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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.
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.
Activation mechanisms of coagulation factor IX.
Zögg T, Brandstetter H. Zögg T, et al. Among authors: brandstetter h. Biol Chem. 2009 May-Jun;390(5-6):391-400. doi: 10.1515/BC.2009.057. Biol Chem. 2009. PMID: 19361276 Review.
Structural basis of the cofactor- and substrate-assisted activation of human coagulation factor IXa.
Zögg T, Brandstetter H. Zögg T, et al. Among authors: brandstetter h. Structure. 2009 Dec 9;17(12):1669-1678. doi: 10.1016/j.str.2009.10.011. Structure. 2009. PMID: 20004170
Crystal structure of the NADP-dependent mannitol dehydrogenase from Cladosporium herbarum: Implications for oligomerisation and catalysis.
Nüss D, Goettig P, Magler I, Denk U, Breitenbach M, Schneider PB, Brandstetter H, Simon-Nobbe B. Nüss D, et al. Among authors: brandstetter h. Biochimie. 2010 Aug;92(8):985-93. doi: 10.1016/j.biochi.2010.04.012. Epub 2010 Apr 24. Biochimie. 2010. PMID: 20420880
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
Complex assemblies of factors IX and X regulate the initiation, maintenance, and shutdown of blood coagulation.
Zögg T, Brandstetter H. Zögg T, et al. Among authors: brandstetter h. Prog Mol Biol Transl Sci. 2011;99:51-103. doi: 10.1016/B978-0-12-385504-6.00002-6. Prog Mol Biol Transl Sci. 2011. PMID: 21238934 Review.
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
Structure of collagenase G reveals a chew-and-digest mechanism of bacterial collagenolysis.
Eckhard U, Schönauer E, Nüss D, Brandstetter H. Eckhard U, et al. Among authors: brandstetter h. Nat Struct Mol Biol. 2011 Sep 25;18(10):1109-14. doi: 10.1038/nsmb.2127. Nat Struct Mol Biol. 2011. PMID: 21947205 Free PMC article.
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.
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