PubRank

Jon Beckwith

Author PubWeight™ 87.80‹?›

Top papers

Rank Title Journal Year PubWeight™‹?›
1 Protein disulfide bond formation in prokaryotes. Annu Rev Biochem 2003 3.76
2 Diverse paths to midcell: assembly of the bacterial cell division machinery. Curr Biol 2005 3.69
3 Premature targeting of cell division proteins to midcell reveals hierarchies of protein interactions involved in divisome assembly. Mol Microbiol 2006 3.07
4 An open letter to Elias Zerhouni. Science 2005 2.19
5 The plug domain of the SecY protein stabilizes the closed state of the translocation channel and maintains a membrane seal. Mol Cell 2007 2.18
6 Snapshots of DsbA in action: detection of proteins in the process of oxidative folding. Science 2004 2.18
7 Bacterial species exhibit diversity in their mechanisms and capacity for protein disulfide bond formation. Proc Natl Acad Sci U S A 2008 2.12
8 NMR solution structure of the integral membrane enzyme DsbB: functional insights into DsbB-catalyzed disulfide bond formation. Mol Cell 2008 1.92
9 The DsbA signal sequence directs efficient, cotranslational export of passenger proteins to the Escherichia coli periplasm via the signal recognition particle pathway. J Bacteriol 2003 1.80
10 The XYY syndrome: a dangerous myth. New Sci 1974 1.80
11 A complex of the Escherichia coli cell division proteins FtsL, FtsB and FtsQ forms independently of its localization to the septal region. Mol Microbiol 2004 1.78
12 Assembly of cell division proteins at the E. coli cell center. Curr Opin Microbiol 2002 1.73
13 IcsA, a polarly localized autotransporter with an atypical signal peptide, uses the Sec apparatus for secretion, although the Sec apparatus is circumferentially distributed. Mol Microbiol 2003 1.68
14 A novel regulatory mechanism couples deoxyribonucleotide synthesis and DNA replication in Escherichia coli. EMBO J 2006 1.65
15 In vivo oxidative protein folding can be facilitated by oxidation-reduction cycling. Mol Microbiol 2009 1.62
16 Premature targeting of a cell division protein to midcell allows dissection of divisome assembly in Escherichia coli. Genes Dev 2005 1.58
17 Four cysteines of the membrane protein DsbB act in concert to oxidize its substrate DsbA. EMBO J 2002 1.55
18 Use of thioredoxin as a reporter to identify a subset of Escherichia coli signal sequences that promote signal recognition particle-dependent translocation. J Bacteriol 2005 1.45
19 Structure of a bacterial homologue of vitamin K epoxide reductase. Nature 2010 1.44
20 Mechanisms of oxidative protein folding in the bacterial cell envelope. Antioxid Redox Signal 2010 1.42
21 The nonconsecutive disulfide bond of Escherichia coli phytase (AppA) renders it dependent on the protein-disulfide isomerase, DsbC. J Biol Chem 2005 1.41
22 Production of functional single-chain Fv antibodies in the cytoplasm of Escherichia coli. J Mol Biol 2002 1.39
23 The disulfide bond isomerase DsbC is activated by an immunoglobulin-fold thiol oxidoreductase: crystal structure of the DsbC-DsbDalpha complex. EMBO J 2002 1.37
24 Detecting folding intermediates of a protein as it passes through the bacterial translocation channel. Cell 2009 1.36
25 Interactions of glutaredoxins, ribonucleotide reductase, and components of the DNA replication system of Escherichia coli. Proc Natl Acad Sci U S A 2004 1.33
26 Rapid beta-lactam-induced lysis requires successful assembly of the cell division machinery. Proc Natl Acad Sci U S A 2009 1.29
27 Analysis of ftsQ mutant alleles in Escherichia coli: complementation, septal localization, and recruitment of downstream cell division proteins. J Bacteriol 2002 1.28
28 In vivo requirement for glutaredoxins and thioredoxins in the reduction of the ribonucleotide reductases of Escherichia coli. Antioxid Redox Signal 2006 1.24
29 Functional plasticity of a peroxidase allows evolution of diverse disulfide-reducing pathways. Proc Natl Acad Sci U S A 2008 1.22
30 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 Bacteriol 2006 1.18
31 Genetic screen yields mutations in genes encoding all known components of the Escherichia coli signal recognition particle pathway. J Bacteriol 2002 1.16
32 Evolutionary domain fusion expanded the substrate specificity of the transmembrane electron transporter DsbD. EMBO J 2002 1.13
33 Divisome under construction: distinct domains of the small membrane protein FtsB are necessary for interaction with multiple cell division proteins. J Bacteriol 2009 1.11
34 Diversity of chemical mechanisms in thioredoxin catalysis revealed by single-molecule force spectroscopy. Nat Struct Mol Biol 2009 1.11
35 Inhibition of bacterial disulfide bond formation by the anticoagulant warfarin. Proc Natl Acad Sci U S A 2009 1.08
36 Mutant AhpC peroxiredoxins suppress thiol-disulfide redox deficiencies and acquire deglutathionylating activity. Mol Cell 2008 1.07
37 Role and location of the unusual redox-active cysteines in the hydrophobic domain of the transmembrane electron transporter DsbD. Proc Natl Acad Sci U S A 2003 1.05
38 A new family of membrane electron transporters and its substrates, including a new cell envelope peroxiredoxin, reveal a broadened reductive capacity of the oxidative bacterial cell envelope. MBio 2012 1.05
39 Redox-active cysteines of a membrane electron transporter DsbD show dual compartment accessibility. EMBO J 2007 1.02
40 The prokaryotic enzyme DsbB may share key structural features with eukaryotic disulfide bond forming oxidoreductases. Protein Sci 2005 1.02
41 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. Antioxid Redox Signal 2011 1.00
42 Role for the nonessential N terminus of FtsN in divisome assembly. J Bacteriol 2006 1.00
43 Multiple interaction domains in FtsL, a protein component of the widely conserved bacterial FtsLBQ cell division complex. J Bacteriol 2010 0.99
44 Functions of thiol-disulfide oxidoreductases in E. coli: redox myths, realities, and practicalities. Antioxid Redox Signal 2003 0.97
45 The unusual transmembrane electron transporter DsbD and its homologues: a bacterial family of disulfide reductases. Res Microbiol 2004 0.97
46 A selection for mutants that interfere with folding of Escherichia coli thioredoxin-1 in vivo. Proc Natl Acad Sci U S A 2005 0.95
47 Distinguishing genetic from nongenetic medical tests: some implications for antidiscrimination legislation. Sci Eng Ethics 1998 0.94
48 Artificial septal targeting of Bacillus subtilis cell division proteins in Escherichia coli: an interspecies approach to the study of protein-protein interactions in multiprotein complexes. J Bacteriol 2008 0.94
49 Ribonucleotide reductases: influence of environment on synthesis and activity. Antioxid Redox Signal 2006 0.94
50 Conserved role of the linker alpha-helix of the bacterial disulfide isomerase DsbC in the avoidance of misoxidation by DsbB. J Biol Chem 2005 0.94
51 Redox state of cytoplasmic thioredoxin. Methods Enzymol 2002 0.93
52 Mutations of the membrane-bound disulfide reductase DsbD that block electron transfer steps from cytoplasm to periplasm in Escherichia coli. J Bacteriol 2006 0.91
53 Laboratory evolution of glutathione biosynthesis reveals natural compensatory pathways. Nat Chem Biol 2010 0.91
54 Mutational alterations of the key cis proline residue that cause accumulation of enzymatic reaction intermediates of DsbA, a member of the thioredoxin superfamily. J Bacteriol 2005 0.90
55 Contribution of the FtsQ transmembrane segment to localization to the cell division site. J Bacteriol 2007 0.90
56 Illusions of scientific legitimacy: misrepresented science in the direct-to-consumer genetic-testing marketplace. Trends Genet 2010 0.90
57 Two snapshots of electron transport across the membrane: insights into the structure and function of DsbD. J Biol Chem 2009 0.89
58 Reply to Hook and Lowden: the definition and implications of genetic discrimination. Am J Hum Genet 1992 0.89
59 Crystal structure of an unusual thioredoxin protein with a zinc finger domain. J Biol Chem 2007 0.85
60 Role of leucine zipper motifs in association of the Escherichia coli cell division proteins FtsL and FtsB. J Bacteriol 2011 0.84
61 Disulfide bond formation in periplasm of Escherichia coli. Methods Enzymol 2002 0.83
62 The reducing activity of glutaredoxin 3 toward cytoplasmic substrate proteins is restricted by methionine 43. Biochemistry 2007 0.82
63 Evidence from artificial septal targeting and site-directed mutagenesis that residues in the extracytoplasmic β domain of DivIB mediate its interaction with the divisomal transpeptidase PBP 2B. J Bacteriol 2010 0.81
64 Mutations at several loci cause increased expression of ribonucleotide reductase in Escherichia coli. J Bacteriol 2012 0.79
65 Determinants of activity in glutaredoxins: an in vitro evolved Grx1-like variant of Escherichia coli Grx3. Biochem J 2010 0.77
66 Misreading Dr. Venter's genome. Science 2007 0.75
67 Amino acid residues important for folding of thioredoxin are revealed only by study of the physiologically relevant reduced form of the protein. Biochemistry 2010 0.75
68 The XYY male: the making of a myth. Harv Mag 1976 0.75
69 Recombinant DNA: does the fault lie within our genes? Sci People 1979 0.75
70 The politics of genetic engineering: who decides who's defective? Psychol Today 1974 0.75