R. Bass

发表

The two-component signaling pathway of bacterial chemotaxis: a molecular view of signal transduction by receptors, kinases, and adaptation enzymes.

S. Chervitz, J. Falke, R. Bass, 1997, Annual review of cell and developmental biology.

Crystal Structure of Escherichia coli MscS, a Voltage-Modulated and Mechanosensitive Channel

Pavel Strop, D. Rees, P. Strop, 2002, Science.

Structures of the Prokaryotic Mechanosensitive Channels MscL and MscS

Douglas C. Rees, Pavel Strop, S. Steinbacher, 2007 .

Signaling domain of the aspartate receptor is a helical hairpin with a localized kinase docking surface: cysteine and disulfide scanning studies.

J. Falke, R. Bass, M. D. Coleman, 1999, Biochemistry.

N-terminal Glutamate to Pyroglutamate Conversion in Vivo for Human IgG2 Antibodies

R. Bass, G. C. Flynn, A. Goetze, 2011, The Journal of Biological Chemistry.

Ion Channel Structural Studies

R. Bass, R. Spencer, Randal B. Bass, 2008 .

Use of site-directed cysteine and disulfide chemistry to probe protein structure and dynamics: applications to soluble and transmembrane receptors of bacterial chemotaxis.

S. Chervitz, S. Gloor, J. Falke, 2007, Methods in enzymology.

Conversion of a mechanosensitive channel protein from a membrane-embedded to a water-soluble form by covalent modification with amphiphiles.

G. Kochendoerfer, D. Rees, M. Yeager, 2004, Journal of molecular biology.

Open-state disulfide crosslinking between Mycobacterium tuberculosis mechanosensitive channel subunits.

H. Lester, D. Rees, R. Bass, 2003, Biophysical journal.

Prokaryotic mechanosensitive channels.

D. Rees, P. Strop, R. Bass, 2003, Advances in protein chemistry.

Cysteine and Disulfide Scanning Reveals a Regulatory α-Helix in the Cytoplasmic Domain of the Aspartate Receptor*

J. Falke, R. Bass, M. A. Danielson, 1997, The Journal of Biological Chemistry.

The structures of BtuCD and MscS and their implications for transporter and channel function

Pavel Strop, D. Rees, K. Locher, 2003, FEBS letters.

The aspartate receptor cytoplasmic domain: in situ chemical analysis of structure, mechanism and dynamics.

J. Falke, R. Bass, Randal B. Bass, 1999, Structure.

Breaching the Barrier

D. Rees, K. Locher, R. Bass, 2003, Science.

Detection of a Conserved α-Helix in the Kinase-docking Region of the Aspartate Receptor by Cysteine and Disulfide Scanning*

J. Falke, R. Bass, Randal B. Bass, 1998, The Journal of Biological Chemistry.

Conserved glycine residues in the cytoplasmic domain of the aspartate receptor play essential roles in kinase coupling and on-off switching.

J. Falke, R. Bass, Joseph J Falke, 2005, Biochemistry.

The PICM chemical scanning method for identifying domain-domain and protein-protein interfaces: applications to the core signaling complex of E. coli chemotaxis.

S. Gloor, J. Falke, R. Bass, 2007, Methods in enzymology.