Buchner J - Search Results

1

Reduction of disulphide bonds unmasks potent antimicrobial activity of human β-defensin 1.

Schroeder BO, Wu Z, Nuding S, Groscurth S, Marcinowski M, Beisner J, Buchner J, Schaller M, Stange EF, Wehkamp J. Schroeder BO, et al. Among authors: buchner j. Nature. 2011 Jan 20;469(7330):419-23. doi: 10.1038/nature09674. Nature. 2011. PMID: 21248850

2

Substrate discrimination of the chaperone BiP by autonomous and cochaperone-regulated conformational transitions.

Marcinowski M, Höller M, Feige MJ, Baerend D, Lamb DC, Buchner J. Marcinowski M, et al. Among authors: buchner j. Nat Struct Mol Biol. 2011 Feb;18(2):150-8. doi: 10.1038/nsmb.1970. Epub 2011 Jan 9. Nat Struct Mol Biol. 2011. PMID: 21217698

3

The structure of a folding intermediate provides insight into differences in immunoglobulin amyloidogenicity.

Feige MJ, Groscurth S, Marcinowski M, Yew ZT, Truffault V, Paci E, Kessler H, Buchner J. Feige MJ, et al. Among authors: buchner j. Proc Natl Acad Sci U S A. 2008 Sep 9;105(36):13373-8. doi: 10.1073/pnas.0802809105. Epub 2008 Sep 3. Proc Natl Acad Sci U S A. 2008. PMID: 18768806 Free PMC article.

4

An unfolded CH1 domain controls the assembly and secretion of IgG antibodies.

Feige MJ, Groscurth S, Marcinowski M, Shimizu Y, Kessler H, Hendershot LM, Buchner J. Feige MJ, et al. Among authors: buchner j. Mol Cell. 2009 Jun 12;34(5):569-79. doi: 10.1016/j.molcel.2009.04.028. Mol Cell. 2009. PMID: 19524537 Free PMC article.

5

Conformational selection in substrate recognition by Hsp70 chaperones.

Marcinowski M, Rosam M, Seitz C, Elferich J, Behnke J, Bello C, Feige MJ, Becker CF, Antes I, Buchner J. Marcinowski M, et al. Among authors: buchner j. J Mol Biol. 2013 Feb 8;425(3):466-74. doi: 10.1016/j.jmb.2012.11.030. Epub 2012 Dec 1. J Mol Biol. 2013. PMID: 23207294

6

The structural analysis of shark IgNAR antibodies reveals evolutionary principles of immunoglobulins.

Feige MJ, Gräwert MA, Marcinowski M, Hennig J, Behnke J, Ausländer D, Herold EM, Peschek J, Castro CD, Flajnik M, Hendershot LM, Sattler M, Groll M, Buchner J. Feige MJ, et al. Among authors: buchner j. Proc Natl Acad Sci U S A. 2014 Jun 3;111(22):8155-60. doi: 10.1073/pnas.1321502111. Epub 2014 May 15. Proc Natl Acad Sci U S A. 2014. PMID: 24830426 Free PMC article.

7

Hsp90 chaperones protein folding in vitro.

Wiech H, Buchner J, Zimmermann R, Jakob U. Wiech H, et al. Among authors: buchner j. Nature. 1992 Jul 9;358(6382):169-70. doi: 10.1038/358169a0. Nature. 1992. PMID: 1614549

8

The structure and oxidation of the eye lens chaperone αA-crystallin.

Kaiser CJO, Peters C, Schmid PWN, Stavropoulou M, Zou J, Dahiya V, Mymrikov EV, Rockel B, Asami S, Haslbeck M, Rappsilber J, Reif B, Zacharias M, Buchner J, Weinkauf S. Kaiser CJO, et al. Among authors: buchner j. Nat Struct Mol Biol. 2019 Dec;26(12):1141-1150. doi: 10.1038/s41594-019-0332-9. Epub 2019 Dec 2. Nat Struct Mol Biol. 2019. PMID: 31792453 Free PMC article.

9

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: buchner j. Nat Commun. 2020 Mar 16;11(1):1410. doi: 10.1038/s41467-020-15050-0. Nat Commun. 2020. PMID: 32179743 Free PMC article.

10

Phosphorylation activates the yeast small heat shock protein Hsp26 by weakening domain contacts in the oligomer ensemble.

Mühlhofer M, Peters C, Kriehuber T, Kreuzeder M, Kazman P, Rodina N, Reif B, Haslbeck M, Weinkauf S, Buchner J. Mühlhofer M, et al. Among authors: buchner j. Nat Commun. 2021 Nov 18;12(1):6697. doi: 10.1038/s41467-021-27036-7. Nat Commun. 2021. PMID: 34795272 Free PMC article.

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