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Hans Brandstetter

Hans Brandstetter

D-Index & Metrics

Biology and Biochemistry

D-Index
47
Citations
8141
World Ranking
18703
National Ranking
171

Overview

Hans Brandstetter is affiliated with the University of Salzburg in Austria. Their research primarily spans the fields of biochemistry, genetics, and molecular biology, with a focused engagement in medicine. The main subfields of study include molecular biology, biotechnology, plant science, cell biology, and microbiology.

The scientist's work covers several key research topics such as biochemical and structural characterization, enzyme production and characterization, antimicrobial peptides and activities, transgenic plants and applications, ubiquitin and proteasome pathways, phytase and its applications, and peptidase inhibition and analysis.

Frequent collaborators in their research include Elfriede Dall, Sven O. Dahms, Esther Schönauer, Christian G. Huber, and Peter Briza.

Key recent publications by Hans Brandstetter include:

  • Ligand Binding of PR-10 Proteins with a Particular Focus on the Bet v 1 Allergen Family (2020), published in Current Allergy and Asthma Reports
  • N-Aryl-3-mercaptosuccinimides as Antivirulence Agents Targeting Pseudomonas aeruginosa Elastase and Clostridium Collagenases (2020), Journal of Medicinal Chemistry
  • Structural and functional studies of Arabidopsis thaliana legumain beta reveal isoform specific mechanisms of activation and substrate recognition (2020), Journal of Biological Chemistry
  • The Peptide Ligase Activity of Human Legumain Depends on Fold Stabilization and Balanced Substrate Affinities (2021), ACS Catalysis
  • ExteNDing Proteome Coverage with Legumain as a Highly Specific Digestion Protease (2020), Analytical Chemistry

Hans Brandstetter has published frequently in venues such as the International Journal of Molecular Sciences, ChemMedChem, bioRxiv (Cold Spring Harbor Laboratory), Journal of Medicinal Chemistry, and STAR Protocols.

Best Publications

  • The crystal structure of dipeptidyl peptidase IV (CD26) reveals its functional regulation and enzymatic mechanism

    Michael Engel;Torsten Hoffmann;Leona Wagner;Michael Wermann

  • X-ray Structure of Active Site-inhibited Clotting Factor Xa IMPLICATIONS FOR DRUG DESIGN AND SUBSTRATE RECOGNITION

    H Brandstetter;A Kühne;W Bode;R Huber

  • X-ray structure of clotting factor IXa: active site and module structure related to Xase activity and hemophilia B.

    Hans Brandstetter;Margit Bauer;Robert Huber;Pete Lollar

  • Molecular Machines for Protein Degradation

    Michael Groll;Matthias Bochtler;Hans Brandstetter;Tim Clausen

  • Refined 2.3 A X-ray crystal structure of bovine thrombin complexes formed with the benzamidine and arginine-based thrombin inhibitors NAPAP, 4-TAPAP and MQPA. A starting point for improving antithrombotics.

    H. Brandstetter;D. Turk;H.W. Hoeffken;D. Grosse

  • Structure and function of legumain in health and disease.

    Elfriede Dall;Hans Brandstetter

  • Crystal structures of the methane monooxygenase hydroxylase from Methylococcus capsulatus (Bath): implications for substrate gating and component interactions.

    Amy C. Rosenzweig;Hans Brandstetter;Hans Brandstetter;Douglas A. Whittington;Pär Nordlund

  • Mechanistic and Structural Studies on Legumain Explain its Zymogenicity, Distinct Activation Pathways, and Regulation

    Elfriede Dall;Hans Brandstetter

  • Structural basis of the adaptive molecular recognition by MMP9.

    Hyunju Cha;Erhard Kopetzki;Robert Huber;Martin Lanzendörfer

  • Natural and synthetic inhibitors of kallikrein-related peptidases (KLKs).

    Peter Goettig;Viktor Magdolen;Hans Brandstetter

  • Pyrimidine-2,4,6-Triones: a new effective and selective class of matrix metalloproteinase inhibitors.

    Grams F;Brandstetter H;D'Alò S;Geppert D

  • Coagulation factor IXa: the relaxed conformation of Tyr99 blocks substrate binding.

    Karl-Peter Hopfner;Anja Lang;Annette Karcher;Katrin Sichler

  • Comparative analysis of haemostatic proteinases : Structural aspects of thrombin, factor Xa, factor IXa and protein C

    Wolfram Bode;Hans Brandstetter;Timothy Mather;Milton T Stubbs

  • The 1.8-Å Crystal Structure of a Matrix Metalloproteinase 8-Barbiturate Inhibitor Complex Reveals a Previously Unobserved Mechanism for Collagenase Substrate Recognition

    Hans Brandstetter;Frank Grams;Dagmar Glitz;Anja Lang

  • Changing Residue 338 in Human Factor IX from Arginine to Alanine Causes an Increase in Catalytic Activity

    Jinli Chang;Jianping Jin;Pete Lollar;Wolfram Bode

  • Structure of collagenase G reveals a chew-and-digest mechanism of bacterial collagenolysis.

    Ulrich Eckhard;Esther Schönauer;Dorota Nüss;Hans Brandstetter

  • Enzyme flexibility, solvent and 'weak' interactions characterize thrombin-ligand interactions: implications for drug design.

    Richard A Engh;Hans Brandstetter;Gudrun Sucher;Andreas Eichinger

  • Investigations on the Maturation and Regulation of Archaebacterial Proteasomes

    Michael Groll;Hans Brandstetter;Hans Bartunik;Gleb Bourenkow

  • Crystal structure of the catalytic domain of human atypical protein kinase C-iota reveals interaction mode of phosphorylation site in turn motif.

    Albrecht Messerschmidt;Sofia Macieira;Milko Velarde;Mathias Bädeker

  • Inhibition of delta-secretase improves cognitive functions in mouse models of Alzheimer's disease.

    Zhentao Zhang;Zhentao Zhang;Obiamaka Obianyo;Elfriede Dall;Yuhong Du

Frequent Co-Authors

Robert Huber
Robert Huber University of Duisburg-Essen
Fatima Ferreira
Fatima Ferreira University of Salzburg
Wolfram Bode
Wolfram Bode Max Planck Society
Peter Briza
Peter Briza University of Salzburg
Richard A. Engh
Richard A. Engh University of Tromsø - The Arctic University of Norway
Albert Duschl
Albert Duschl University of Salzburg
Christian G. Huber
Christian G. Huber University of Salzburg
Michael Groll
Michael Groll Technical University of Munich
Viktor Magdolen
Viktor Magdolen Technical University of Munich
Karl-Peter Hopfner
Karl-Peter Hopfner Ludwig-Maximilians-Universität München

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