T. Baldwin

发表

Process of biosynthetic protein folding determines the rapid formation of native structure.

A. Fedorov, T. Baldwin, Alexey N. Fedorov, 1999, Journal of molecular biology.

Cotranslational Protein Folding*

A. Fedorov, T. Baldwin, 1997, The Journal of Biological Chemistry.

Protein folding and assembly in a cell-free expression system.

A. Fedorov, T. Baldwin, 1998, Methods in enzymology.

Bioluminescence and chemiluminescence

W. D. Mcelroy, W. McELROY, T. Baldwin, 1978 .

Transcriptional regulation of bioluminesence genes from Vibrio fischeri

T. Baldwin, T O Baldwin, D. Sitnikov, 1995, Molecular microbiology.

Use of bacterial and firefly luciferases as reporter genes in DEAE-dextran-mediated transfection of mammalian cells.

T. Baldwin, M. Pazzagli, J. Devine, 1992, Analytical biochemistry.

Patents and literature

W. J. Warren, J. C. Hinshaw, K. Mullis, 1985 .

Individual α and β subunits of bacterial luciferase exhibit bioluminescence activity

T. Baldwin, J. Waddle, 1991 .

Studies on the complex formed between bacitracin A and divalent cations.

R. Gennis, T. Baldwin, D. A. Scogin, 1983, Biochimica et Biophysica Acta.

Isolation of the Escherichia coli iron superoxide dismutase gene: evidence that intracellular superoxide concentration does not regulate oxygen-dependent synthesis of the manganese superoxide dismutase.

T. Baldwin, C. Bull, J. Fee, 1984, Proceedings of the National Academy of Sciences of the United States of America.

Two Lysine Residues in the Bacterial Luciferase Mobile Loop Stabilize Reaction Intermediates

T. Baldwin, Z. Campbell, 2009, The Journal of Biological Chemistry.

Isolation of bacterial luciferases by affinity chromatography on 2,2-diphenylpropylamine-Sepharose: phosphate-mediated binding to an immobilized substrate analogue.

T. Holzman, T. Baldwin, 1982, Biochemistry.

Binding of 2,2-diphenylpropylamine at the aldehyde site of bacterial luciferase increases the affinity of the reduced riboflavin 5'-phosphate site.

T. Holzman, T. Baldwin, 1981, Biochemistry.

Interaction of Bacterial Luciferase with 8-Substituted Flavin Mononucleotide Derivatives (*)

F. Raushel, T. Baldwin, H. Abu-Soud, 1996, The Journal of Biological Chemistry.

Pulsed-alkylation mass spectrometry for the study of protein folding and dynamics: development and application to the study of a folding/unfolding intermediate of bacterial luciferase.

L. Dangott, T. Baldwin, P. Swartz, 2001, Biochemistry.

Observations of Spark‐Erosion Damage in Copper Crystals

T. Baldwin, H. D. Guberman, K. Bachmann, 1970 .

Active center-based immunoassay approach using bacterial luciferase.

T. Holzman, T. Baldwin, R. Holzman, 1986, Methods in enzymology.

Enhanced stable expression of aVibrio luciferase under the control of the Ω-translational enhancer in transgenic plants

T. Baldwin, C. Kado, K. Okumura, 1992, World journal of microbiology & biotechnology.

Enhanced stable expression luciferase under the control fMranslational enhancer in plants of a Vibrio of the transgenic

T. Baldwin, C. Kado, K. Okumura, 1992 .

The hemoglobins of the bullfrog, Rana catesbeiana. Partial amino acid sequence of the beta chain of the major adult component.

A. Riggs, T. Baldwin, 1974, The Journal of biological chemistry.

Cloning of the Vibrio harveyi luciferase genes: use of a synthetic oligonucleotide probe.

M. Simon, K. Nealson, R. Ogden, 1983, Proceedings of the National Academy of Sciences of the United States of America.

Fre Is the Major Flavin Reductase Supporting Bioluminescence from Vibrio harveyi Luciferase in Escherichia coli*

T. Baldwin, Z. Campbell, 2009, Journal of Biological Chemistry.

Overexpression of bacterial luciferase and purification from recombinant sources.

T. Baldwin, M. D. Thomas, M. Ziegler, 2000, Methods in enzymology.

Stopped-flow kinetic analysis of the bacterial luciferase reaction.

F. Raushel, L. S. Mullins, T. Baldwin, 1992, Biochemistry.

Expression in Escherichia coli K-12 of the 76,000-dalton iron-regulated outer membrane protein of Shigella flexneri confers sensitivity to cloacin DF13 in the absence of Shigella O antigen

T. Baldwin, M. Roberts, P. Williams, 1989, Infection and immunity.

Expression in Escherichia coli K-12 of the 76 , 000-Dalton Iron-Regulated Outer Membrane Protein of Shigella flexneri Confers Sensitivity to Cloacin DF 13 in the Absence of Shigella 0 Antigen

T. Baldwin, M. Roberts, P. Derbyshire, 2022 .

Proteolytic inactivation of luciferases from three species of luminous marine bacteria, Beneckea harveyi, Photobacterium fischeri, and Photobacterium phosphoreum: evidence of a conserved structural feature.

T. Holzman, T. Baldwin, 1980, Proceedings of the National Academy of Sciences of the United States of America.

Bioluminescence in Root Nodules of Soybean Controlled by Nitrogenase Promoters

T. Baldwin, A. Szalay, R. P. Legocki, 1987 .

Cloning of the luciferase structural genes from Vibrio harveyi and expression of bioluminescence in Escherichia coli.

T. Holzman, T. Baldwin, M. Ziegler, 1984, Biochemistry.

Light for All Reasons: Versatility in the Behavioral Repertoire of the Flashlight Fish

K. Nealson, J. W. Hastings, T. Baldwin, 1975, Science.

Polypeptide folding and dimerization in bacterial luciferase occur by a concerted mechanism in vivo.

T. Baldwin, J. Waddle, T. Johnston, 1987, Biochemistry.

Ratiometric pulsed alkylation/mass spectrometry of the cysteine pairs in individual zinc fingers of MRE-binding transcription factor-1 (MTF-1) as a probe of zinc chelate stability.

D. Giedroc, T. Baldwin, X. Chen, 2001, Biochemistry.

OBSERVATION OF X-RAY DIFFUSE SCATTERING FROM NEUTRON-IRRADIATED SILICON.

R. Coy, T. Baldwin, James E. Thomas, 1971 .

ACTIVE CENTER STUDIES ON BACTERIAL LUCIFERASE: EVIDENCE THAT THE REACTIVE CYSTEINYL RESIDUE IS WITHIN THE PROTEASE-LABILE REGION OF THE α SUBUNIT1

J. J. Dougherty, T. Baldwin, M. Merritt, 1981 .

Modification of the reactive sulfhydryl of bacterial luciferase with spin-labeled maleimides.

T. Baldwin, M. Merritt, 1980, Archives of biochemistry and biophysics.

Bacterial luciferase. Binding of oxidized flavin mononucleotide.

J. W. Hastings, T. Baldwin, J. Becvar, 1975, The Journal of biological chemistry.

A sensitive assay for proteolytic enzymes using bacterial luciferase as a substrate.

J. W. Hastings, T. Baldwin, D. Njus, 1974, Analytical biochemistry.

Structure of the β2 homodimer of bacterial luciferase from vibrio harveyi: X‐ray analysis of a kinetic protein folding trap

A. Fisher, I. Rayment, J. Thoden, 1997, Protein science : a publication of the Protein Society.

The 1.5-Å Resolution Crystal Structure of Bacterial Luciferase in Low Salt Conditions*

A. Fisher, I. Rayment, J. Thoden, 1996, The Journal of Biological Chemistry.

Carbon monoxide dehydrogenase from Clostridium thermoaceticum: quaternary structure, stoichiometry of its SDS-induced dissociation, and characterization of the faster-migrating form.

T. Baldwin, P. Lindahl, J. Sinclair, 1996, Biochemistry.

X‐Ray Debye Temperatures of Zinc Sulfide and Zinc Telluride

T. Baldwin, L. Walford, R. Blattner, 1972 .

X‐Ray Characteristic Temperatures of Some II—VI Ionic Compounds

T. Baldwin, C. W. Tompson, 1964 .

The x-ray characteristic temperature of potassium bromide as a function of temperature

T. Baldwin, C. W. Tompson, G. Pearman, 1965 .

Diffuse X-Ray Scattering in Fast-Neutron-Irradiated Copper Crystals

T. Baldwin, P. Dederichs, J. Thomas, 1971 .

Yellow light emission of Vibrio fischeri strain Y-1: purification and characterization of the energy-accepting yellow fluorescent protein.

T. Baldwin, S. Daubner, G. Leisman, 1987, Proceedings of the National Academy of Sciences of the United States of America.

The Amino Acid Sequence of the Monomeric Hemoglobin Component from the Bloodworm, Glycera dibranchiata

A. Riggs, T. Baldwin, T. Imamura, 1972 .

Chemical Aspects of Enzyme Biotechnology

F. Raushel, T. Baldwin, A. Scott, 1990, Industry-University Cooperative Chemistry Program Symposia.

[22] Bacterial luciferase as a generalized substrate for the assay of proteases

T. Baldwin, 1978 .

Identification of the operator of the lux regulon from the Vibrio fischeri strain ATCC7744.

T. Baldwin, G. Shadel, J. Devine, 1989, Proceedings of the National Academy of Sciences of the United States of America.

Site-directed mutagenesis of bacterial luciferase: analysis of the 'essential' thiol.

T. Baldwin, M. Ziegler, L. Chen, 1989, Journal of bioluminescence and chemiluminescence.

Effect of Neutron Irradiation on Copper Crystals at High Temperatures

T. Baldwin, F. Young, L. Hulett, 1968 .

Investigation of Fast‐Neutron Radiation Damage in Nearly Perfect Copper Crystals by X‐Ray Diffraction Techniques

T. Baldwin, F. Young, F. Sherrill, 1968 .

ABSOLUTE INTENSITIES OF X RAYS DIFFRACTED IN ANOMALOUS TRANSMISSION THROUGH NEARLY PERFECT COPPER CRYSTALS: A COMPARISON BETWEEN THEORY AND EXPERIMENT.

T. Baldwin, F. Young, A. Merlini, 1967 .

Use of Anomalous X‐Ray Transmission for the Detection of Defects Produced in Silicon and Germanium by Fast Neutron Irradiation

T. Baldwin, J. Thomas, 1968 .

A Camera for Borrmann Stereo X-Ray Topographs

T. Baldwin, F. Young, A. Merlini, 1965 .

Applications of Enzyme Biotechnology

J. Kelly, T. Baldwin, J. Kelly, 1991, Industry-University Cooperative Chemistry Program Symposia.

Crystal structure of the bacterial luciferase/flavin complex provides insight into the function of the beta subunit.

T. Baldwin, Andrzej Weichsel, W. Montfort, 2009, Biochemistry.

The hemoglobins of the bullfrog, Rana catesbeiana. The cDNA-derived amino acid sequences of the alpha chains of adult hemoglobins B and C: their roles in deoxygenation-induced aggregation.

B. Roe, P. Kolatkar, H. Zhu, 1993, The Journal of biological chemistry.

Purification of firefly luciferase from recombinant sources.

T. Baldwin, V. A. Green, 2000, Methods in enzymology.

Nucleotide sequence of the luxR and luxI genes and structure of the primary regulatory region of the lux regulon of Vibrio fischeri ATCC 7744

T. Baldwin, J. Devine, C. Countryman, 1988 .

Nucleotide sequence of the luxA gene of Vibrio harveyi and the complete amino acid sequence of the alpha subunit of bacterial luciferase.

M. Simon, K. Nealson, T. Baldwin, 1986, The Journal of biological chemistry.

[14] Bacterial luciferase: Assay, purification, and properties

J. W. Hastings, T. Baldwin, Nicoli Mz, 1978 .

GroE modulates kinetic partitioning of folding intermediates between alternative states to maximize the yield of biologically active protein.

A. Fedorov, T. Baldwin, A N Fedorov, 1997, Journal of molecular biology.

The complete nucleotide sequence of the lux regulon of Vibrio fischeri and the luxABN region of Photobacterium leiognathi and the mechanism of control of bacterial bioluminescence.

T. Baldwin, G. Shadel, J. Devine, 1989, Journal of bioluminescence and chemiluminescence.

Identification of a distantly located regulatory element in the luxD gene required for negative autoregulation of the Vibrio fischeri luxR gene.

T. Baldwin, G. Shadel, 1992, The Journal of biological chemistry.

Active center studies on bacterial luciferase: modification of the enzyme with 2,4-dinitrofluorobenzene.

T. Baldwin, W. Welches, 1981, Biochemistry.

Random and site-directed mutagenesis of bacterial luciferase: investigation of the aldehyde binding site.

T. Baldwin, L. Chen, 1989, Biochemistry.

Biochemistry of Bacterial Bioluminescence

T. Baldwin, M. Ziegler, 1981 .

The binding and spectral alterations of oxidized flavin mononucleotide by bacterial luciferase.

T. Baldwin, 1974, Biochemical and biophysical research communications.

Proteolytic inactivation of the luciferase from the luminous marine bacterium Beneckea harveyi.

J. W. Hastings, T. Baldwin, P. Riley, 1978, The Journal of biological chemistry.

Bacterial Bioluminescence. Mechanistic Implications of Active Center Chemistry of Luciferase

K. Nealson, J. W. Hastings, T. Cline, 1973 .

Interaction of bacterial luciferase with aldehyde substrates and inhibitors.

F. Raushel, T. Baldwin, H. Abu-Soud, 1993, The Journal of biological chemistry.

Three-dimensional structure of bacterial luciferase from Vibrio harveyi at 2.4 A resolution.

A. Fisher, I. Rayment, F. Raushel, 1995, Biochemistry.

Digitization of sedimentation equilibrium and velocity data for analysis by minicomputer.

T. Holzman, T. Baldwin, W. Mangel, 1982, Analytical biochemistry.

Algorithms for Finding the Axis of a Helix: Fast Rotational and Parametric Least-squares Methods

Rosemarie Swanson, Thomas O. Baldwin, Jon A. Christopher, 1996, Comput. Chem..

The Effect of Fast-Neutron Irradiation at Ambient Temperature on the Lattice Parameters of Silicon and Germanium Crystals

T. Baldwin, 1968 .

Control of cell division in Escherichia coli: regulation of transcription of ftsQA involves both rpoS and SdiA-mediated autoinduction.

T. Baldwin, D. Sitnikov, J. Schineller, 1996, Proceedings of the National Academy of Sciences of the United States of America.

Protein folding in vivo: the importance of ribosomes

Thomas O. Baldwin, T. Baldwin, 1999, Nature Cell Biology.

Effects of 3' end deletions from the Vibrio harveyi luxB gene on luciferase subunit folding and enzyme assembly: generation of temperature-sensitive polypeptide folding mutants.

T. Baldwin, J. Sugihara, 1988, Biochemistry.

Bioluminescence in soybean root nodules: Demonstration of a general approach to assay gene expression in vivo by using bacterial luciferase.

A A Szalay, M Legocki, T. Baldwin, 1986, Proceedings of the National Academy of Sciences of the United States of America.

Cloning and expression of the luxY gene from Vibrio fischeri strain Y-1 in Escherichia coli and complete amino acid sequence of the yellow fluorescent protein.

T. Baldwin, S. Daubner, M. L. Treat, 1990, Biochemistry.

Proposed mechanism for the bacterial bioluminescence reaction involving a dioxirane intermediate.

F. Raushel, T. Baldwin, 1989, Biochemical and Biophysical Research Communications - BBRC.

Interaction between luciferases from various species of bioluminescent bacteria and the yellow fluorescent protein of Vibrio fischeri strain Y-1.

T. Baldwin, S. Daubner, 1989, Biochemical and biophysical research communications.

Contribution of cotranslational folding to the rate of formation of native protein structure.

A. Fedorov, T. Baldwin, A N Fedorov, 1995, Proceedings of the National Academy of Sciences of the United States of America.

Firefly luciferase: the structure is known, but the mystery remains.

T. Baldwin, T O Baldwin, Thomas O. Baldwin, 1996, Structure.

The Vibrio fischeri LuxR protein is capable of bidirectional stimulation of transcription and both positive and negative regulation of the luxR gene

T. Baldwin, G. Shadel, Gerald S. Shadel, 1991, Journal of bacteriology.

Kinetic destabilization of the hydroperoxy flavin intermediate by site-directed modification of the reactive thiol in bacterial luciferase.

F. Raushel, T. Baldwin, A. C. Clark, 1993, The Journal of biological chemistry.

Functional implications of the unstructured loop in the (beta/alpha)(8) barrel structure of the bacterial luciferase alpha subunit.

T. Baldwin, J. M. Sparks, 2001, Biochemistry.

The effect of neutron irradiation on the lattice parameter and anomalous x‐ray transmission of silicon

T. Baldwin, James E. Thomas, James K. Haldeman, 1979 .

Effect of Dislocations on X‐Ray Diffraction Properties of Copper

T. Baldwin, F. Young, K. Bachmann, 1970 .

Implications of N and C-terminal proximity for protein folding.

T. Baldwin, J. Christopher, T O Baldwin, 1996, Journal of molecular biology.

Use of regulated cell lysis in a lethal genetic selection in Escherichia coli: identification of the autoinducer-binding region of the LuxR protein from Vibrio fischeri ATCC 7744

T. Baldwin, G. Shadel, R. Young, 1990, Journal of bacteriology.

Analysis of the bacterial luciferase mobile loop by replica-exchange molecular dynamics.

O. Miyashita, T. Baldwin, Z. Campbell, 2010, Biophysical journal.

Luciferase from the east European firefly Luciola mingrelica: cloning and nucleotide sequence of the cDNA, overexpression in Escherichia coli and purification of the enzyme.

T. Baldwin, T O Baldwin, J. Devine, 1993, Biochimica et biophysica acta.

Reversible inhibition of the bacterial luciferase catalyzed bioluminescence reaction by aldehyde substrate: kinetic mechanism and ligand effects

T. Holzman, T. Baldwin, 1983 .

Purified native subunits of bacterial luciferase are active in the bioluminescence reaction but fail to assemble into the alpha beta structure.

T. Baldwin, J. Sinclair, J. Waddle, 1993, Biochemistry.

Purification of bacterial luciferase by affinity methods.

T. Holzman, T. Baldwin, V. Riddle, 1986, Methods in enzymology.

The effects of phosphate on the structure and stability of the luciferases from Beneckea harveyi, Photobacterium fischeri, and Photobacterium phosphoreum.

T. Holzman, T. Baldwin, 1980, Biochemical and biophysical research communications.

Bacterial luciferase activity does not require a disulfide-dithiol conversion.

J. W. Hastings, T. Baldwin, S. Tu, 1977, Archives of biochemistry and biophysics.

Kinetic partitioning during protein folding yields multiple native states

T. Baldwin, M. Ziegler, J. Sinclair, 1994, Nature Structural Biology.

A plasmid vector and quantitative techniques for the study of transcription termination in Escherichia coli using bacterial luciferase.

T. Baldwin, D. Bear, D. Peabody, 1989, Gene.

Anomalous x‐ray transmission evidence for clustering in the annealing stage of neutron‐irradiated copper

E. E. Gruber, T. Baldwin, T. H. Blewitt, 1974 .

The Temperature Dependence of the Borrmann Effect in Copper

T. Baldwin, 1968, January 1.

Folding of bacterial luciferase involves a non-native heterodimeric intermediate in equilibrium with the native enzyme and the unfolded subunits.

T. Baldwin, A. C. Clark, J. Sinclair, 1993, The Journal of biological chemistry.

Inactivation of luciferase from the Luminous marine bacterium Beneckea harveyi by proteases: evidence for a protease labile region and properties of the protein following inactivation.

T. Holzman, T. Baldwin, P. Riley, 1980, Archives of biochemistry and biophysics.

A rapid chromatographic method to separate the subunits of bacterial luciferase in urea-containing buffer.

T. Baldwin, B. Noland, A. C. Clark, 2000, Methods in enzymology.

Positive autoregulation of the Vibrio fischeri luxR gene. LuxR and autoinducer activate cAMP-catabolite gene activator protein complex-independent and -dependent luxR transcription.

T. Baldwin, G. Shadel, T O Baldwin, 1992, The Journal of biological chemistry.

The amino acid sequence of the monomeric hemoglobin component from the bloodworm, Glyat liver.

A. Riggs, T. Baldwin, T. Imamura, 1972, The Journal of biological chemistry.

Cotranslational Protein Folding*

A. Fedorov, T. Baldwin, 1997, The Journal of Biological Chemistry.

ACTIVE CENTER STUDIES ON BACTERIAL LUCIFERASE: MODIFICATION WITH METHYL METHANETHIOLSULFONATE

T. Baldwin, M. Ziegler, 1981 .

A Study of Subunit Folding and Dimer Assembly In Vivo

T. Baldwin, 1990 .