double-ring structure of proteasome α7 homo-tetradecamer by α6.Q36367257
The proteasome: overview of structure and functionsQ36472495
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Crystal structure of human proteasome assembly chaperone PAC4 involved in proteasome formation.Q38927230
The Logic of the 26S ProteasomeQ39318404
Proteasome Structure and AssemblyQ39352782
Computational design of trimeric influenza-neutralizing proteins targeting the hemagglutinin receptor binding site.Q40163658
Three-dimensional structure of the alpha1-beta complex in the skeletal muscle dihydropyridine receptor by single-particle electron microscopyQ43227369
Two-step process for disassembly mechanism of proteasome α7 homo-tetradecamer by α6 revealed by high-speed atomic force microscopy.Q46937287
Structural insights on the dynamics of proteasome formationQ47247682
Cyclic oligomer design with de novo αβ-proteinsQ47802240
Pba3-Pba4 heterodimer acts as a molecular matchmaker in proteasome α-ring formation.Q53509643
Guide to video recording of structure dynamics and dynamic processes of proteins by high-speed atomic force microscopy.Q54508514
The human alpha-type proteasomal subunit HsC8 forms a double ringlike structure, but does not assemble into proteasome-like particles with the beta-type subunits HsDelta or HsBPROS26.Q54567772
P275copyright licenseCreative Commons Attribution 4.0 InternationalQ20007257
P6216copyright statuscopyrightedQ50423863
P433issue9
P407language of work or nameEnglishQ1860
P921main subjectself-assemblyQ910150
P304page(s)2308
P577publication date2019-01-01
2019-05-09
P1433published inInternational Journal of Molecular SciencesQ3153277
P1476titleMutational and Combinatorial Control of Self-Assembling and Disassembling of Human Proteasome α Subunits
P478volume20

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Q89732218Biophysical research in Okazaki, Japancites workP2860