D. Westphal

发表

Prototype Foamy Virus Envelope Glycoprotein Leader Peptide Processing Is Mediated by a Furin-Like Cellular Protease, but Cleavage Is Not Essential for Viral Infectivity

S. Eastman, T. Pietschmann, D. Lindemann, 2004, Journal of Virology.

BAX Activation: Mutations Near Its Proposed Non-canonical BH3 Binding Site Reveal Allosteric Changes Controlling Mitochondrial Association.

J. Sandow, Jerry M. Adams, G. Dewson, 2019, Cell reports.

Bax Crystal Structures Reveal How BH3 Domains Activate Bax and Nucleate Its Oligomerization to Induce Apoptosis

Erinna F. Lee, W. D. Fairlie, Peter M. Colman, 2013, Cell.

Biophysical Characterization of Pro-apoptotic BimBH3 Peptides Reveals an Unexpected Capacity for Self-Association.

E. Bordignon, I. Usón, P. Czabotar, 2020, Structure.

Bak core and latch domains separate during activation, and freed core domains form symmetric homodimers.

P. Colman, Rachel T. Uren, G. Dewson, 2014, Molecular cell.

A Novel Bcl-2-Like Inhibitor of Apoptosis Is Encoded by the Parapoxvirus Orf Virus

A. Mercer, D. Westphal, E. Ledgerwood, 2007, Journal of Virology.

Restriction of Foamy Viruses by Primate Trim5α

H. Hanenberg, D. Lindemann, Nicole Stanke, 2008, Journal of Virology.

Molecular biology of Bax and Bak activation and action.

G. Dewson, R. Kluck, P. Czabotar, 2011, Biochimica et biophysica acta.

Murine Norovirus Replication Induces G0/G1 Cell Cycle Arrest in Asynchronously Growing Cells

Chris M. Brown, Colin T. R. Davies, V. Ward, 2015, Journal of Virology.

Building blocks of the apoptotic pore: how Bax and Bak are activated and oligomerize during apoptosis

G. Dewson, R. Kluck, D. Westphal, 2013, Cell Death and Differentiation.

NMR studies of interactions between Bax and BH3 domain-containing peptides in the absence and presence of CHAPS.

P. Colman, S. Yao, Jerry M. Adams, 2014, Archives of biochemistry and biophysics.

The orf virus inhibitor of apoptosis functions in a Bcl-2-like manner, binding and neutralizing a set of BH3-only proteins and active Bax

A. Mercer, J. Tyndall, D. Westphal, 2009, Apoptosis.

Bak apoptotic pores involve a flexible C-terminal region and juxtaposition of the C-terminal transmembrane domains

J. Gulbis, G. Dewson, R. Kluck, 2015, Cell Death and Differentiation.

Bak apoptotic function is not directly regulated by phosphorylation

G. Dewson, R. Kluck, D. Westphal, 2013, Cell Death and Disease.

Apoptotic pore formation is associated with in-plane insertion of Bak or Bax central helices into the mitochondrial outer membrane

Brian J. Smith, M. Ménard, Jerry M. Adams, 2014, Proceedings of the National Academy of Sciences.

Crystal structure of Bax bound to the BH3 peptide of Bim identifies important contacts for interaction

P. Colman, G. Dewson, P. Czabotar, 2015, Cell Death and Disease.

Molecular biology of Bax and Bak activation and action.

G. Dewson, R. Kluck, P. Czabotar, 2011, Biochimica et biophysica acta.

Restriction of Foamy Viruses by Primate Trim5α

H. Hanenberg, D. Lindemann, Nicole Stanke, 2008, Journal of Virology.

Bak core and latch domains separate during activation, and freed core domains form symmetric homodimers.

P. Colman, Rachel T. Uren, G. Dewson, 2014, Molecular cell.

Apoptotic pore formation is associated with in-plane insertion of Bak or Bax central helices into the mitochondrial outer membrane

Brian J. Smith, Jerry M. Adams, G. Dewson, 2014, Proceedings of the National Academy of Sciences of the United States of America.