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A methylated lysine is a switch point for conformational communication in the chaperone Hsp90.
Nat Commun. 2020 Mar 5;11(1):1219. doi: 10.1038/s41467-020-15048-8.
Nat Commun. 2020.
PMID: 32139682
Free PMC article.
Conformational dynamics modulate the catalytic activity of the molecular chaperone Hsp90.
Mader SL, Lopez A, Lawatscheck J, Luo Q, Rutz DA, Gamiz-Hernandez AP, Sattler M, Buchner J, Kaila VRI.
Mader SL, et al. Among authors: lawatscheck j.
Nat Commun. 2020 Mar 16;11(1):1410. doi: 10.1038/s41467-020-15050-0.
Nat Commun. 2020.
PMID: 32179743
Free PMC article.
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Author Correction: A methylated lysine is a switch point for conformational communication in the chaperone Hsp90.
Rehn A, Lawatscheck J, Jokisch ML, Mader SL, Luo Q, Tippel F, Blank B, Richter K, Lang K, Kaila VRI, Buchner J.
Rehn A, et al. Among authors: lawatscheck j.
Nat Commun. 2020 Jul 21;11(1):3727. doi: 10.1038/s41467-020-17621-7.
Nat Commun. 2020.
PMID: 32694502
Free PMC article.
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Structural elements in the flexible tail of the co-chaperone p23 coordinate client binding and progression of the Hsp90 chaperone cycle.
Biebl MM, Lopez A, Rehn A, Freiburger L, Lawatscheck J, Blank B, Sattler M, Buchner J.
Biebl MM, et al. Among authors: lawatscheck j.
Nat Commun. 2021 Feb 5;12(1):828. doi: 10.1038/s41467-021-21063-0.
Nat Commun. 2021.
PMID: 33547294
Free PMC article.
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Coordinated Conformational Processing of the Tumor Suppressor Protein p53 by the Hsp70 and Hsp90 Chaperone Machineries.
Dahiya V, Agam G, Lawatscheck J, Rutz DA, Lamb DC, Buchner J.
Dahiya V, et al. Among authors: lawatscheck j.
Mol Cell. 2019 May 16;74(4):816-830.e7. doi: 10.1016/j.molcel.2019.03.026. Epub 2019 Apr 23.
Mol Cell. 2019.
PMID: 31027879
Free article.
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The switch from client holding to folding in the Hsp70/Hsp90 chaperone machineries is regulated by a direct interplay between co-chaperones.
Dahiya V, Rutz DA, Moessmer P, Mühlhofer M, Lawatscheck J, Rief M, Buchner J.
Dahiya V, et al. Among authors: lawatscheck j.
Mol Cell. 2022 Apr 21;82(8):1543-1556.e6. doi: 10.1016/j.molcel.2022.01.016. Epub 2022 Feb 16.
Mol Cell. 2022.
PMID: 35176233
Free article.
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The IMiD target CRBN determines HSP90 activity toward transmembrane proteins essential in multiple myeloma.
Heider M, Eichner R, Stroh J, Morath V, Kuisl A, Zecha J, Lawatscheck J, Baek K, Garz AK, Rudelius M, Deuschle FC, Keller U, Lemeer S, Verbeek M, Götze KS, Skerra A, Weber WA, Buchner J, Schulman BA, Kuster B, Fernández-Sáiz V, Bassermann F.
Heider M, et al. Among authors: lawatscheck j.
Mol Cell. 2021 Mar 18;81(6):1170-1186.e10. doi: 10.1016/j.molcel.2020.12.046. Epub 2021 Feb 10.
Mol Cell. 2021.
PMID: 33571422
Free PMC article.
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Cytosolic Hsp70 and Hsp40 chaperones enable the biogenesis of mitochondrial β-barrel proteins.
Jores T, Lawatscheck J, Beke V, Franz-Wachtel M, Yunoki K, Fitzgerald JC, Macek B, Endo T, Kalbacher H, Buchner J, Rapaport D.
Jores T, et al. Among authors: lawatscheck j.
J Cell Biol. 2018 Sep 3;217(9):3091-3108. doi: 10.1083/jcb.201712029. Epub 2018 Jun 21.
J Cell Biol. 2018.
PMID: 29930205
Free PMC article.
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