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Article title matches
- Category:Hsp104 (37 bytes)
1: List of pages with the keyword Hsp104
Page text matches
- 4hse (4,587 bytes)
14: ...he Hsp100 chaperone inhibition by GdmCl using the Hsp104 homolog ClpB from T. thermophilus. Initially, we ... - 8tqm (3,127 bytes)
11: ...ns include MATALPHA2, TBF1, SLK19, YMR090W, HIS3, HSP104, UBP6 and ARO8.<ref>PMID:11641273</ref> <ref>PMID... - Heat Shock Protein structures (27,185 bytes)
409: *Hsp104
411: **[[5kne]], [[6n8z]], [[6n8v]], [[6n8t]] – yHsp104 - Cryo EM<br />
412: **[[6ahf]] – yHsp104 (mutant) – Cryo EM<br />
413: **[[5u2u]], [[6amn]], [[5wbw]] – yHsp104 NTD<br />
414: **[[5vy8]] – yHsp104 + ADP<br /> - Category:Hsp104 (37 bytes)
1: List of pages with the keyword Hsp104 - 2m6m (2,900 bytes)
11: ...ns include MATALPHA2, TBF1, SLK19, YMR090W, HIS3, HSP104, UBP6 and ARO8.<ref>PMID:11641273</ref> <ref>PMID... - 4lj5 (4,279 bytes)
14: ...ecular chaperone ClpB, the bacterial homologue of Hsp104, which reactivates aggregated proteins under cell... - 4lj6 (4,358 bytes)
14: ...ecular chaperone ClpB, the bacterial homologue of Hsp104, which reactivates aggregated proteins under cell... - 4lj7 (4,374 bytes)
14: ...ecular chaperone ClpB, the bacterial homologue of Hsp104, which reactivates aggregated proteins under cell... - 4lj8 (4,285 bytes)
14: ...ecular chaperone ClpB, the bacterial homologue of Hsp104, which reactivates aggregated proteins under cell... - 4lj9 (4,362 bytes)
14: ...ecular chaperone ClpB, the bacterial homologue of Hsp104, which reactivates aggregated proteins under cell... - 4lja (4,436 bytes)
14: ...ecular chaperone ClpB, the bacterial homologue of Hsp104, which reactivates aggregated proteins under cell... - 8pda (4,815 bytes)
11: ...ns include MATALPHA2, TBF1, SLK19, YMR090W, HIS3, HSP104, UBP6 and ARO8.<ref>PMID:11641273</ref> <ref>PMID... - 8pd0 (4,798 bytes)
11: ...ns include MATALPHA2, TBF1, SLK19, YMR090W, HIS3, HSP104, UBP6 and ARO8.<ref>PMID:11641273</ref> <ref>PMID... - 5d4w (1,783 bytes)
2: ==Crystal structure of Hsp104== - 5kne (3,356 bytes)
2: ==CryoEM Reconstruction of Hsp104 Hexamer==
11: ...s of the prions [PSI+], [URE3] and [PIN+]. Excess HSP104 can also specifically cure cells of [PSI+].<ref>P... - 5u2l (1,581 bytes)
2: ==Crystal structure of the Hsp104 N-terminal domain from Candida albicans== - 5u2u (3,119 bytes)
2: ==Crystal structure of the Hsp104 N-terminal domain from Saccharomyces cerevisiae==
10: ...s of the prions [PSI+], [URE3] and [PIN+]. Excess HSP104 can also specifically cure cells of [PSI+].<ref>P... - 5vjh (5,521 bytes)
2: ==Closed State CryoEM Reconstruction of Hsp104:ATPyS and FITC casein==
12: ...s of the prions [PSI+], [URE3] and [PIN+]. Excess HSP104 can also specifically cure cells of [PSI+].<ref>P...
15: ...anism and substrate-responsive flexibility during Hsp104-catalyzed disaggregation.
17: ... translocation mechanism of the AAA+ disaggregase Hsp104.,Gates SN, Yokom AL, Lin J, Jackrel ME, Rizo AN, ...
48: [[Category: Hsp104]] - 5vya (5,498 bytes)
2: ==S. cerevisiae Hsp104:casein complex, Extended Conformation==
12: ...s of the prions [PSI+], [URE3] and [PIN+]. Excess HSP104 can also specifically cure cells of [PSI+].<ref>P...
15: ...anism and substrate-responsive flexibility during Hsp104-catalyzed disaggregation.
17: ... translocation mechanism of the AAA+ disaggregase Hsp104.,Gates SN, Yokom AL, Lin J, Jackrel ME, Rizo AN, ...
48: [[Category: Hsp104]] - 5vy8 (5,478 bytes)
2: ==S. cerevisiae Hsp104-ADP complex==
8: ..."><b>[[Gene|Gene:]]</b></td><td class="sblockDat">HSP104, YLL026W, L0948 ([http://www.ncbi.nlm.nih.gov/Tax...
12: ...s of the prions [PSI+], [URE3] and [PIN+]. Excess HSP104 can also specifically cure cells of [PSI+].<ref>P...
15: ...anism and substrate-responsive flexibility during Hsp104-catalyzed disaggregation.
17: ... translocation mechanism of the AAA+ disaggregase Hsp104.,Gates SN, Yokom AL, Lin J, Jackrel ME, Rizo AN, ...
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