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Paul Horowitz

Research Profile

Chemicals & Drugs

Physiology

Protein Folding

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Protein Denaturation

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TOP 3
Yogeet Kaur; Paul M Horowitz
Prodan fluorescence mimics the GroEL folding cycle.
Yogeet Kaur; Jesse Ybarra; Paul M Horowitz
Active rhodanese lacking nonessential sulfhydryl groups has increased hydrophobic exposure not observed in wild-type enzyme.
Markandeswar Panda; Paul M Horowitz
Activation parameters for the spontaneous and pressure-induced phases of the dissociation of single-ring GroEL (SR1) chaperonin.

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All Publications

2004: Yogeet Kaur; Paul M Horowitz
Prodan fluorescence mimics the GroEL folding cycle.
The protein journal 2004;23(7):475-81.
2004: Yogeet Kaur; Jesse Ybarra; Paul M Horowitz
Active rhodanese lacking nonessential sulfhydryl groups has increased hydrophobic exposure not observed in wild-type enzyme.
The protein journal 2004;23(4):255-61.
2004: Markandeswar Panda; Paul M Horowitz
Activation parameters for the spontaneous and pressure-induced phases of the dissociation of single-ring GroEL (SR1) chaperonin.
The protein journal 2004;23(1):85-94.
2003: Jesse Ybarra; Anusri Mitra Bhattacharyya; Markandeswar Panda; Paul M Horowitz
Active rhodanese lacking nonessential sulfhydryl groups contains an unstable C-terminal domain and can be bound, inactivated, and reactivated by GroEL.
The Journal of biological chemistry 2003;278(3):1693-9.
2002: Markandeswar Panda; Jesse Ybarra; Paul M Horowitz
Dissociation of the single-ring chaperonin GroEL by high hydrostatic pressure.
Biochemistry 2002;41(42):12843-9.
2002: Gisela Kramer; Vasanthi Ramachandiran; Paul M Horowitz; Boyd Hardesty
The molecular chaperone DnaK is not recruited to translating ribosomes that lack trigger factor.
Archives of biochemistry and biophysics 2002;403(1):63-70.
2002: Anusri Mitra Bhattacharyya; Paul M Horowitz
Rhodanese can partially refold in its GroEL-GroES-ADP complex and can be released to give a homogeneous product.
Biochemistry 2002;41(7):2421-8.
2002: Vasanthi Ramachandiran; Gisela Kramer; Paul M Horowitz; Boyd Hardesty
Single synonymous codon substitution eliminates pausing during chloramphenicol acetyl transferase synthesis on Escherichia coli ribosomes in vitro.
FEBS letters 2002;512(1-3):209-12.
2002: Markandeswar Panda; Paul M Horowitz
Conformational heterogeneity is revealed in the dissociation of the oligomeric chaperonin GroEL by high hydrostatic pressure.
Biochemistry 2002;41(6):1869-76.
2002: Anusri Mitra Bhattacharyya; Paul M Horowitz
Isolation and characterization of rhodanese intermediates during thermal inactivation and their implications for the mechanism of protein aggregation.
Biochemistry 2002;41(1):422-9.
2001: Markandeswar Panda; A L Smoot; Paul M Horowitz
The 4,4'-dipyridyl disulfide-induced formation of GroEL monomers is cooperative and leads to increased hydrophobic exposure.
Biochemistry 2001;40(34):10402-10.
2001: Anusri Mitra Bhattacharyya; Paul M Horowitz
The aggregation state of rhodanese during folding influences the ability of GroEL to assist reactivation.
The Journal of biological chemistry 2001;276(31):28739-43.
2001: A L Smoot; Markandeswar Panda; BT Brazil; A M Buckle; Alan Fersht; Paul M Horowitz
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.
Biochemistry 2001;40(14):4484-92.
2001: Markandeswar Panda; Jesse Ybarra; Paul M Horowitz
High hydrostatic pressure can probe the effects of functionally related ligands on the quaternary structures of the chaperonins GroEL and GroES.
The Journal of biological chemistry 2001;276(9):6253-9.
2001: Gisela Kramer; Vasanthi Ramachandiran; Paul M Horowitz; Boyd Hardesty
An additional serine residue at the C terminus of rhodanese destabilizes the enzyme.
Archives of biochemistry and biophysics 2001;385(2):332-7.
2000: Markandeswar Panda; Paul M Horowitz
Active-site sulfhydryl chemistry plays a major role in the misfolding of urea-denatured rhodanese.
Journal of protein chemistry 2000;19(5):399-409.
2000: Anusri Mitra Bhattacharyya; Paul M Horowitz
Alteration around the active site of rhodanese during urea-induced denaturation and its implications for folding.
The Journal of biological chemistry 2000;275(20):14860-4.
2000: Markandeswar Panda; boris gorovits; Paul M Horowitz
Productive and nonproductive intermediates in the folding of denatured rhodanese.
The Journal of biological chemistry 2000;275(1):63-70.
1999: T Shibatani; Gisela Kramer; Boyd Hardesty; Paul M Horowitz
Domain separation precedes global unfolding of rhodanese.
The Journal of biological chemistry 1999;274(47):33795-9.
1999: BT Brazil; Paul M Horowitz
The hydrophobic properties of GroEL: a review of ligand effects on the modulation of GroEL hydrophobic surfaces.
Cell stress & chaperones 1999;4(3):177-90.
1999: R J Trevino; F Gliubich; Rodolfo Berni; Michele Cianci; JM Chirgwin; Giuseppe Zanotti; Paul M Horowitz
NH2-terminal sequence truncation decreases the stability of bovine rhodanese, minimally perturbs its crystal structure, and enhances interaction with GroEL under native conditions.
The Journal of biological chemistry 1999;274(20):13938-47.
1999: E A Jai; Paul M Horowitz
Nucleotide and Mg2+ induced conformational changes in GroEL can be detected by sulfhydryl labeling.
Journal of protein chemistry 1999;18(3):387-96.
1999: Paul M Horowitz; G H Lorimer; Jesse Ybarra
GroES in the asymmetric GroEL14-GroES7 complex exchanges via an associative mechanism.
Proceedings of the National Academy of Sciences of the United States of America 1999;96(6):2682-6.
1998: R J Trevino; T Tsalkova; Gisela Kramer; Boyd Hardesty; JM Chirgwin; Paul M Horowitz
Truncations at the NH2 terminus of rhodanese destabilize the enzyme and decrease its heterologous expression.
The Journal of biological chemistry 1998;273(43):27841-7.
1998: boris gorovits; Paul M Horowitz
High hydrostatic pressure can reverse aggregation of protein folding intermediates and facilitate acquisition of native structure.
Biochemistry 1998;37(17):6132-5.
1998: BT Brazil; Jesse Ybarra; Paul M Horowitz
Divalent cations can induce the exposure of GroEL hydrophobic surfaces and strengthen GroEL hydrophobic binding interactions. Novel effects of Zn2+ GroEL interactions.
The Journal of biological chemistry 1998;273(6):3257-63.
1998: boris gorovits; W A McGee; Paul M Horowitz
Rhodanese folding is controlled by the partitioning of its folding intermediates.
Biochimica et biophysica acta 1998;1382(1):120-8.
1998: JW Seale; BT Brazil; Paul M Horowitz
Photoincorporation of fluorescent probe into GroEL: defining site of interaction.
Methods in enzymology 1998;290():318-23.
1998: boris gorovits; Paul M Horowitz
Fluorescence anisotropy method for investigation of GroEL-GroES interaction.
Methods in enzymology 1998;290():313-7.
1997: boris gorovits; Jesse Ybarra; JW Seale; Paul M Horowitz
Conditions for nucleotide-dependent GroES-GroEL interactions. GroEL14(groES7)2 is favored by an asymmetric distribution of nucleotides.
The Journal of biological chemistry 1997;272(43):26999-7004.
1997: JW Seale; JM Chirgwin; Borries Demeler; Paul M Horowitz
Preformed GroES oligomers are not required as functional cochaperonins.
Journal of protein chemistry 1997;16(7):661-8.
1997: boris gorovits; Jesse Ybarra; Paul M Horowitz
ATP hydrolysis is critical for induction of conformational changes in GroEL that expose hydrophobic surfaces.
The Journal of biological chemistry 1997;272(11):6842-5.
1997: BT Brazil; J L Cleland; R S McDowell; Nicholas J Skelton; Ken Paris; Paul M Horowitz
Model peptide studies demonstrate that amphipathic secondary structures can be recognized by the chaperonin GroEL (cpn60).
The Journal of biological chemistry 1997;272(8):5105-11.
1997: R Narayanasami; J S Nishimura; K McMillan; Linda Roman; Thomas M Shea; A M Robida; Paul M Horowitz; Bettie Sue Masters
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.
Nitric oxide : biology and chemistry / official journal of the Nitric Oxide Society 1997;1(1):39-49.
1997: boris gorovits; Paul M Horowitz
Conditions of forming protein complexes with GroEL can influence the mechanism of chaperonin-assisted refolding.
The Journal of biological chemistry 1997;272(1):32-5.
1996: D L Gibbons; J D Hixson; N Hay; P Lund; boris gorovits; Jesse Ybarra; Paul M Horowitz
Intrinsic fluorescence studies of the chaperonin GroEL containing single Tyr --> Trp replacements reveal ligand-induced conformational changes.
The Journal of biological chemistry 1996;271(50):31989-95.
1996: Jesse Ybarra; Paul M Horowitz
Nucleotides reveal polynucleotide phosphorylase activity from conventionally purified GroEL.
The Journal of biological chemistry 1996;271(41):25063-6.
1996: J W Seale; boris gorovits; Jesse Ybarra; Paul M Horowitz
Reversible oligomerization and denaturation of the chaperonin GroES.
Biochemistry 1996;35(13):4079-83.
1996: D L Gibbons; Paul M Horowitz
Ligand-induced conformational changes in the apical domain of the chaperonin GroEL.
The Journal of biological chemistry 1996;271(1):238-43.
1995: J W Seale; Paul M Horowitz
The C-terminal sequence of the chaperonin GroES is required for oligomerization.
The Journal of biological chemistry 1995;270(51):30268-70.
1995: boris gorovits; Paul M Horowitz
The chaperonin GroEL is destabilized by binding of ADP.
The Journal of biological chemistry 1995;270(48):28551-6.
1995: boris gorovits; J W Seale; Paul M Horowitz
Residual structure in urea-denatured chaperonin GroEL.
Biochemistry 1995;34(42):13928-33.
1995: R J Trevino; J Hunt; Paul M Horowitz; John M Chirgwin
Chinese hamster rhodanese cDNA: activity of the expressed protein is not blocked by a C-terminal extension.
Protein expression and purification 1995;6(5):693-9.
1995: Jesse Ybarra; Paul M Horowitz
Inactive GroEL monomers can be isolated and reassembled to functional tetradecamers that contain few bound peptides.
The Journal of biological chemistry 1995;270(39):22962-7.
1995: G X Luo; S Hua; Paul M Horowitz
Mutation in the interdomain tether influences the stability and refolding of the enzyme rhodanese.
Biochimica et biophysica acta 1995;1252(1):165-71.
1995: Jesse Ybarra; Paul M Horowitz
Refolding and reassembly of active chaperonin GroEL after denaturation.
The Journal of biological chemistry 1995;270(38):22113-5.
1995: Subramanian Dhandayuthapani; Laura Via; C A Thomas; Paul M Horowitz; Dusanka Deretic; Vojo Deretic
Green fluorescent protein as a marker for gene expression and cell biology of mycobacterial interactions with macrophages.
Molecular microbiology 1995;17(5):901-12.
1995: Paul M Horowitz; S Hua
Rhodanese conformational changes permit oxidation to give disulfides that form in a kinetically determined sequence.
Biochimica et biophysica acta 1995;1249(2):161-7.
1995: J W Seale; Joe Martinez; Paul M Horowitz
Photoincorporation of 4,4'-bis(1-anilino-8-naphthalenesulfonic acid) into the apical domain of GroEL: specific information from a nonspecific probe.
Biochemistry 1995;34(22):7443-9.
1995: boris gorovits; Paul M Horowitz
The molecular chaperonin cpn60 displays local flexibility that is reduced after binding with an unfolded protein.
The Journal of biological chemistry 1995;270(22):13057-62.
1995: W Kudlicki; Obed W Odom; Gisela Kramer; Boyd Hardesty; G A Merrill; Paul M Horowitz
The importance of the N-terminal segment for DnaJ-mediated folding of rhodanese while bound to ribosomes as peptidyl-tRNA.
The Journal of biological chemistry 1995;270(18):10650-7.
1995: D L Gibbons; Paul M Horowitz
Exposure of hydrophobic surfaces on the chaperonin GroEL oligomer by protonation or modification of His-401.
The Journal of biological chemistry 1995;270(13):7335-40.
1995: J A Mendoza; Joe Martinez; Paul M Horowitz
Tetradecameric chaperonin 60 can be assembled in vitro from monomers in a process that is ATP independent.
Biochimica et biophysica acta 1995;1247(2):209-14.
1995: boris gorovits; C.S. Raman; Paul M Horowitz
High hydrostatic pressure induces the dissociation of cpn60 tetradecamers and reveals a plasticity of the monomers.
The Journal of biological chemistry 1995;270(5):2061-6.
1995: Paul M Horowitz; S Hua; D L Gibbons
Hydrophobic surfaces that are hidden in chaperonin Cpn60 can be exposed by formation of assembly-competent monomers or by ionic perturbation of the oligomer.
The Journal of biological chemistry 1995;270(4):1535-42.
1995: Paul M Horowitz
Chaperonin-assisted protein folding of the enzyme rhodanese by GroEL/GroES.
Methods in molecular biology (Clifton, N.J.) 1995;40():361-8.
1994: G X Luo; Paul M Horowitz
The stability of the molecular chaperonin cpn60 is affected by site-directed replacement of cysteine 518.
The Journal of biological chemistry 1994;269(51):32151-4.
1994: Gustavo Zardeneta; Paul M Horowitz
Detergent, liposome, and micelle-assisted protein refolding.
Analytical biochemistry 1994;223(1):1-6.
1994: I S Sloan; Paul M Horowitz; John M Chirgwin
Rapid secretion by a nonclassical pathway of overexpressed mammalian mitochondrial rhodanese.
The Journal of biological chemistry 1994;269(44):27625-30.
1994: george Georgiou; P Valax; M Ostermeier; Paul M Horowitz
Folding and aggregation of TEM beta-lactamase: analogies with the formation of inclusion bodies in Escherichia coli.
Protein science : a publication of the Protein Society 1994;3(11):1953-60.
1994: J A Mendoza; Paul M Horowitz
Bound substrate polypeptides can generally stabilize the tetradecameric structure of Cpn60 and induce its reassembly from monomers.
The Journal of biological chemistry 1994;269(42):25963-5.
1994: Gustavo Zardeneta; Paul M Horowitz
Protein refolding at high concentrations using detergent/phospholipid mixtures.
Analytical biochemistry 1994;218(2):392-8.
1994: D M Miller-Martini; S Hua; Paul M Horowitz
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.
The Journal of biological chemistry 1994;269(17):12414-8.
1994: G X Luo; Paul M Horowitz
The sulfurtransferase activity and structure of rhodanese are affected by site-directed replacement of Arg-186 or Lys-249.
The Journal of biological chemistry 1994;269(11):8220-5.
1994: T A Islam; D M Miller-Martini; Paul M Horowitz
Mutation of cysteine 254 facilitates the conformational changes accompanying the interconversion of persulfide-substituted and persulfide-free rhodanese.
The Journal of biological chemistry 1994;269(11):7903-13.
1994: D M Miller-Martini; John M Chirgwin; Paul M Horowitz
Mutations of noncatalytic sulfhydryl groups influence the stability, folding, and oxidative susceptibility of rhodanese.
The Journal of biological chemistry 1994;269(5):3423-8.
1994: J A Mendoza; Borries Demeler; Paul M Horowitz
Alteration of the quaternary structure of cpn60 modulates chaperonin-assisted folding. Implications for the mechanism of chaperonin action.
The Journal of biological chemistry 1994;269(4):2447-51.
1994: J A Mendoza; Paul M Horowitz
The chaperonin assisted and unassisted refolding of rhodanese can be modulated by its N-terminal peptide.
Journal of protein chemistry 1994;13(1):15-22.
1993: Gustavo Zardeneta; Paul M Horowitz
Physical characterization of a reactivatable liposome-bound rhodanese folding intermediate.
Biochemistry 1993;32(50):13941-8.
1993: R J Trevino; Paul M Horowitz; John M Chirgwin
Elimination of glycerol artifacts in cycle sequencing.
BioTechniques 1993;15(3):366-8.
1993: J M Dungan; Paul M Horowitz
Thermally perturbed rhodanese can be protected from inactivation by self-association.
Journal of protein chemistry 1993;12(3):311-21.
1993: G X Luo; Paul M Horowitz
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.
The Journal of biological chemistry 1993;268(14):10246-51.
1993: T Tsalkova; G Zardeneta; W Kudlicki; Gisela Kramer; Paul M Horowitz; Boyd Hardesty
GroEL and GroES increase the specific enzymatic activity of newly-synthesized rhodanese if present during in vitro transcription/translation.
Biochemistry 1993;32(13):3377-80.
1993: Paul M Horowitz; M Butler
Interactive intermediates are formed during the urea unfolding of rhodanese.
The Journal of biological chemistry 1993;268(4):2500-4.
1993: J A Mendoza; E Grant; Paul M Horowitz
Partially folded rhodanese or its N-terminal sequence can disrupt phospholipid vesicles.
Journal of protein chemistry 1993;12(1):65-9.
1992: Gustavo Zardeneta; Paul M Horowitz
Cardiolipin liposomes sequester a reactivatable partially folded rhodanese intermediate.
European journal of biochemistry / FEBS 1992;210(3):831-7.
1992: Gustavo Zardeneta; Paul M Horowitz
Analysis of the perturbation of phospholipid model membranes by rhodanese and its presequence.
The Journal of biological chemistry 1992;267(34):24193-8.
1992: J A Mendoza; M C Butler; Paul M Horowitz
Characterization of a stable, reactivatable complex between chaperonin 60 and mitochondrial rhodanese.
The Journal of biological chemistry 1992;267(34):24648-54.
1992: J A Mendoza; Paul M Horowitz
Sulfhydryl modification of E. coli Cpn60 leads to loss of its ability to support refolding of rhodanese but not to form a binary complex.
Journal of protein chemistry 1992;11(6):589-94.
1992: Paul M Horowitz; M Butler; G D McClure
Reducing sugars can induce the oxidative inactivation of rhodanese.
The Journal of biological chemistry 1992;267(33):23596-600.
1992: Lee-Chuan C Yeh; Paul M Horowitz; John C Lee
Yeast 5S rRNA binding to ribosomal protein L1a alters the fluorescence of tryptophan residues lying outside the binding site.
Biochimie 1992;74(11):1025-30.
1992: Paul M Horowitz; R Xu
Acid pH-induced conformational changes in bovine liver rhodanese.
The Journal of biological chemistry 1992;267(27):19464-9.
1992: J A Mendoza; G H Lorimer; Paul M Horowitz
Chaperonin cpn60 from Escherichia coli protects the mitochondrial enzyme rhodanese against heat inactivation and supports folding at elevated temperatures.
The Journal of biological chemistry 1992;267(25):17631-4.
1992: D M Miller; G P Kurzban; J A Mendoza; John M Chirgwin; Stephen Hardies; Paul M Horowitz
Recombinant bovine rhodanese: purification and comparison with bovine liver rhodanese.
Biochimica et biophysica acta 1992;1121(3):286-92.
1992: Gustavo Zardeneta; Paul M Horowitz
Micelle-assisted protein folding. Denatured rhodanese binding to cardiolipin-containing lauryl maltoside micelles results in slower refolding kinetics but greater enzyme reactivation.
The Journal of biological chemistry 1992;267(9):5811-6.
1992: John C Lee; Paul M Horowitz
Sulfhydryl groups on yeast ribosomal proteins L7 and L26 are significantly more reactive in the 80 S particles than in the 60 S subunits.
The Journal of biological chemistry 1992;267(4):2502-6.
1991: G P Kurzban; Paul M Horowitz
Purification of bovine liver rhodanese by low-pH column chromatography.
Protein expression and purification 1991;2(5-6):379-84.
1991: J A Mendoza; G H Lorimer; Paul M Horowitz
Intermediates in the chaperonin-assisted refolding of rhodanese are trapped at low temperature and show a small stoichiometry.
The Journal of biological chemistry 1991;266(26):16973-6.
1991: John C Lee; Lee-Chuan C Yeh; Paul M Horowitz
The initiation codon AUG binds at a hydrophobic site on yeast 40S ribosomal subunits as revealed by fluorescence studies with bis (1,8-anilinonaphthalenesulfonate).
Biochimie 1991;73(9):1245-7.
1991: G P Kurzban; E A Bayer; M Wilchek; Paul M Horowitz
The quaternary structure of streptavidin in urea.
The Journal of biological chemistry 1991;266(22):14470-7.
1991: J A Mendoza; E Rogers; G H Lorimer; Paul M Horowitz
Unassisted refolding of urea unfolded rhodanese.
The Journal of biological chemistry 1991;266(21):13587-91.
1991: J A Mendoza; E Rogers; G H Lorimer; Paul M Horowitz
Chaperonins facilitate the in vitro folding of monomeric mitochondrial rhodanese.
The Journal of biological chemistry 1991;266(20):13044-9.
1991: D M Miller; R Delgado; John M Chirgwin; Stephen Hardies; Paul M Horowitz
Expression of cloned bovine adrenal rhodanese.
The Journal of biological chemistry 1991;266(8):4686-91.
1990: G P Kurzban; G Gitlin; E A Bayer; M Wilchek; Paul M Horowitz
Biotin binding changes the conformation and decreases tryptophan accessibility of streptavidin.
Journal of protein chemistry 1990;9(6):673-82.
1990: S Tandon; Paul M Horowitz
The detection of kinetic intermediate(s) during refolding of rhodanese.
The Journal of biological chemistry 1990;265(11):5967-70.
1990: B A Aird; Paul M Horowitz
A physical characterization of sulfane sulfurtransferase.
Biochimica et biophysica acta 1990;1038(1):10-7.
1990: Paul M Horowitz; N L Criscimagna
Stable intermediates can be trapped during the reversible refolding of urea-denatured rhodanese.
The Journal of biological chemistry 1990;265(5):2576-83.
1990: J S Nishimura; C J Mann; Jesse Ybarra; T Mitchell; Paul M Horowitz
Intrinsic fluorescence of succinyl-CoA synthetase and four tryptophan mutants. Tryptophan 76 and tryptophan 248 of the beta-subunit are responsive to CoA binding.
Biochemistry 1990;29(4):862-5.
1989: G P Kurzban; G Gitlin; E A Bayer; M Wilchek; Paul M Horowitz
Shielding of tryptophan residues of avidin by the binding of biotin.
Biochemistry 1989;28(21):8537-42.
1989: S Tandon; Paul M Horowitz
Reversible folding of rhodanese. Presence of intermediate(s) at equilibrium.
The Journal of biological chemistry 1989;264(17):9859-66.
1989: Paul M Horowitz; S Bowman
Oxidative inactivation of rhodanese by hydrogen peroxide produces states that show differential reactivation.
The Journal of biological chemistry 1989;264(6):3311-6.
1989: R J King; D Simon; Paul M Horowitz
Aspects of secondary and quaternary structure of surfactant protein A from canine lung.
Biochimica et biophysica acta 1989;1001(3):294-301.
1988: G A Merrill; Paul M Horowitz; S Bowman; K Bentley; RJ Klebe
Detection of time-dependent and oxidatively induced antigens of bovine liver rhodanese with monoclonal antibodies.
The Journal of biological chemistry 1988;263(36):19324-30.
1988: Lee-Chuan C Yeh; Paul M Horowitz; John C Lee
Studies of RNA-protein interactions in the yeast 5 S ribonucleoprotein particles by fluorescence and tritium exchange. Implications for ribosomal assembly.
The Journal of biological chemistry 1988;263(33):17412-7.
1988: B A Aird; Paul M Horowitz
Acceptor substrate-potentiated inactivation of bovine liver rhodanese.
The Journal of biological chemistry 1988;263(30):15270-6.
1988: B A Aird; Paul M Horowitz
The differential functional stability of various forms of bovine liver rhodanese.
Biochimica et biophysica acta 1988;956(1):30-8.
1988: Paul M Horowitz; N L Criscimagna
Sulfhydryl-directed triggering of conformational changes in the enzyme rhodanese.
The Journal of biological chemistry 1988;263(21):10278-83.
1988: S Tandon; Paul M Horowitz
The effects of lauryl maltoside on the reactivation of several enzymes after treatment with guanidinium chloride.
Biochimica et biophysica acta 1988;955(1):19-25.
1988: J S Nishimura; Jesse Ybarra; T Mitchell; Paul M Horowitz
Isolation, amino acid analyses and refolding of subunits of pig heart succinyl-CoA synthetase.
The Biochemical journal 1988;250(2):429-34.
1987: Paul M Horowitz; S Bowman
Oxidation increases the proteolytic susceptibility of a localized region in rhodanese.
The Journal of biological chemistry 1987;262(30):14544-8.
1987: Paul M Horowitz; S Bowman
Ion-enhanced fluorescence staining of sodium dodecyl sulfate-polyacrylamide gels using bis(8-p-toluidino-1-naphthalenesulfonate).
Analytical biochemistry 1987;165(2):430-4.
1986: S Tandon; Paul M Horowitz
Detergent-assisted refolding of guanidinium chloride-denatured rhodanese. The effect of lauryl maltoside.
The Journal of biological chemistry 1986;261(33):15615-8.