R. Brooker

发表

Control of H+/Lactose Coupling by Ionic Interactions in the Lactose Permease ofEscherichia coli

J. Johnson, R. Brooker, 2004, The Journal of Membrane Biology.

A Suppressor Analysis of Residues Involved in Cation Transport in the Lactose Permease: Identification of a Coupling Sensor

Brian M. Wiczer, R. Brooker, P. J. Franco, 2006, The Journal of Membrane Biology.

Characterization of the double mutant, Val-177/Asn-322, of the lactose permease.

R. Brooker, 1990, The Journal of biological chemistry.

Effects of Mg2+ ions on the plasma membrane [H+]-ATPase of Neurospora crassa. II. Kinetic studies.

C. Slayman, R. Brooker, 1983, The Journal of biological chemistry.

Concepts of Genetics

R. Brooker, 2011 .

A Triple Mutant, K319N/H322Q/E325Q, of the Lactose Permease Cotransports H+ with Thiodigalactoside

J. Johnson, R. Brooker, M. Lockheart, 2001, The Journal of Membrane Biology.

A Revised Model for the Structure and Function of the Lactose Permease

E. Anderson, E. Anderson, R. Brooker, 2000, The Journal of Biological Chemistry.

A Reaction-induced Fourier Transform-Infrared Spectroscopic Study of the Lactose Permease

B. Barry, J. S. Patzlaff, R. Brooker, 2000, The Journal of Biological Chemistry.

The Conserved Motif in Hydrophilic Loop 2/3 and Loop 8/9 of the Lactose Permease of Escherichia coli. Analysis of Suppressor Mutations

R. Brooker, E. Matzke, S. Cain, 2000, The Journal of Membrane Biology.

Analysis of the structural specificity of the lactose permease toward sugars.

R. Brooker, S. Olsen, 1989, The Journal of biological chemistry.

Evidence that highly conserved residues of transmembrane segment 6 of Escherichia coli MntH are important for transport activity.

Heather A H Haemig, R. Brooker, Patrick J Moen, 2010, Biochemistry.

A facile transport assay for H+ coupled membrane transport using fluorescence probes

Yufang Xu, Jingyan Zhang, Chusen Huang, 2012 .

A K319N/E325Q Double Mutant of the Lactose Permease Cotransports H+ with Lactose

R. Brooker, Jerry L. Johnson, 1999, The Journal of Biological Chemistry.

Structural Topology of Transmembrane Helix 10 in the Lactose Permease of Escherichia coli*

R. Brooker, E. Matzke, V. C. Goswitz, 1996, The Journal of Biological Chemistry.

Role of cysteine residues in the lac permease of Escherichia coli.

H. Kaback, D. Menick, R. Brooker, 1987, Biochemistry.

Fourier transform infrared analysis of purified lactose permease: a monodisperse lactose permease preparation is stably folded, alpha-helical, and highly accessible to deuterium exchange.

J. Moeller, B. Barry, J. S. Patzlaff, 1998, Biochemistry.

Electrogenic H+ translocation by the plasma membrane ATPase of Neurospora. Studies on plasma membrane vesicles and reconstituted enzyme.

C. Slayman, D. Perlin, R. Brooker, 1984, The Journal of biological chemistry.

Suppressor analysis of mutations in the loop 2-3 motif of lactose permease: evidence that glycine-64 is an important residue for conformational changes

R. Brooker, N. Parker, A. Jessen-Marshall, 1997, Journal of bacteriology.

Site-specific alteration of cysteine 176 and cysteine 234 in the lactose carrier of Escherichia coli.

R. Brooker, T. Wilson, 1986, The Journal of biological chemistry.

The Conserved Motif, GXXX(D/E)(R/K)XG[X](R/K)(R/K), in Hydrophilic Loop 2/3 of the Lactose Permease (*)

R. Brooker, A. Jessen-Marshall, Nanette J. Paul, 1995, The Journal of Biological Chemistry.

Lactose permease mutants which transport (malto)-oligosaccharides

R. Brooker, S. Olsen, K. M. Greene, 1993, Journal of bacteriology.

Inhibition of the plasma membrane [H+]-ATPase of Neurospora crassa by N-ethylmaleimide. Protection by nucleotides.

C. Slayman, R. Brooker, 1982, The Journal of biological chemistry.

[14C]N-ethylmaleimide labeling of the plasma membrane [H+]-ATPase of Neurospora crassa.

C. Slayman, R. Brooker, 1983, The Journal of biological chemistry.

Characterization of lactose carrier mutants which transport maltose.

K. Fiebig, R. Brooker, T. Wilson, 1985, The Journal of biological chemistry.

Effects of Mg2+ ions on the plasma membrane [H+]-ATPase of Neurospora crassa. I. Inhibition by N-ethylmaleimide and trypsin.

C. Slayman, R. Brooker, 1983, The Journal of biological chemistry.

Roles of Charged Residues in the Conserved Motif, G-X-X-X-D/E-R/K-X-G-[X]-R/K-R/K, of the Lactose Permease of Escherichia coli

N. Pazdernik, N. J. Pazdernik, E. A. Matzke, 2000, The Journal of Membrane Biology.

Role of conserved residues in hydrophilic loop 8-9 of the lactose permease

N. Pazdernik, R J Brooker, N J Pazdernik, 1997, Journal of bacteriology.

Isolation of lactose permease mutants which recognize arabinose.

R. Brooker, V. C. Goswitz, 1993, Membrane biochemistry.

Lactose carrier mutants of Escherichia coli with changes in sugar recognition (lactose versus melibiose)

R. Brooker, M. Varela, T. Wilson, 1997, Journal of bacteriology.

Genetics: Analysis and Principles

Robert J. Brooker, R. Brooker, 1998 .

The lactose permease of Escherichia coli.

R J Brooker, R. Brooker, 1990, Research in microbiology.

Importance of Conserved Acidic Residues in MntH, the Nramp homolog of Escherichia coli

Heather A H Haemig, R. Brooker, 2004, The Journal of Membrane Biology.

Functional roles of Glu-269 and Glu-325 within the lactose permease of Escherichia coli.

R. Brooker, P. J. Franco, 1994, The Journal of biological chemistry.

Functional role of arginine 302 within the lactose permease of Escherichia coli.

E A Matzke, L J Stephenson, R J Brooker, 1992, The Journal of biological chemistry.

Evidence That Transmembrane Segment 2 of the Lactose Permease Is Part of a Conformationally Sensitive Interface between the Two Halves of the Protein (*)

R. Brooker, A. Jessen-Marshall, 1996, The Journal of Biological Chemistry.

Structural features of the uniporter/symporter/antiporter superfamily

R. Brooker, V. C. Goswitz, 1995, Protein science : a publication of the Protein Society.

An analysis of the side chain requirement at position 177 within the lactose permease which confers the ability to recognize maltose.

R. Brooker, C. Gram, 1992, The Journal of biological chemistry.