scholarly article | Q13442814 |
P356 | DOI | 10.3390/IJMS20092231 |
P953 | full work available at URL | https://www.mdpi.com/1422-0067/20/9/2231 |
P932 | PMC publication ID | 6539346 |
P698 | PubMed publication ID | 31067643 |
P50 | author | Koichi Kato | Q57030726 |
Maho Yagi-Utsumi | Q61097228 | ||
Tadashi Satoh | Q73227431 | ||
P2093 | author name string | Kenta Okamoto | |
Keiji Tanaka | |||
Koichi Kato | |||
Tadashi Satoh | |||
Maho Yagi-Utsumi | |||
Eiji Kurimoto | |||
P2860 | cites work | Pba3-Pba4 heterodimer acts as a molecular matchmaker in proteasome α-ring formation. | Q53509643 |
PAC1-PAC2 proteasome assembly chaperone retains the core α4-α7 assembly intermediates in the cytoplasm | Q64166841 | ||
MolProbity: all-atom structure validation for macromolecular crystallography | Q24649111 | ||
Crystal structure of a chaperone complex that contributes to the assembly of yeast 20S proteasomes | Q27649865 | ||
Molecular architecture and assembly of the eukaryotic proteasome | Q27693890 | ||
The inhibition mechanism of human 20S proteasomes enables next-generation inhibitor design | Q27725464 | ||
XDS | Q27860472 | ||
The CCPN data model for NMR spectroscopy: development of a software pipeline | Q27860601 | ||
NMRPipe: a multidimensional spectral processing system based on UNIX pipes | Q27860859 | ||
Automated macromolecular model building for X-ray crystallography using ARP/wARP version 7 | Q27860936 | ||
Refinement of macromolecular structures by the maximum-likelihood method | Q27861011 | ||
Features and development of Coot | Q27861079 | ||
20S proteasome assembly is orchestrated by two distinct pairs of chaperones in yeast and in mammals. | Q27936515 | ||
The proteasome: a novel target for cancer chemotherapy | Q28215095 | ||
An introduction to data reduction: space-group determination, scaling and intensity statistics | Q29547659 | ||
The proteasome: paradigm of a self-compartmentalizing protease | Q29615187 | ||
Cooperation of multiple chaperones required for the assembly of mammalian 20S proteasomes | Q34594682 | ||
Molecular mechanisms of proteasome assembly | Q34928594 | ||
Kinetic asymmetry of subunit exchange of homooligomeric protein as revealed by deuteration-assisted small-angle neutron scattering | Q35342400 | ||
Bortezomib as the first proteasome inhibitor anticancer drug: current status and future perspectives | Q35836881 | ||
Disassembly of the self-assembled, double-ring structure of proteasome α7 homo-tetradecamer by α6. | Q36367257 | ||
The proteasome: overview of structure and functions | Q36472495 | ||
A fast and accurate computational approach to protein ionization | Q36962666 | ||
Structural biology of the proteasome | Q38081952 | ||
MicroRNA-101 Suppresses Tumor Cell Proliferation by Acting as an Endogenous Proteasome Inhibitor via Targeting the Proteasome Assembly Factor POMP. | Q38856491 | ||
Crystal structure of human proteasome assembly chaperone PAC4 involved in proteasome formation. | Q38927230 | ||
The Logic of the 26S Proteasome | Q39318404 | ||
Proteasome Structure and Assembly | Q39352782 | ||
Backbone and side chain 1H, 13C, and 15N assignments of the ubiquitin-like domain of human HOIL-1L, an essential component of linear ubiquitin chain assembly complex | Q44462227 | ||
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 formation | Q47247682 | ||
P275 | copyright license | Creative Commons Attribution 4.0 International | Q20007257 |
P6216 | copyright status | copyrighted | Q50423863 |
P433 | issue | 9 | |
P407 | language of work or name | English | Q1860 |
P304 | page(s) | 2231 | |
P577 | publication date | 2019-01-01 | |
2019-05-07 | |||
P1433 | published in | International Journal of Molecular Sciences | Q3153277 |
P1476 | title | Molecular and Structural Basis of the Proteasome α Subunit Assembly Mechanism Mediated by the Proteasome-Assembling Chaperone PAC3-PAC4 Heterodimer | |
P478 | volume | 20 |
Q64990528 | Mutational and Combinatorial Control of Self-Assembling and Disassembling of Human Proteasome α Subunits. |
Q90339359 | Proteomic analysis of affinity-purified 26S proteasomes identifies a suite of assembly chaperones in Arabidopsis |
Q95650650 | The proteasome as a druggable target with multiple therapeutic potentialities: Cutting and non-cutting edges |
Search more.