Brandstetter H - Search Results

1

Structures of the NLRP14 pyrin domain reveal a conformational switch mechanism regulating its molecular interactions.

Eibl C, Hessenberger M, Wenger J, Brandstetter H. Eibl C, et al. Among authors: brandstetter h. Acta Crystallogr D Biol Crystallogr. 2014 Jul;70(Pt 7):2007-18. doi: 10.1107/S1399004714010311. Epub 2014 Jun 29. Acta Crystallogr D Biol Crystallogr. 2014. PMID: 25004977 Free PMC article.

2

Structural basis for activity regulation and substrate preference of clostridial collagenases G, H, and T.

Eckhard U, Schönauer E, Brandstetter H. Eckhard U, et al. Among authors: brandstetter h. J Biol Chem. 2013 Jul 12;288(28):20184-94. doi: 10.1074/jbc.M112.448548. Epub 2013 May 23. J Biol Chem. 2013. PMID: 23703618 Free PMC article.

3

Crystallization and preliminary X-ray characterization of the catalytic domain of collagenase G from Clostridium histolyticum.

Eckhard U, Nüss D, Ducka P, Schönauer E, Brandstetter H. Eckhard U, et al. Among authors: brandstetter h. Acta Crystallogr Sect F Struct Biol Cryst Commun. 2008 May 1;64(Pt 5):419-21. doi: 10.1107/S1744309108010476. Epub 2008 Apr 24. Acta Crystallogr Sect F Struct Biol Cryst Commun. 2008. PMID: 18453715 Free PMC article.

4

Molecular metamorphosis in polcalcin allergens by EF-hand rearrangements and domain swapping.

Magler I, Nüss D, Hauser M, Ferreira F, Brandstetter H. Magler I, et al. Among authors: brandstetter h. FEBS J. 2010 Jun;277(12):2598-610. doi: 10.1111/j.1742-464X.2010.07671.x. FEBS J. 2010. PMID: 20553495 Free article.

5

Polycystic kidney disease-like domains of clostridial collagenases and their role in collagen recruitment.

Eckhard U, Brandstetter H. Eckhard U, et al. Among authors: brandstetter h. Biol Chem. 2011 Nov;392(11):1039-45. doi: 10.1515/BC.2011.099. Epub 2011 Aug 28. Biol Chem. 2011. PMID: 21871007

6

Real space refinement of crystal structures with canonical distributions of electrons.

Ginzinger SW, Gruber M, Brandstetter H, Sippl MJ. Ginzinger SW, et al. Among authors: brandstetter h. Structure. 2011 Dec 7;19(12):1739-43. doi: 10.1016/j.str.2011.10.011. Structure. 2011. PMID: 22153496 Free PMC article.

7

Activation of legumain involves proteolytic and conformational events, resulting in a context- and substrate-dependent activity profile.

Dall E, Brandstetter H. Dall E, et al. Among authors: brandstetter h. Acta Crystallogr Sect F Struct Biol Cryst Commun. 2012 Jan 1;68(Pt 1):24-31. doi: 10.1107/S1744309111048020. Epub 2011 Dec 24. Acta Crystallogr Sect F Struct Biol Cryst Commun. 2012. PMID: 22232165 Free PMC article.

8

Mechanistic and structural studies on legumain explain its zymogenicity, distinct activation pathways, and regulation.

Dall E, Brandstetter H. Dall E, et al. Among authors: brandstetter h. Proc Natl Acad Sci U S A. 2013 Jul 2;110(27):10940-5. doi: 10.1073/pnas.1300686110. Epub 2013 Jun 17. Proc Natl Acad Sci U S A. 2013. PMID: 23776206 Free PMC article.

9

Structure-function analyses of human kallikrein-related peptidase 2 establish the 99-loop as master regulator of activity.

Skala W, Utzschneider DT, Magdolen V, Debela M, Guo S, Craik CS, Brandstetter H, Goettig P. Skala W, et al. Among authors: brandstetter h. J Biol Chem. 2014 Dec 5;289(49):34267-83. doi: 10.1074/jbc.M114.598201. Epub 2014 Oct 16. J Biol Chem. 2014. PMID: 25326387 Free PMC article.

10

Structure and mechanism of an aspartimide-dependent peptide ligase in human legumain.

Dall E, Fegg JC, Briza P, Brandstetter H. Dall E, et al. Among authors: brandstetter h. Angew Chem Int Ed Engl. 2015 Mar 2;54(10):2917-21. doi: 10.1002/anie.201409135. Epub 2015 Jan 28. Angew Chem Int Ed Engl. 2015. PMID: 25630877 Free PMC article.

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