D. Boyd

发表

J. Beckwith, D. Boyd, C. Schierle, 1998, Protein science : a publication of the Protein Society.

Comparative genomic analysis of Vibrio cholerae: Genes that correlate with cholera endemic and pandemic disease

John F. Heidelberg, J. Heidelberg, J. Mekalanos, 2002, Proceedings of the National Academy of Sciences of the United States of America.

Localization of FtsI (PBP3) to the Septal Ring Requires Its Membrane Anchor, the Z Ring, FtsA, FtsQ, and FtsL

J. Beckwith, D. Boyd, D. S. Weiss, 1999, Journal of bacteriology.

The Nonconsecutive Disulfide Bond of Escherichia coli Phytase (AppA) Renders It Dependent on the Protein-disulfide Isomerase, DsbC*

J. Beckwith, D. Boyd, M. Berkmen, 2005, Journal of Biological Chemistry.

Bacterial species exhibit diversity in their mechanisms and capacity for protein disulfide bond formation

J. Beckwith, D. Boyd, M. Berkmen, 2008, Proceedings of the National Academy of Sciences.

A signaling network reciprocally regulates genes associated with acute infection and chronic persistence in Pseudomonas aeruginosa.

S. Lory, D. Boyd, Roger S Smith, 2004, Developmental cell.

Genes required for mycobacterial growth defined by high density mutagenesis

E. Rubin, D. Boyd, C. Sassetti, 2003, Molecular microbiology.

Conservation of genome content and virulence determinants among clinical and environmental isolates of Pseudomonas aeruginosa

Qing Yang, Stephen Lory, Kai Wu, 2003, Proceedings of the National Academy of Sciences of the United States of America.

Mutant AhpC peroxiredoxins suppress thiol-disulfide redox deficiencies and acquire deglutathionylating activity.

J. Beckwith, D. Boyd, D. Ritz, 2008, Molecular cell.

Use of Thioredoxin as a Reporter To Identify a Subset of Escherichia coli Signal Sequences That Promote Signal Recognition Particle-Dependent Translocation

M. Gerstein, Yu Xia, Michael H. Olma, 2005, Journal of bacteriology.

From Biology to Biotechnology: Disulfide Bond Formation in Escherichia coli

D. Boyd, M. Berkmen, Guoping Ren, 2017 .

The Protein Translocation Apparatus Contributes to Determining the Topology of an Integral Membrane Protein in Escherichia coli *

J. Beckwith, W. Prinz, M. Ehrmann, 1998, The Journal of Biological Chemistry.

Disulfide Bond Formation in the Periplasm of Escherichia coli.

D. Boyd, M. Berkmen, Bruno Manta, 2019, EcoSal Plus.

Chapter 18 From Biology to Biotechnology : Disulfide Bond Formation in Escherichia coli

D. Boyd, M. Berkmen, Guoping Ren, 2018 .

Repurposing lipoic acid changes electron flow in two important metabolic pathways of Escherichia coli

J. Beckwith, G. Georgiou, D. Boyd, 2011, Proceedings of the National Academy of Sciences.

Mutants, Suppressors, and Wrinkled Colonies: Mutant Alleles of the Cell Division Gene ftsQ Point to Functional Domains in FtsQ and a Role for Domain 1C of FtsA in Divisome Assembly

J. Beckwith, I. Petrovska, D. Boyd, 2006, Journal of bacteriology.

Molecular genetic analysis of membrane protein topology.

J. Beckwith, D. Boyd, C. Manoil, 1988, Trends in genetics : TIG.

Minimization of the Legionella pneumophila genome reveals chromosomal regions involved in host range expansion

D. Boyd, R. Isberg, Tamara J. O’Connor, 2011, Proceedings of the National Academy of Sciences.

Laboratory evolution of glutathione biosynthesis reveals natural compensatory pathways.

J. Beckwith, G. Georgiou, D. Boyd, 2011, Nature chemical biology.

The Bacterial ATPase SecA Functions as a Monomer in Protein Translocation*

T. Rapoport, J. Beckwith, D. Boyd, 2005, Journal of Biological Chemistry.

Human ferritin H and L sequences lie on ten different chromosomes

T. Shows, D. Boyd, A. Sakaguchi, 1987, Human Genetics.

Chemical Biology Approaches Reveal Conserved Features of a C‐Terminal Processing PDZ Protease

R. Huber, P. Hauske, M. Meltzer, 2012, Chembiochem : a European journal of chemical biology.

Inhibition of Pseudomonas aeruginosa and Mycobacterium tuberculosis disulfide bond forming enzymes

S. Lory, J. Beckwith, E. Rubin, 2019, Molecular microbiology.

Title : Inhibition of Pseudomonas aeruginosa and Mycobacterium tuberculosis disulfide bond forming enzymes Running Title : Targeting virulence and growth of pathogenic bacteria

Tanweer, S. Lory, J. Beckwith, 2018 .

Folding LacZ in the Periplasm of Escherichia coli

J. Beckwith, T. Silhavy, D. Boyd, 2014, Journal of bacteriology.

Membrane topology analysis of the Escherichia coli cytosine permease.

D. Boyd, S. Danielsen, J. Neuhard, 1995, Microbiology.

The dynamics of assembly of a cytoplasmic membrane protein in Escherichia coli.

J. Beckwith, D. Boyd, C. Lee, 1992, The Journal of biological chemistry.

Positively charged amino acid residues can act as topogenic determinants in membrane proteins.

J. Beckwith, D. Boyd, 1989, Proceedings of the National Academy of Sciences of the United States of America.

Inhibition of virulence-promoting disulfide bond formation enzyme DsbB is blocked by mutating residues in two distinct regions

J. Beckwith, Feras Hatahet, D. Boyd, 2017, The Journal of Biological Chemistry.

Use of phoA fusions to study the topology of the Escherichia coli inner membrane protein leader peptidase

J. Beckwith, D. Boyd, J. L. San Millán, 1989, Journal of bacteriology.

The Disulﬁde Bond Formation Pathway Is Essential for Anaerobic Growth of Escherichia coli

J. Beckwith, D. Boyd, B. Meehan, 2017 .

Structural and functional relationships of human ferritin H and L chains deduced from cDNA clones.

S. Jain, D. Boyd, C. Vecoli, 1985, The Journal of biological chemistry.

Membrane topology and mutational analysis of Mycobacterium tuberculosis VKOR, a protein involved in disulfide bond formation and a homologue of human vitamin K epoxide reductase.

J. Beckwith, D. Boyd, R. Dutton, 2011, Antioxidants & redox signaling.

The Reconstitution of Escherichia coli DNA-Dependent RNA Polymerase from Its Isolated Subunits

D. Boyd, W. Zillig, P. Palm, 1975 .

The plug domain of the SecY protein stabilizes the closed state of the translocation channel and maintains a membrane seal.

Sol Schulman, Weikai Li, Jon Beckwith, 2007, Molecular cell.

Identification of YidC Residues That Define Interactions with the Sec Apparatus

D. Boyd, M. Goldberg, M. Reindl, 2013, Journal of bacteriology.

Disulfide bond formation in prokaryotes

J. Beckwith, D. Boyd, Cristina Landeta, 2018, Nature Microbiology.

Release of Escherichia coli DNA from membrane complexes by single-strand endonucleases.

D. Boyd, M. Schaechter, W. Hendrickson, 1977, Proceedings of the National Academy of Sciences of the United States of America.

Genetic selection for and molecular dynamic modeling of a protein transmembrane domain multimerization motif from a random Escherichia coli genomic library.

D. Engelman, J. Beckwith, D. Boyd, 2001, Journal of molecular biology.

TnTIN and TnTAP: mini-transposons for site-specific proteolysis in vivo.

M. Ehrmann, D. Boyd, R. Lange, 1997, Proceedings of the National Academy of Sciences of the United States of America.

The role of charged amino acids in the localization of secreted and membrane proteins

Jon Beckwith, J. Beckwith, D. Boyd, 1990, Cell.

Isolation and characterization of a cDNA clone for human ferritin heavy chain.

S. Jain, J. Crampton, D. Boyd, 1984, Proceedings of the National Academy of Sciences of the United States of America.

Ferritin H and L chains are derived from different multigene families.

S. Jain, J. Crampton, D. Boyd, 1985, The Journal of biological chemistry.

Identification of the Thioredoxin Partner of Vitamin K Epoxide Reductase in Mycobacterial Disulfide Bond Formation

J. Beckwith, D. Boyd, Xiao-yun Wang, 2018, Journal of bacteriology.

The DsbA Signal Sequence Directs Efficient, Cotranslational Export of Passenger Proteins to the Escherichia coli Periplasm via the Signal Recognition Particle Pathway

J. Beckwith, D. Boyd, C. Schierle, 2003, Journal of bacteriology.

A mutant hunt for defects in membrane protein assembly yields mutations affecting the bacterial signal recognition particle and Sec machinery.

J. Beckwith, D. Boyd, H. Tian, 2000, Proceedings of the National Academy of Sciences of the United States of America.

Target-directed proteolysis in vivo.

M. Ehrmann, D. Boyd, Markus Eser, 2007, Methods in Enzymology.

Target-directed proteolysis at the ribosome.

N. Ban, M. Ehrmann, D. Boyd, 2005, Proceedings of the National Academy of Sciences of the United States of America.

Screening of Escherichia coli Temperature-sensitive Mutants by Pretreatment with Glucose Starvation

D. Boyd, D. Gillespie, S. Gillespie, 1968, Journal of bacteriology.

Disulfide Rearrangement Triggered by Translocon Assembly Controls Lipopolysaccharide Export

J. Beckwith, D. Boyd, D. Kahne, 2012, Science.

Twin RNA Polymerase–Associated Proteins Control Virulence Gene Expression in Francisella tularensis

E. Rubin, D. Boyd, E. Balon, 2007, PLoS pathogens.

The E Block motif is associated with Legionella pneumophila translocated substrates

Zhao-Qing Luo, D. Boyd, R. Isberg, 2010, Cellular microbiology.

Multiple Interaction Domains in FtsL, a Protein Component of the Widely Conserved Bacterial FtsLBQ Cell Division Complex

J. Beckwith, D. Boyd, Mark D. Gonzalez, 2010, Journal of bacteriology.

The essential cell division protein FtsN contains a critical disulfide bond in a non‐essential domain

J. Beckwith, D. Boyd, Cristina Landeta, 2017, Molecular microbiology.

Insight into Disulfide Bond Catalysis in Chlamydia from the Structure and Function of DsbH, a Novel Oxidoreductase*

D. Boyd, T. Ulmer, J. Bardwell, 2008, Journal of Biological Chemistry.

Aggravating Genetic Interactions Allow a Solution to Redundancy in a Bacterial Pathogen

D. Boyd, R. Isberg, Marion S. Dorer, 2012, Science.

Aeropyrum pernix membrane topology of protein VKOR promotes protein disulfide bond formation in two subcellular compartments.

J. Beckwith, D. Boyd, M. Berkmen, 2017, Microbiology.

Structure of a bacterial homolog of vitamin K epoxide reductase

T. Rapoport, J. Beckwith, D. Boyd, 2010, Nature.

Disulfide bond formation in prokaryotes: history, diversity and design.

J. Beckwith, Feras Hatahet, D. Boyd, 2014, Biochimica et biophysica acta.

Towards Single-Copy Gene Expression Systems Making Gene Cloning Physiologically Relevant: Lambda InCh, a Simple Escherichia coli Plasmid-Chromosome Shuttle System

J. Beckwith, D. Boyd, Joseph C. Chen, 2000, Journal of bacteriology.

Isolation of a replication origin complex from Escherichia coli.

D. Boyd, M. Schaechter, K. Nagai, 1980, Proceedings of the National Academy of Sciences of the United States of America.

In vivo oxidative protein folding can be facilitated by oxidation–reduction cycling

J. Beckwith, D. Boyd, M. Berkmen, 2010, Molecular microbiology.

Use of Thioredoxin as a Reporter To Identify a Subset of Escherichia coli Signal Sequences That Promote Signal Recognition Particle-Dependent Translocation

M. Gerstein, Yu Xia, Michael H. Olma, 2005, Journal of Bacteriology.

Genetic analysis of the membrane insertion and topology of MalF, a cytoplasmic membrane protein of Escherichia coli.

J. Beckwith, D. Boyd, J Beckwith, 1988, Journal of molecular biology.

The ArcB Sensor Kinase of Escherichia coli: Genetic Exploration of the Transmembrane Region

A. S. Lynch, E. Lin, D. Georgellis, 2000, Journal of bacteriology.

A mutational study of the ArcA-P binding sequences in the aldA promoter of Escherichia coli

J. Aguilar, A. S. Lynch, E. Lin, 1999, Molecular and General Genetics MGG.

Unbalanced Charge Distribution as a Determinant for Dependence of a Subset of Escherichia coli Membrane Proteins on the Membrane Insertase YidC

H. Niki, D. Boyd, M. Goldberg, 2011, mBio.

Determinants of membrane protein topology.

J. Beckwith, D. Boyd, C. Manoil, 1987, Proceedings of the National Academy of Sciences of the United States of America.

Altered Escherichia coli membrane protein assembly machinery allows proper membrane assembly of eukaryotic protein vitamin K epoxide reductase

Yongxin Zhao, R. Campbell, J. Beckwith, 2015, Proceedings of the National Academy of Sciences.

Inhibition of bacterial disulfide bond formation by the anticoagulant warfarin

J. Beckwith, E. Rubin, D. Boyd, 2009, Proceedings of the National Academy of Sciences.

Aberrant Cell Division and Random FtsZ Ring Positioning in Escherichia coli cpxA* Mutants

R. Losick, K. Pogliano, J. Pogliano, 1998, Journal of bacteriology.

Genetic analysis of membrane protein topology by a sandwich gene fusion approach.

J. Beckwith, M. Ehrmann, D. Boyd, 1990, Proceedings of the National Academy of Sciences of the United States of America.

Use of Gene Fusions to Determine Membrane Protein Topology

D. Boyd, Dana Boyd, 1994 .

Disulfide bond formation in prokaryotes

J. Beckwith, D. Boyd, Cristina Landeta, 2018, Nature Microbiology.

Compounds targeting disulfide bond forming enzyme DsbB of Gram-negative bacteria

J. Beckwith, Alissa Myrick, E. Rubin, 2015, Nature chemical biology.

Erratum: Minimization of the Legionella pneumophila genome reveals chromosomal regions involved in host range expansion (Proceedings of the National Academy of Sciences of the United States of America (2011) 108, 36 (14733-14740) DOI: 10.1073/pnas.1111678108)

D. Boyd, R. Isberg, Y. Adepoju, 2011 .

Converting a Sulfenic Acid Reductase into a Disulfide Bond Isomerase

D. Boyd, J. Bardwell, M. Berkmen, 2015, Antioxidants & redox signaling.

Analysis of the topology of a membrane protein by using a minimum number of alkaline phosphatase fusions

J. Beckwith, D. Boyd, J Beckwith, 1993, Journal of bacteriology.

YgbQ, a cell division protein in Escherichia coli and Vibrio cholerae, localizes in codependent fashion with FtsL to the division site

J. Beckwith, J. Mekalanos, D. Boyd, 2002, Proceedings of the National Academy of Sciences of the United States of America.

The topological analysis of integral cytoplasmic membrane proteins

Jon Beckwith, J. Beckwith, D. Boyd, 1993, The Journal of Membrane Biology.

Disulfide Bond Formation in the Periplasm of Escherichia coli

D. Boyd, M. Berkmen, Bruno Manta, 2019, EcoSal Plus.