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Richard A. Kammerer

Richard A. Kammerer

D-Index & Metrics

Biology and Biochemistry

D-Index
57
Citations
8599
World Ranking
14100
National Ranking
259

Overview

Richard A. Kammerer is affiliated with the Paul Scherrer Institute in Switzerland. Their research primarily spans the fields of biochemistry, genetics, and molecular biology, with significant contributions also made in medicine. Within these broad domains, their key subfields of study include molecular biology, neurology, cellular and molecular neuroscience, endocrinology, and cell biology.

The scientist's main research topics encompass areas such as botulinum toxin and related neurological disorders, genetic neurodegenerative diseases, neurological disorders and treatments, bacterial genetics and biotechnology, Escherichia coli research, Vibrio bacteria research, and erythrocyte function and pathophysiology.

Richard A. Kammerer's body of work includes multiple publications in respected venues. Frequent publication sites include:

  • Nature Communications
  • bioRxiv (Cold Spring Harbor Laboratory)
  • Advanced Synthesis & Catalysis
  • Biochimica et Biophysica Acta (BBA) - Biomembranes
  • Virulence

Recent research papers authored or co-authored by Kammerer include:

  • The role of the N-terminal amphipathic helix in bacterial YidC: Insights from functional studies, the crystal structure and molecular dynamics simulations (2021, Biochimica et Biophysica Acta (BBA) - Biomembranes)
  • High-Level Production of Phenylacetaldehyde using Fusion-Tagged Styrene Oxide Isomerase (2021, Advanced Synthesis & Catalysis)
  • Targeting virulence regulation to disarm Acinetobacter baumannii pathogenesis (2022, Virulence)
  • A DARPin promotes faster onset of botulinum neurotoxin A1 action (2023, Nature Communications)
  • Structural basis of the Meinwald rearrangement catalysed by styrene oxide isomerase (2024, Nature Chemistry)

Collaboration has been an integral part of Kammerer's work. Frequent co-authors include Xiaodan Li, Oneda Leka, Daniel Frey, Volodymyr M. Korkhov, and Joel P. S. Choo.

Best Publications

  • The crystal structure of a five-stranded coiled coil in COMP: a prototype ion channel?

    Vladimir N. Malashkevich;Richard A. Kammerer;Vladimir P. Efimov;Therese Schulthess

  • Stabilization of short collagen-like triple helices by protein engineering.

    Sabine Frank;Richard A Kammerer;Diane Mechling;Therese Schulthess

  • COMP-Ang1: A designed angiopoietin-1 variant with nonleaky angiogenic activity

    Chung Hyun Cho;Richard A. Kammerer;Hyuek Jong Lee;Michel O. Steinmetz

  • Structural basis of tubulin tyrosination by tubulin tyrosine ligase

    Andrea E. Prota;Maria M. Magiera;Marijn Kuijpers;Katja Bargsten

  • Cortexillins, Major Determinants of Cell Shape and Size, Are Actin-Bundling Proteins with a Parallel Coiled-Coil Tail

    Jan Faix;Michel Steinmetz;Heike Boves;Richard A. Kammerer

  • Crystal structure of a naturally occurring parallel right-handed coiled coil tetramer.

    Jörg Stetefeld;Margrit Jenny;Therese Schulthess;Ruth Landwehr

  • An autonomous folding unit mediates the assembly of two-stranded coiled coils

    Richard A. Kammerer;Therese Schulthess;Ruth Landwehr;Ariel Lustig

  • Oligomerization and Multimerization Are Critical for Angiopoietin-1 to Bind and Phosphorylate Tie2 *

    Kyung Tae Kim;Han Ho Choi;Michel O. Steinmetz;Bohumil Maco

  • Exploring amyloid formation by a de novo design

    Richard A. Kammerer;Dirk Kostrewa;Jesús Zurdo;Andreas Detken

  • Designed angiopoietin-1 variant, COMP-Ang1, protects against radiation-induced endothelial cell apoptosis

    Chung Hyun Cho;Richard A. Kammerer;Hyuek Jong Lee;Kunio Yasunaga

  • Subdomain-Specific Localization of Climp-63 (P63) in the Endoplasmic Reticulum Is Mediated by Its Luminal α-Helical Segment

    Dieter R. Klopfenstein;Judith Klumperman;Ariel Lustig;Richard A. Kammerer

  • Microtubule minus-end regulation at spindle poles by an ASPM-katanin complex

    Kai Jiang;Lenka Rezabkova;Shasha Hua;Qingyang Liu

  • A distinct 14 residue site triggers coiled‐coil formation in cortexillin I

    Michel O. Steinmetz;Alexander Stock;Therese Schulthess;Ruth Landwehr

  • Tenascin-C Hexabrachion Assembly Is a Sequential Two-step Process Initiated by Coiled-coil α-Helices

    Richard A. Kammerer;Therese Schulthess;Ruth Landwehr;Ariel Lustig

  • Molecular basis of coiled-coil formation.

    Michel O. Steinmetz;Ilian Jelesarov;William M. Matousek;Srinivas Honnappa

  • Structural basis for recognition of synaptic vesicle protein 2C by botulinum neurotoxin A

    Roger M. Benoit;Daniel Frey;Manuel Hilbert;Josta T. Kevenaar

  • The coiled-coil trigger site of the rod domain of cortexillin I unveils a distinct network of interhelical and intrahelical salt bridges

    Peter Burkhard;Richard A Kammerer;Michel O Steinmetz;Gleb P Bourenkov

  • Op18/stathmin caps a kinked protofilament-like tubulin tetramer

    Michel O. Steinmetz;Richard A. Kammerer;Wolfgang Jahnke;Kenneth N. Goldie

  • A conserved trimerization motif controls the topology of short coiled coils

    Richard A. Kammerer;Dirk Kostrewa;Pavlos Progias;Srinivas Honnappa

  • Electron microscopic structure of agrin and mapping of its binding site in laminin-1

    Alain J. Denzer;Therese Schulthess;Charlotte Fauser;Beat Schumacher

Frequent Co-Authors

Michel O. Steinmetz
Michel O. Steinmetz Paul Scherrer Institute
Jürgen Engel
Jürgen Engel University of Basel
Ariel Lustig
Ariel Lustig University of Basel
Anna Akhmanova
Anna Akhmanova Utrecht University
Ueli Aebi
Ueli Aebi University of Basel
Markus A. Rüegg
Markus A. Rüegg University of Basel
Beat H. Meier
Beat H. Meier ETH Zurich
Pierre Gönczy
Pierre Gönczy École Polytechnique Fédérale de Lausanne
Gou Young Koh
Gou Young Koh Korea Advanced Institute of Science and Technology

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