P. Horowitz

发表

Green fluorescent protein as a marker for gene expression and cell biology of mycobacterial interactions with macrophages

S. Dhandayuthapani, V. Deretic, L. VIa, 1995, Molecular microbiology.

Binding of ethidium to bacteriophages t7 and p22.

P. Horowitz, G. Greiss, P. Serwer, 1986, Biophysical journal.

Bis(1,8-anilinonaphthalenesulfonate). A novel and potent inhibitor of microtubule assembly.

P. Horowitz, V. Prasad, R. Ludueña, 1984, The Journal of biological chemistry.

Hydrophobic Surfaces That Are Hidden in Chaperonin Cpn60 Can Be Exposed by Formation of Assembly-Competent Monomers or by Ionic Perturbation of the Oligomer (*)

D. Gibbons, P. Horowitz, S. Hua, 1995, The Journal of Biological Chemistry.

Detergent-assisted refolding of guanidinium chloride-denatured rhodanese. The effect of lauryl maltoside.

P. Horowitz, S. Tandon, 1986, The Journal of biological chemistry.

Chaperonins facilitate the in vitro folding of monomeric mitochondrial rhodanese.

G. Lorimer, P. Horowitz, E. Rogers, 1991, The Journal of biological chemistry.

Intermediates in the chaperonin-assisted refolding of rhodanese are trapped at low temperature and show a small stoichiometry.

G. Lorimer, P. Horowitz, J. A. Mendoza, 1991, The Journal of biological chemistry.

Bound substrate polypeptides can generally stabilize the tetradecameric structure of Cpn60 and induce its reassembly from monomers.

P. Horowitz, J. A. Mendoza, 1994, The Journal of biological chemistry.

Refolding and Reassembly of Active Chaperonin GroEL After Denaturation (*)

P. Horowitz, J. Ybarra, 1995, The Journal of Biological Chemistry.

Tetradecameric chaperonin 60 can be assembled in vitro from monomers in a process that is ATP independent.

P. Horowitz, J. A. Mendoza, J. L. Martinez, 1995, Biochimica et biophysica acta.

6.1 – The Competition among Biprotonic Phototautomerism, Excimer Formation, and Proton Tunneling in DNA Base-Pairs†

M. Kasha, P. Horowitz, M. El-Bayoumi, 1972 .

Folding and aggregation of TEM β‐lactamase: Analogies with the formation of inclusion bodies in Escherichia coli

G. Georgiou, M. Ostermeier, P. Horowitz, 1994, Protein science : a publication of the Protein Society.

Low concentrations of guanidinium chloride expose apolar surfaces and cause differential perturbation in catalytic intermediates of rhodanese.

P. Horowitz, N. Criscimagna, 1986, The Journal of biological chemistry.

Interactive intermediates are formed during the urea unfolding of rhodanese.

P. Horowitz, M. Butler, 1993, The Journal of biological chemistry.

Detection of energy transfer between tryptophan residues in the tubulin molecule and bound bis(8-anilinonaphthalene-1-sulfonate), an inhibitor of microtubule assembly, that binds to a flexible region on tubulin.

P. Horowitz, R. Luduena, A. R. Prasad, 1986, Biochemistry.

Oxidation increases the proteolytic susceptibility of a localized region in rhodanese.

P. Horowitz, S. Bowman, 1987, The Journal of biological chemistry.

Characterization of a stable, reactivatable complex between chaperonin 60 and mitochondrial rhodanese.

P. Horowitz, J. A. Mendoza, M. Butler, 1992, The Journal of biological chemistry.

Chaperonin cpn60 from Escherichia coli protects the mitochondrial enzyme rhodanese against heat inactivation and supports folding at elevated temperatures.

G. Lorimer, P. Horowitz, J. A. Mendoza, 1992, The Journal of biological chemistry.

Ion-enhanced fluorescence staining of sodium dodecyl sulfate-polyacrylamide gels using bis(8-p-toluidino-1-naphthalenesulfonate).

P. Horowitz, S. Bowman, 1987, Analytical biochemistry.

the formation of inclusion bodies in Escherichia coli Folding and aggregation of TEM { beta }-lactamase : Analogies with

G. Georgiou, P. Horowitz, P. Valax, 2002 .

Rhodanese folding is controlled by the partitioning of its folding intermediates.

P. Horowitz, B. Gorovits, W. A. McGee, 1998, Biochimica et biophysica acta.

Aspects of secondary and quaternary structure of surfactant protein A from canine lung.

P. Horowitz, D. Simon, R. J. King, 1989, Biochimica et biophysica acta.

The initiation codon AUG binds at a hydrophobic site on yeast 40S ribosomal subunits as revealed by fluorescence studies with bis (1,8-anilinonaphthalenesulfonate).

J. Lee, P. Horowitz, L. Yeh, 1991, Biochimie.

Nucleotides Reveal Polynucleotide Phosphorylase Activity from Conventionally Purified GroEL*

P. Horowitz, J. Ybarra, Jesse Ybarra, 1996, The Journal of Biological Chemistry.

Binding of colchicine to renal tubulin at 5°C

L. D. Barnes, P. Horowitz, Robert F. Williams, 1983 .

Use of 6-p-toluidino-2-naphthalenesulfonic acid to quantitate lipids after thin-layer chromatography

P. Horowitz, Marjorie A. Jones, R. Keenan, 1982 .

An additional serine residue at the C terminus of rhodanese destabilizes the enzyme.

P. Horowitz, G. Kramer, B. Hardesty, 2001, Archives of biochemistry and biophysics.

Interactions of Vinblastine and Maytansine with Tubulin a

D. Murphy, P. Horowitz, M. Jordan, 1986, Annals of the New York Academy of Sciences.

Thermally perturbed rhodanese can be protected from inactivation by self-association

P. Horowitz, J. Dungan, 1993, Journal of protein chemistry.

Purification of bovine liver rhodanese by low-pH column chromatography.

G. Kurzban, P. Horowitz, 1991, Protein expression and purification.

A study of the single polypeptide nature of rhodanese. A comparison of different preparations.

P. Horowitz, J. M. Crawford, 1976, Biochimica et biophysica acta.

The effects of the anilinonaphthalenesulfonates on the alkylation of tubulin: correlation between the appearance of sulfhydryl groups and apolar binding sites.

P. Horowitz, R. Luduena, M. C. Roach, 1986, Biochimica et biophysica acta.

Bis(8-anilinonaphthalene-1-sulfonate) as a probe for tubulin decay.

P. Horowitz, R. Luduena, A. R. Prasad, 1986, Biochemistry.

Interaction of tubulin with the macromolecular apolar probe, octyl sepharose.

P. Horowitz, V. Prasad, R. Ludueña, 1987, Biochemical and biophysical research communications.

Activation of Pseudomonas cytochrome oxidase by limited proteolysis with subtilisin.

P. Horowitz, B. Muhoberac, D. Wharton, 1982, The Journal of biological chemistry.

Unassisted refolding of urea unfolded rhodanese.

G. Lorimer, P. Horowitz, E. Rogers, 1991, The Journal of biological chemistry.

Fluorescence anisotropy method for investigation of GroEL-GroES interaction.

P. Horowitz, B. Gorovits, 1998, Methods in enzymology.

The Importance of the N-terminal Segment for DnaJ-mediated Folding of Rhodanese While Bound to Ribosomes as Peptidyl-tRNA (*)

O. W. Odom, P. Horowitz, G. Kramer, 1995, The Journal of Biological Chemistry.

Physical characterization of a reactivatable liposome-bound rhodanese folding intermediate.

P. Horowitz, G. Zardeneta, 1993, Biochemistry.

GroEL and GroES increase the specific enzymatic activity of newly-synthesized rhodanese if present during in vitro transcription/translation.

P. Horowitz, G. Kramer, B. Hardesty, 1993, Biochemistry.

Cardiolipin liposomes sequester a reactivatable partially folded rhodanese intermediate.

P. Horowitz, G. Zardeneta, 1992, European journal of biochemistry.

Photoincorporation of 4,4'-bis(1-anilino-8-naphthalenesulfonic acid) into the apical domain of GroEL: specific information from a nonspecific probe.

P. Horowitz, J. L. Martinez, J. Seale, 1995, Biochemistry.

The binding of bis-ANS to the isolated GroEL apical domain fragment induces the formation of a folding intermediate with increased hydrophobic surface not observed in tetradecameric GroEL.

A. Fersht, A. Buckle, P. Horowitz, 2001, Biochemistry.

Mutation in the interdomain tether influences the stability and refolding of the enzyme rhodanese.

P. Horowitz, S. Hua, G. Luo, 1995, Biochimica et biophysica acta.

Interaction between the 35 kDa apolipoprotein of pulmonary surfactant and saturated phosphatidylcholines. Effects of temperature.

P. Horowitz, M. Phillips, R. J. King, 1986, Biochimica et biophysica acta.

The effects of lauryl maltoside on the reactivation of several enzymes after treatment with guanidinium chloride.

P. Horowitz, S. Tandon, 1988, Biochimica et biophysica acta.

Differential binding of the fluorescent probe 8-anilinonaphthalene-2-sulfonic acid to rhodanese catalytic intermediates.

P. Horowitz, N. Criscimagna, 1985, Biochemistry.

Localization of the ganglioside-binding site of fibronectin.

K. Bentley, D. D. Thomas, P. Horowitz, 1986, The Journal of biological chemistry.

Shielding of tryptophan residues of avidin by the binding of biotin.

M. Wilchek, E. Bayer, G. Kurzban, 1989, Biochemistry.

Intrinsic fluorescence of succinyl-CoA synthetase and four tryptophan mutants. Tryptophan 76 and tryptophan 248 of the beta-subunit are responsive to CoA binding.

P. Horowitz, J. Ybarra, J. Nishimura, 1990, Biochemistry.

Detection, characterization, and quenching of the intrinsic fluorescence of bovine heart cytochrome c oxidase.

P. Horowitz, N. C. Robinson, B. Hill, 1986, Biochemistry.

Active Rhodanese Lacking Nonessential Sulfhydryl Groups Has Increased Hydrophobic Exposure Not Observed in Wild-Type Enzyme

P. Horowitz, J. Ybarra, Yogeet Kaur, 2004, The protein journal.

Active Rhodanese Lacking Nonessential Sulfhydryl Groups Contains an Unstable C-terminal Domain and Can Be Bound, Inactivated, and Reactivated by GroEL*

P. Horowitz, A. Bhattacharyya, M. Panda, 2003, The Journal of Biological Chemistry.

Domain Separation Precedes Global Unfolding of Rhodanese*

P. Horowitz, G. Kramer, B. Hardesty, 1999, The Journal of Biological Chemistry.

The C-terminal Sequence of the Chaperonin GroES Is Required for Oligomerization (*)

P. Horowitz, J. Seale, 1995, The Journal of Biological Chemistry.

The sulfurtransferase activity and structure of rhodanese are affected by site-directed replacement of Arg-186 or Lys-249.

P. Horowitz, G. Luo, 1994, The Journal of biological chemistry.

Electrophoresis of proteins and nucleic acids on acrylamide-agarose gels lacking covalent crosslinking.

L. D. Barnes, R. F. Williams, J. Lee, 1984, Analytical biochemistry.

The use of polyacrylamide gels that can be dissassembled and reassembled to permit a wide variety of electrophoretic procedures with a common polymerization history

P. Horowitz, S. Bowman, 1986 .

Studies of the N-bromosuccinimide inactivation of the enzyme rhodanese.

P. Horowitz, K. Guido, 1977, Biochimica et biophysica acta.

Reassembly of lipid-protein complexes of pulmonary surfactant. Proposed mechanism of interaction.

P. Horowitz, R. J. King, M. Carmichael, 1983, The Journal of biological chemistry.

Binding of ethidium to bacteriophage T7 and T7 deletion mutants

P. Horowitz, P. Serwer, G. Griess, 1985, Biopolymers.

Conditions of Forming Protein Complexes with GroEL Can Influence the Mechanism of Chaperonin-assisted Refolding*

P. Horowitz, B. Gorovits, 1997, The Journal of Biological Chemistry.

Heparin binding is necessary, but not sufficient, for fibronectin aggregation. A fluorescence polarization study.

K. Bentley, P. Horowitz, R. Klebe, 1985, The Journal of biological chemistry.

Chaperonin-assisted protein folding of the enzyme rhodanese by GroEL/GroES.

P. Horowitz, 1995, Methods in molecular biology.

The specificity of active-site alkylation by iodoacetic acid in the enzyme thiosulfate sulfurtransferase.

P. Horowitz, N. Criscimagna, 1982, Biochimica et biophysica acta.

The Aggregation State of Rhodanese during Folding Influences the Ability of GroEL to Assist Reactivation*

P. Horowitz, A. Bhattacharyya, 2001, The Journal of Biological Chemistry.

The chaperonin assisted and unassisted refolding of rhodanese can be modulated by its N-terminal peptide

P. Horowitz, J. A. Mendoza, 1994, Journal of protein chemistry.

Preliminary studies of the secondary structure in solution of two phosphoproteins of chicken bone matrix by Circular Dichroism and Fourier Tranform-Infrared Spectroscopy

M. Glimcher, V. Renugopalakrishnan, P. Horowitz, 1986, Calcified Tissue International.

Rhodanese as a thioredoxin oxidase.

P. Horowitz, J. Westley, D. Nandi, 2000, The international journal of biochemistry & cell biology.

Some comparisons between solution and crystal properties of thiosulfate sulfurtransferase.

P. Horowitz, K. Patel, 1980, Biochemical and biophysical research communications.

Purification of thiosulfate sulfurtransferase by selective immobilization on blue agarose.

P. Horowitz, 1978, Analytical biochemistry.

A chaperone-mimetic effect of serum albumin on rhodanese.

P. Horowitz, J. Westley, J. Dungan, 1993, Journal of biochemical toxicology.

pi. vs. .sigma. Structures in imidazyl and related heteroraticals

P. Horowitz, T. Lee, E. Evleth, 1973 .

The diverse chemical forms of heavy metals in tissue extracts of some metallophytes from Shaba Province, Zaïre

R. S. Morrison, P. Horowitz, F. Malaisse, 1981 .

Detergent-assisted refolding of guanidinium chloride-denatured rhodanese. The effects of the concentration and type of detergent.

P. Horowitz, S. Tandon, 1987, The Journal of biological chemistry.

A simple, inexpensive, and precise microcell for the exchange dialysis and equilibrium dialysis of small samples.

L. D. Barnes, P. Horowitz, 1983, Analytical biochemistry.

Divalent Cations Can Induce the Exposure of GroEL Hydrophobic Surfaces and Strengthen GroEL Hydrophobic Binding Interactions

P. Horowitz, J. Ybarra, Bill T. Brazil, 1998, The Journal of Biological Chemistry.

The influence of chaotropic reagents on neuronal nitric oxide synthase and its flavoprotein module. Urea and guanidine hydrochloride stimulate NADPH-cytochrome c reductase activity of both proteins.

B. Masters, P. Horowitz, K. McMillan, 1997, Nitric oxide : biology and chemistry.

Residual structure in urea-denatured chaperonin GroEL.

P. Horowitz, B. Gorovits, J. Seale, 1995, Biochemistry.

Studies of the secondary structures of amelogenin from bovine tooth enamel.

M. Glimcher, V. Renugopalakrishnan, P. Horowitz, 1986, Biochemistry.

A reexamination of the postulated charge transfer interactions at the active site of the enzyme rhodanese.

P. Horowitz, R. Baillie, 1976, Biochimica et biophysica acta.

The interaction of α2 macroglobulin with trypsin releases a soluble glycopeptide

P. Horowitz, A. Elbein, Y. T. Pan, 1980 .

Comparative photophysics of indolizine and related heterocyclics

P. Horowitz, D. Lerner, E. Evleth, 1977 .

Activation Parameters for the Spontaneous and Pressure-Induced Phases of the Dissociation of Single-Ring GroEL (SR1) Chaperonin

P. Horowitz, M. Panda, 2004, The Protein Journal.

Isolation, amino acid analyses and refolding of subunits of pig heart succinyl-CoA synthetase.

P. Horowitz, J. Ybarra, J. Nishimura, 1988, Biochemical Journal.

Single synonymous codon substitution eliminates pausing during chloramphenicol acetyl transferase synthesis on Escherichia coli ribosomes in vitro

P. Horowitz, G. Kramer, B. Hardesty, 2002, FEBS letters.

The stability of the molecular chaperonin cpn60 is affected by site-directed replacement of cysteine 518.

P. Horowitz, G. Luo, 1994, The Journal of biological chemistry.

Fluorescence polarization a general method for measuring ligand binding and membrane microviscosity

K. Bentley, P. Horowitz, R. Klebe, 1985 .

Secondary structure of a core protein from pig skin proteodermatan sulfate: Cd and fourier transform ir spectroscopic studies in solution

J. D. Gregory, V. Renugopalakrishnan, P. Horowitz, 1989, Biopolymers.

High hydrostatic pressure can reverse aggregation of protein folding intermediates and facilitate acquisition of native structure.

P. Horowitz, B M Gorovits, P M Horowitz, 1998, Biochemistry.

The Molecular Chaperonin cpn60 Displays Local Flexibility That Is Reduced after Binding with an Unfolded Protein (*)

P. Horowitz, B. Gorovits, 1995, The Journal of Biological Chemistry.

The quaternary structure of streptavidin in urea.

M. Wilchek, E. Bayer, G. Kurzban, 1991, The Journal of biological chemistry.

The folding and stability of rhodanese are influenced by the replacement of glutamic acid 17 in the NH2-terminal helix by proline but not by glutamine.

P. Horowitz, G. Luo, 1993, The Journal of biological chemistry.

Truncations at the NH2 Terminus of Rhodanese Destabilize the Enzyme and Decrease Its Heterologous Expression*

J. Chirgwin, P. Horowitz, G. Kramer, 1998, The Journal of Biological Chemistry.

Reversible folding of rhodanese. Presence of intermediate(s) at equilibrium.

P. Horowitz, S. Tandon, 1989, The Journal of biological chemistry.

A comparison between 8-anilinonaphthalene-1-suifonate and 2-p-toluidinylnaphthalene-6-sulfonate as fluorescent indicators of the critical micelle concentration of sodium dodecyl sulfate

P. Horowitz, 1977 .

Studies on rhodanese synthesis in bovine adrenocortical cells.

M. Waterman, V. Boggaram, P. Horowitz, 1985, Biochemical and biophysical research communications.

Improved preparation of bovine liver rhodanese.

P. Horowitz, F. Detoma, 1970, The Journal of biological chemistry.

Extraction of proteins from Saccharomyces cerevisiae ribosomes under nondenaturing conditions.

J. Lee, P. Horowitz, Y. Yeh, 1985, Archives of biochemistry and biophysics.

A study of the quenching of the intrinsic fluorescence of succinyl-CoA synthetase from Escherichia coli by acrylamide, iodide, and coenzyme A.

P. Horowitz, A. R. Prasad, J. Nishimura, 1983, Biochemistry.

A study of the apolar interaction of the enzyme rhodanese with octyl substituted agarose gel.

P. Horowitz, N. Criscimagna, 1983, Biochemical and biophysical research communications.

A fluorescence study of conformational changes induced by substrate and temperature in bovine liver thiosulfate sulfurtransferase.

Z. Wasylewski, P. Horowitz, 1982, Biochimica et biophysica acta.

The aromatic residue content of the enzyme rhodanese.

P. Horowitz, R. Baillie, 1976, Biochimica et biophysica acta.

Spectral studies of the tryptophan exposure in the enzyme rhodanese.

P. Horowitz, R. Baillie, K. Guido, 1976, Biochimica et biophysica acta.

Contact versus energy transfer fluorescence quenching in the sulfur substituted form of the enzyme rhodanese: a study using cesium ion resolved emission spectra.

P. Horowitz, K. Guido, 1975, Biochemical and biophysical research communications.

Micelle-assisted protein folding. Denatured rhodanese binding to cardiolipin-containing lauryl maltoside micelles results in slower refolding kinetics but greater enzyme reactivation.

P. Horowitz, G. Zardeneta, Paul M. Horowitz, 1992, The Journal of biological chemistry.

Reversible thermal denaturation of immobilized rhodanese.

P. Horowitz, S. Bowman, 1987, The Journal of biological chemistry.

Conditions for Nucleotide-dependent GroES-GroEL Interactions

P. Horowitz, J. Ybarra, B. Gorovits, 1997, The Journal of Biological Chemistry.

Expression of cloned bovine adrenal rhodanese.

J. Chirgwin, S. Hardies, P. Horowitz, 1991, The Journal of biological chemistry.

Alteration Around the Active Site of Rhodanese during Urea-induced Denaturation and Its Implications for Folding*

P. Horowitz, A. Bhattacharyya, 2000, The Journal of Biological Chemistry.

Assisted Protein Folding by Amphiphiles and Molecular Chaperones

P. Horowitz, 1997 .

Reversible oligomerization and denaturation of the chaperonin GroES.

P. Horowitz, J. Ybarra, B. Gorovits, 1996, Biochemistry.

Active-Site Sulfhydryl Chemistry Plays a Major Role in the Misfolding of Urea-Denatured Rhodanese

P. Horowitz, M. Panda, 2000, Journal of protein chemistry.

Cysteine 254 can cooperate with active site cysteine 247 in reactivation of 5,5'-dithiobis(2-nitrobenzoic acid)-inactivated rhodanese as determined by site-directed mutagenesis.

P. Horowitz, S. Hua, D. Miller‐Martini, 1994, The Journal of biological chemistry.

Mutations of noncatalytic sulfhydryl groups influence the stability, folding, and oxidative susceptibility of rhodanese.

J. Chirgwin, P. Horowitz, D. M. Miller-Martini, 1994, Journal of Biological Chemistry.

Oxidative inactivation of the enzyme rhodanese by reduced nicotinamide adenine dinucleotide.

P. Horowitz, K. Falksen, 1986, The Journal of biological chemistry.

The enzyme rhodanese can be reactivated after denaturation in guanidinium chloride.

P. Horowitz, D. Simon, 1986, The Journal of biological chemistry.

Enhancement of rhodanese activity during controlled digestion with trypsin.

B. Trumpower, P. Horowitz, A. Katki, 1974, Biochemical and biophysical research communications.

Rhodanese conformational changes permit oxidation to give disulfides that form in a kinetically determined sequence.

P. Horowitz, S. Hua, 1995, Biochimica et biophysica acta.

Alteration of the quaternary structure of cpn60 modulates chaperonin-assisted folding. Implications for the mechanism of chaperonin action.

P. Horowitz, B. Demeler, J. A. Mendoza, 1994, The Journal of biological chemistry.

Reducing sugars can induce the oxidative inactivation of rhodanese.

P. Horowitz, M. Butler, G. D. Mcclure, 1992, The Journal of biological chemistry.

Oxidative inactivation of rhodanese by hydrogen peroxide produces states that show differential reactivation.

P. Horowitz, S. Bowman, 1989, The Journal of biological chemistry.

Sulfhydryl-directed triggering of conformational changes in the enzyme rhodanese.

P. Horowitz, N. Criscimagna, 1988, Journal of Biological Chemistry.

Conformational changes accompany the oxidative inactivation of rhodanese by a variety of reagents.

P. Horowitz, S. Bowman, 1987, The Journal of biological chemistry.

High Hydrostatic Pressure Can Probe the Effects of Functionally Related Ligands on the Quaternary Structures of the Chaperonins GroEL and GroES*

P. Horowitz, M. Panda, J. Ybarra, 2001, The Journal of Biological Chemistry.

Preformed GroES Oligomers Are Not Required as Functional Cochaperonins

J. Chirgwin, P. Horowitz, B. Demeler, 1997, Journal of protein chemistry.

Intrinsic Fluorescence Studies of the Chaperonin GroEL Containing Single Tyr → Trp Replacements Reveal Ligand-induced Conformational Changes*

P. Lund, P. Horowitz, J. Ybarra, 1996, The Journal of Biological Chemistry.

Ligand-induced Conformational Changes in the Apical Domain of the Chaperonin GroEL (*)

D. Gibbons, P. Horowitz, 1996, The Journal of Biological Chemistry.

NH2-terminal Sequence Truncation Decreases the Stability of Bovine Rhodanese, Minimally Perturbs Its Crystal Structure, and Enhances Interaction with GroEL under Native Conditions*

J. Chirgwin, P. Horowitz, G. Zanotti, 1999, The Journal of Biological Chemistry.

GroES in the asymmetric GroEL14-GroES7 complex exchanges via an associative mechanism.

G. Lorimer, P. Horowitz, J. Ybarra, 1999, Proceedings of the National Academy of Sciences of the United States of America.

ATP Hydrolysis Is Critical for Induction of Conformational Changes in GroEL That Expose Hydrophobic Surfaces*

P. Horowitz, J. Ybarra, B. Gorovits, 1997, The Journal of Biological Chemistry.

Protein refolding at high concentrations using detergent/phospholipid mixtures.

P. Horowitz, G. Zardeneta, 1994, Analytical biochemistry.

A physical characterization of sulfane sulfurtransferase.

P. Horowitz, B. A. Aird, 1990, Biochimica et biophysica acta.

Chemical modification of bovine liver rhodanese with tetrathionate: differential effects on the sulfur-free and sulfur-containing catalytic intermediates.

P. Horowitz, A. R. Prasad, A. Prasad, 1987, Biochimica et biophysica acta.

The use of tritium exchange to detect conformational differences between intermediates in catalysis by the enzyme rhodanese.

P. Horowitz, K. Falksen, 1983, Biochimica et biophysica acta.

The differential functional stability of various forms of bovine liver rhodanese.

P. Horowitz, B. A. Aird, 1988, Biochimica et biophysica acta.

Denaturation-induced disulfide formation in the enzyme rhodanese.

P. Horowitz, R. Baillie, 1976, Biochimica et biophysica acta.

Ironing out the protein folding problem?

P. Horowitz, 1999, Nature Biotechnology.

Partially folded rhodanese or its N-terminal sequence can disrupt phospholipid vesicles

P. Horowitz, J. A. Mendoza, Earl Grant, 1993, Journal of protein chemistry.

Recombinant bovine rhodanese: purification and comparison with bovine liver rhodanese.

J. Chirgwin, G. Kurzban, S. Hardies, 1992, Biochimica et Biophysica Acta.

Productive and Nonproductive Intermediates in the Folding of Denatured Rhodanese*

P. Horowitz, M. Panda, B. Gorovits, 2000, The Journal of Biological Chemistry.

Photoincorporation of fluorescent probe into GroEL: defining site of interaction.

P. Horowitz, J. Seale, B. Brazil, 1998, Methods in enzymology.

Inactive GroEL Monomers Can Be Isolated and Reassembled to Functional Tetradecamers That Contain Few Bound Peptides (*)

P. Horowitz, J. Ybarra, 1995, The Journal of Biological Chemistry.

Exposure of Hydrophobic Surfaces on the Chaperonin GroEL Oligomer by Protonation or Modification of His-401 (*)

P. Horowitz, Paul M. Horowitz, Don L. Gibbons, 1995, The Journal of Biological Chemistry.

High Hydrostatic Pressure Induces the Dissociation of cpn60 Tetradecamers and Reveals a Plasticity of the Monomers (*)

P. Horowitz, B. Gorovits, C. Raman, 1995, The Journal of Biological Chemistry.

Immunological evidence for a conformational difference between recombinant bovine rhodanese and rhodanese purified from bovine liver

J. Chirgwin, P. Horowitz, G. Merrill, 1992, Journal of protein chemistry.

Acceptor substrate-potentiated inactivation of bovine liver rhodanese.

P. Horowitz, B. A. Aird, 1988, The Journal of biological chemistry.

Evidence for dynamically determined conformational states in rhodanese catalysis.

P. Horowitz, J. Westley, R. Jarabak, 1985, The Journal of biological chemistry.

The Chaperonin GroEL Is Destabilized by Binding of ADP (*)

P. Horowitz, B. Gorovits, Boris M. Gorovits, 1995, The Journal of Biological Chemistry.

Limited tryptic digestion near the amino terminus of bovine liver rhodanese produces active electrophoretic variants with altered refolding.

P. Horowitz, M. Butler, G. Merrill, 1993, The Journal of biological chemistry.

Model Peptide Studies Demonstrate That Amphipathic Secondary Structures Can Be Recognized by the Chaperonin GroEL (cpn60)*

N. Skelton, P. Horowitz, R. Mcdowell, 1997, The Journal of Biological Chemistry.

Sulfhydryl modification ofE. coli cpn60 leads to loss of its ability to support refolding of rhodanese but not to form a binary complex

P. Horowitz, J. A. Mendoza, 1992, Journal of protein chemistry.

Stable intermediates can be trapped during the reversible refolding of urea-denatured rhodanese.

P. Horowitz, N. Criscimagna, 1990, The Journal of biological chemistry.

The molecular chaperone DnaK is not recruited to translating ribosomes that lack trigger factor.

P. Horowitz, G. Kramer, B. Hardesty, 2002, Archives of biochemistry and biophysics.

Tetracyanonickelate probes the active site of sulfur-free rhodanese.

P. Horowitz, S. F. Chow, 1985, The Journal of biological chemistry.

The use of intrinsic protein fluorescence to quantitate enzyme-bound persulfide and to measure equilibria between intermediates in rhodanese catalysis.

P. Horowitz, N. Criscimagna, 1983, The Journal of biological chemistry.

A study of dithiothreitol inactivation of the enzyme rhodanese.

P. Horowitz, S. -. Kim, 1975, Biochemical and biophysical research communications.

Some molecular properties of rhodanese.

P. Horowitz, J. Westley, 1970, The Journal of biological chemistry.

Biotin binding changes the conformation and decreases tryptophan accessibility of streptavidin

M. Wilchek, E. Bayer, G. Kurzban, 1990, Journal of protein chemistry.

The detection of kinetic intermediate(s) during refolding of rhodanese.

P. Horowitz, S. Tandon, 1990, The Journal of biological chemistry.

Detection of time-dependent and oxidatively induced antigens of bovine liver rhodanese with monoclonal antibodies.

K. Bentley, P. Horowitz, R. Klebe, 1988, The Journal of biological chemistry.

Proteolytic interconversion of electrophoretic variants of the enzyme rhodanese.

P. Horowitz, K. Falksen, 1983, The Journal of biological chemistry.

Facilitation of Protein Folding and the Reversibility of Denaturation

P. Horowitz, 1993 .

Fluorometric detection of low temperature thermal transitions in the C1Q component of human complement.

Z. Wasylewski, P. Horowitz, W. Kolb, 1980, Biochemical and biophysical research communications.

Kinetics of ethidium's intercalation in packaged bacteriophage T7 DNA: Effects of DNA packing density

P. Horowitz, Gary A. Griess, Philip Serwer, 1986, Biopolymers.

Tritium exchange kinetics of yeast ribosomal subunits.

J. Lee, P. Horowitz, 1987, Biochimica et biophysica acta.

Rapid fluorescamine based protein assay usable in the presence of interfering substances.

P. Horowitz, 1985, Journal of chromatography.

Rhodanese can partially refold in its GroEL-GroES-ADP complex and can be released to give a homogeneous product.

P. Horowitz, A. Bhattacharyya, 2002, Biochemistry.

Fluorescence detection of increased local flexibility induced by coenzyme A in succinyl-coA synthetase from Escherichia coli.

P. Horowitz, A. R. Prasad, J. Nishimura, 1982, Biochemistry.

Detergent, liposome, and micelle-assisted protein refolding.

P. Horowitz, G. Zardeneta, 1994, Analytical biochemistry.

Studies of RNA-protein interactions in the yeast 5 S ribonucleoprotein particles by fluorescence and tritium exchange. Implications for ribosomal assembly.

J. Lee, P. Horowitz, L. Yeh, 1988, The Journal of biological chemistry.

The 4,4'-dipyridyl disulfide-induced formation of GroEL monomers is cooperative and leads to increased hydrophobic exposure.

P. Horowitz, M. Panda, A. L. Smoot, 2001, Biochemistry.

Analysis of the perturbation of phospholipid model membranes by rhodanese and its presequence.

P. Horowitz, G. Zardeneta, 1992, The Journal of biological chemistry.

Yeast 5S rRNA binding to ribosomal protein L1a alters the fluorescence of tryptophan residues lying outside the binding site.

J. Lee, P. Horowitz, L. Yeh, 1992, Biochimie.

Micelle-assisted Protein Folding

P. Horowitz, G. Zardeneta, 2001 .

A fluorescence study of thermally induced conformational changes in yeast hexokinase.

Z. Wasylewski, P. Horowitz, N. Criscimagna, 1985, Biochimica et Biophysica Acta.

The hydrophobic properties of GroEL: a review of ligand effects on the modulation of GroEL hydrophobic surfaces.

P. Horowitz, B. Brazil, 1999, Cell stress & chaperones.

Constraints on the flexibility of bacteriorhodopsin's carboxyl-terminal tail at the purple membrane surface.

P. Horowitz, R. Renthal, N. Dawson, 1983, Biochemistry.

Kinetic Control of Protein Folding by Detergent Micelles, Liposomes, and Chaperonins

P. Horowitz, 1993 .

Rapid secretion by a nonclassical pathway of overexpressed mammalian mitochondrial rhodanese.

J. Chirgwin, P. Horowitz, I. Sloan, 1994, The Journal of biological chemistry.

Spectral differences between rhodanese catalytic intermediates unrelated to enzyme conformation.

P. Horowitz, S. F. Chow, 1985, The Journal of biological chemistry.

Elimination of glycerol artifacts in cycle sequencing.

J. Chirgwin, P. Horowitz, R. J. Trevino, 1993, BioTechniques.

Perturbation of Pseudomonas cytochrome oxidase by guanidine hydrochloride to detect differential stabilization of the heme d1 and heme c moieties.

P. Horowitz, B. Muhoberac, D. Wharton, 1986, Biochimica et biophysica acta.

Binding of concanavalin A to nuclei of unsynchronized and synchronized HeLa cells.

P. Horowitz, G. Michaels, P. Levin, 1977, Biochemical and biophysical research communications.