| Year |
Citation |
Score |
| 2004 |
Kaur Y, Horowitz PM. Prodan fluorescence mimics the GroEL folding cycle. The Protein Journal. 23: 475-81. PMID 15635940 DOI: 10.1007/S10930-004-5224-Z |
0.386 |
|
| 2004 |
Kaur Y, Ybarra J, Horowitz PM. Active rhodanese lacking nonessential sulfhydryl groups has increased hydrophobic exposure not observed in wild-type enzyme. The Protein Journal. 23: 255-61. PMID 15214496 DOI: 10.1023/B:Jopc.0000027850.01893.2E |
0.387 |
|
| 2003 |
Ybarra J, Bhattacharyya AM, Panda M, Horowitz PM. 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. 278: 1693-9. PMID 12433928 DOI: 10.1074/Jbc.M207574200 |
0.343 |
|
| 2002 |
Kramer G, Ramachandiran V, Horowitz PM, Hardesty B. The molecular chaperone DnaK is not recruited to translating ribosomes that lack trigger factor. Archives of Biochemistry and Biophysics. 403: 63-70. PMID 12061803 DOI: 10.1016/S0003-9861(02)00213-8 |
0.329 |
|
| 2002 |
Ramachandiran V, Kramer G, Horowitz PM, Hardesty B. Single synonymous codon substitution eliminates pausing during chloramphenicol acetyl transferase synthesis on Escherichia coli ribosomes in vitro. Febs Letters. 512: 209-12. PMID 11852081 DOI: 10.1016/S0014-5793(02)02261-5 |
0.31 |
|
| 2002 |
Bhattacharyya AM, Horowitz PM. Rhodanese can partially refold in its GroEL-GroES-ADP complex and can be released to give a homogeneous product. Biochemistry. 41: 2421-8. PMID 11841236 DOI: 10.1021/Bi0115378 |
0.413 |
|
| 2002 |
Panda M, Horowitz PM. Conformational heterogeneity is revealed in the dissociation of the oligomeric chaperonin GroEL by high hydrostatic pressure. Biochemistry. 41: 1869-76. PMID 11827532 DOI: 10.1021/Bi011794C |
0.31 |
|
| 2002 |
Bhattacharyya AM, Horowitz PM. Isolation and characterization of rhodanese intermediates during thermal inactivation and their implications for the mechanism of protein aggregation. Biochemistry. 41: 422-9. PMID 11772042 DOI: 10.1021/Bi011726Q |
0.41 |
|
| 2001 |
Panda M, Smoot AL, Horowitz PM. The 4,4'-dipyridyl disulfide-induced formation of GroEL monomers is cooperative and leads to increased hydrophobic exposure. Biochemistry. 40: 10402-10. PMID 11513619 DOI: 10.1021/Bi010831X |
0.388 |
|
| 2001 |
Bhattacharyya AM, Horowitz PM. The aggregation state of rhodanese during folding influences the ability of GroEL to assist reactivation. The Journal of Biological Chemistry. 276: 28739-43. PMID 11397797 DOI: 10.1074/Jbc.M102500200 |
0.404 |
|
| 2001 |
Kramer G, Ramachandiran V, Horowitz P, Hardesty B. An additional serine residue at the C terminus of rhodanese destabilizes the enzyme. Archives of Biochemistry and Biophysics. 385: 332-7. PMID 11368014 DOI: 10.1006/Abbi.2000.2166 |
0.403 |
|
| 2001 |
Smoot AL, Panda M, Brazil BT, Buckle AM, Fersht AR, Horowitz PM. 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. 40: 4484-92. PMID 11284705 DOI: 10.1021/Bi001822B |
0.396 |
|
| 2001 |
Panda M, Ybarra J, Horowitz PM. 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. 276: 6253-9. PMID 11085994 DOI: 10.1074/Jbc.M009530200 |
0.335 |
|
| 2000 |
Panda M, Horowitz PM. Active-site sulfhydryl chemistry plays a major role in the misfolding of urea-denatured rhodanese. Journal of Protein Chemistry. 19: 399-409. PMID 11131146 DOI: 10.1023/A:1026491615076 |
0.413 |
|
| 2000 |
Bhattacharyya AM, Horowitz P. Alteration around the active site of rhodanese during urea-induced denaturation and its implications for folding. The Journal of Biological Chemistry. 275: 14860-4. PMID 10809729 DOI: 10.1074/Jbc.275.20.14860 |
0.454 |
|
| 2000 |
Nandi DL, Horowitz PM, Westley J. Rhodanese as a thioredoxin oxidase. The International Journal of Biochemistry & Cell Biology. 32: 465-73. PMID 10762072 DOI: 10.1016/S1357-2725(99)00035-7 |
0.353 |
|
| 2000 |
Panda M, Gorovits BM, Horowitz PM. Productive and nonproductive intermediates in the folding of denatured rhodanese. The Journal of Biological Chemistry. 275: 63-70. PMID 10617586 DOI: 10.1074/Jbc.275.1.63 |
0.358 |
|
| 1999 |
Shibatani T, Kramer G, Hardesty B, Horowitz PM. Domain separation precedes global unfolding of rhodanese. The Journal of Biological Chemistry. 274: 33795-9. PMID 10559274 DOI: 10.1074/Jbc.274.47.33795 |
0.366 |
|
| 1999 |
Jai EA, Horowitz PM. Nucleotide and Mg2+ induced conformational changes in GroEL can be detected by sulfhydryl labeling. Journal of Protein Chemistry. 18: 387-96. PMID 10395457 DOI: 10.1023/A:1021055932648 |
0.38 |
|
| 1999 |
Trevino RJ, Gliubich F, Berni R, Cianci M, Chirgwin JM, Zanotti G, Horowitz PM. 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. 274: 13938-47. PMID 10318804 DOI: 10.1074/Jbc.274.20.13938 |
0.404 |
|
| 1999 |
Horowitz PM, Lorimer GH, Ybarra J. 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. 96: 2682-2686. PMID 10077571 DOI: 10.1073/Pnas.96.6.2682 |
0.31 |
|
| 1998 |
Trevino RJ, Tsalkova T, Kramer G, Hardesty B, Chirgwin JM, Horowitz PM. Truncations at the NH2 terminus of rhodanese destabilize the enzyme and decrease its heterologous expression. The Journal of Biological Chemistry. 273: 27841-7. PMID 9774394 DOI: 10.1074/Jbc.273.43.27841 |
0.394 |
|
| 1998 |
Gorovits BM, Horowitz PM. High hydrostatic pressure can reverse aggregation of protein folding intermediates and facilitate acquisition of native structure. Biochemistry. 37: 6132-5. PMID 9558352 DOI: 10.1021/Bi9730137 |
0.344 |
|
| 1998 |
Seale JW, Brazil BT, Horowitz PM. Photoincorporation of fluorescent probe into GroEL: defining site of interaction. Methods in Enzymology. 290: 318-23. PMID 9534172 DOI: 10.1016/S0076-6879(98)90028-3 |
0.395 |
|
| 1998 |
Gorovits BM, Horowitz PM. Fluorescence anisotropy method for investigation of GroEL-GroES interaction. Methods in Enzymology. 290: 313-7. PMID 9534171 DOI: 10.1016/S0076-6879(98)90027-1 |
0.384 |
|
| 1998 |
Gorovits BM, McGee WA, Horowitz PM. Rhodanese folding is controlled by the partitioning of its folding intermediates. Biochimica Et Biophysica Acta. 1382: 120-8. PMID 9507086 DOI: 10.1016/S0167-4838(97)00158-1 |
0.448 |
|
| 1998 |
Brazil BT, Ybarra J, Horowitz PM. 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. 273: 3257-63. PMID 9452440 DOI: 10.1074/Jbc.273.6.3257 |
0.393 |
|
| 1997 |
Narayanasami R, Nishimura JS, McMillan K, Roman LJ, Shea TM, Robida AM, Horowitz PM, Masters BS. 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. 1: 39-49. PMID 9701043 DOI: 10.1006/Niox.1996.0103 |
0.401 |
|
| 1997 |
Gorovits BM, Ybarra J, Seale JW, Horowitz PM. Conditions for nucleotide-dependent GroES-GroEL interactions. GroEL14(groES7)2 is favored by an asymmetric distribution of nucleotides. The Journal of Biological Chemistry. 272: 26999-7004. PMID 9341138 DOI: 10.1074/Jbc.272.43.26999 |
0.436 |
|
| 1997 |
Seale JW, Chirgwin JM, Demeler B, Horowitz PM. Preformed GroES oligomers are not required as functional cochaperonins. Journal of Protein Chemistry. 16: 661-8. PMID 9330224 DOI: 10.1023/A:1026350303043 |
0.338 |
|
| 1997 |
Gorovits BM, Ybarra J, Horowitz PM. ATP hydrolysis is critical for induction of conformational changes in GroEL that expose hydrophobic surfaces. The Journal of Biological Chemistry. 272: 6842-5. PMID 9054367 DOI: 10.1074/Jbc.272.11.6842 |
0.398 |
|
| 1997 |
Brazil BT, Cleland JL, McDowell RS, Skelton NJ, Paris K, Horowitz PM. Model peptide studies demonstrate that amphipathic secondary structures can be recognized by the chaperonin GroEL (cpn60). The Journal of Biological Chemistry. 272: 5105-11. PMID 9030576 DOI: 10.1074/Jbc.272.8.5105 |
0.341 |
|
| 1997 |
Gorovits BM, Horowitz PM. Conditions of forming protein complexes with GroEL can influence the mechanism of chaperonin-assisted refolding. The Journal of Biological Chemistry. 272: 32-5. PMID 8995221 DOI: 10.1074/Jbc.272.1.32 |
0.449 |
|
| 1996 |
Gibbons DL, Hixson JD, Hay N, Lund P, Gorovits BM, Ybarra J, Horowitz PM. Intrinsic fluorescence studies of the chaperonin GroEL containing single Tyr --> Trp replacements reveal ligand-induced conformational changes. The Journal of Biological Chemistry. 271: 31989-95. PMID 8943246 DOI: 10.1074/Jbc.271.50.31989 |
0.418 |
|
| 1996 |
Ybarra J, Horowitz PM. Nucleotides reveal polynucleotide phosphorylase activity from conventionally purified GroEL. The Journal of Biological Chemistry. 271: 25063-6. PMID 8810258 DOI: 10.1074/Jbc.271.41.25063 |
0.354 |
|
| 1996 |
Seale JW, Gorovits BM, Ybarra J, Horowitz PM. Reversible oligomerization and denaturation of the chaperonin GroES. Biochemistry. 35: 4079-83. PMID 8672442 DOI: 10.1021/Bi953087N |
0.43 |
|
| 1996 |
Gibbons DL, Horowitz PM. Ligand-induced conformational changes in the apical domain of the chaperonin GroEL. The Journal of Biological Chemistry. 271: 238-43. PMID 8550566 DOI: 10.1074/Jbc.271.1.238 |
0.383 |
|
| 1995 |
Trevino RJ, Hunt J, Horowitz PM, Chirgwin JM. Chinese hamster rhodanese cDNA: activity of the expressed protein is not blocked by a C-terminal extension. Protein Expression and Purification. 6: 693-9. PMID 8535164 DOI: 10.1006/Prep.1995.1091 |
0.415 |
|
| 1995 |
Seale JW, Horowitz PM. The C-terminal sequence of the chaperonin GroES is required for oligomerization. The Journal of Biological Chemistry. 270: 30268-70. PMID 8530444 DOI: 10.1074/Jbc.270.51.30268 |
0.339 |
|
| 1995 |
Narayanasami R, Horowitz PM, Masters BS. Flavin-binding and protein structural integrity studies on NADPH-cytochrome P450 reductase are consistent with the presence of distinct domains. Archives of Biochemistry and Biophysics. 316: 267-74. PMID 7840627 DOI: 10.1006/Abbi.1995.1037 |
0.433 |
|
| 1995 |
Gorovits B, Raman CS, Horowitz PM. High hydrostatic pressure induces the dissociation of cpn60 tetradecamers and reveals a plasticity of the monomers. The Journal of Biological Chemistry. 270: 2061-6. PMID 7836434 DOI: 10.1074/Jbc.270.5.2061 |
0.355 |
|
| 1995 |
Horowitz PM, Hua S, Gibbons DL. 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. 270: 1535-42. PMID 7829481 DOI: 10.1074/Jbc.270.4.1535 |
0.44 |
|
| 1995 |
Seale JW, Martinez JL, Horowitz PM. Photoincorporation of 4,4'-bis(1-anilino-8-naphthalenesulfonic acid) into the apical domain of GroEL: specific information from a nonspecific probe. Biochemistry. 34: 7443-9. PMID 7779787 DOI: 10.1021/Bi00022A018 |
0.415 |
|
| 1995 |
Gorovits BM, Horowitz PM. The molecular chaperonin cpn60 displays local flexibility that is reduced after binding with an unfolded protein. The Journal of Biological Chemistry. 270: 13057-62. PMID 7768899 DOI: 10.1074/Jbc.270.22.13057 |
0.384 |
|
| 1995 |
Kudlicki W, Odom OW, Kramer G, Hardesty B, Merrill GA, Horowitz PM. 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. 270: 10650-7. PMID 7738002 DOI: 10.1074/Jbc.270.18.10650 |
0.361 |
|
| 1995 |
Gibbons DL, Horowitz PM. Exposure of hydrophobic surfaces on the chaperonin GroEL oligomer by protonation or modification of His-401. The Journal of Biological Chemistry. 270: 7335-40. PMID 7706275 DOI: 10.1074/Jbc.270.13.7335 |
0.429 |
|
| 1995 |
Mendoza JA, Martinez JL, Horowitz PM. Tetradecameric chaperonin 60 can be assembled in vitro from monomers in a process that is ATP independent. Biochimica Et Biophysica Acta. 1247: 209-14. PMID 7696310 DOI: 10.1016/0167-4838(94)00231-5 |
0.324 |
|
| 1995 |
Ybarra J, Horowitz PM. Refolding and reassembly of active chaperonin GroEL after denaturation. The Journal of Biological Chemistry. 270: 22113-5. PMID 7673187 DOI: 10.1074/Jbc.270.38.22113 |
0.415 |
|
| 1995 |
Horowitz PM. Chaperonin-assisted protein folding of the enzyme rhodanese by GroEL/GroES. Methods in Molecular Biology (Clifton, N.J.). 40: 361-8. PMID 7633531 DOI: 10.1385/0-89603-301-5:361 |
0.399 |
|
| 1995 |
Horowitz PM, Hua S. Rhodanese conformational changes permit oxidation to give disulfides that form in a kinetically determined sequence. Biochimica Et Biophysica Acta. 1249: 161-7. PMID 7599169 DOI: 10.1016/0167-4838(95)00037-U |
0.396 |
|
| 1995 |
Gorovits BM, Seale JW, Horowitz PM. Residual structure in urea-denatured chaperonin GroEL. Biochemistry. 34: 13928-33. PMID 7577988 DOI: 10.1021/Bi00042A026 |
0.422 |
|
| 1995 |
Ybarra J, Horowitz PM. Inactive GroEL monomers can be isolated and reassembled to functional tetradecamers that contain few bound peptides. The Journal of Biological Chemistry. 270: 22962-7. PMID 7559433 DOI: 10.1074/Jbc.270.39.22962 |
0.422 |
|
| 1995 |
Luo GX, Hua S, Horowitz PM. Mutation in the interdomain tether influences the stability and refolding of the enzyme rhodanese. Biochimica Et Biophysica Acta. 1252: 165-71. PMID 7548160 DOI: 10.1016/0167-4838(95)00131-D |
0.393 |
|
| 1995 |
Gorovits BM, Horowitz PM. The chaperonin GroEL is destabilized by binding of ADP. The Journal of Biological Chemistry. 270: 28551-6. PMID 7499369 DOI: 10.1074/Jbc.270.48.28551 |
0.45 |
|
| 1994 |
Zardeneta G, Horowitz PM. Protein refolding at high concentrations using detergent/phospholipid mixtures. Analytical Biochemistry. 218: 392-8. PMID 8074298 DOI: 10.1006/Abio.1994.1197 |
0.411 |
|
| 1994 |
Mendoza JA, Horowitz PM. The chaperonin assisted and unassisted refolding of rhodanese can be modulated by its N-terminal peptide Journal of Protein Chemistry. 13: 15-22. PMID 8011067 DOI: 10.1007/Bf01891988 |
0.344 |
|
| 1994 |
Georgiou G, Valax P, Ostermeier M, Horowitz PM. 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. 3: 1953-60. PMID 7703842 DOI: 10.1002/Pro.5560031107 |
0.374 |
|
| 1994 |
Zardeneta G, Horowitz PM. Detergent, liposome, and micelle-assisted protein refolding. Analytical Biochemistry. 223: 1-6. PMID 7695083 DOI: 10.1006/Abio.1994.1537 |
0.324 |
|
| 1993 |
Jarabak R, Westley J, Dungan JM, Horowitz P. A chaperone-mimetic effect of serum albumin on rhodanese. Journal of Biochemical Toxicology. 8: 41-48. PMID 8492302 DOI: 10.1002/Jbt.2570080107 |
0.334 |
|
| 1993 |
Mendoza JA, Grant E, Horowitz PM. Partially folded rhodanese or its N-terminal sequence can disrupt phospholipid vesicles Journal of Protein Chemistry. 12: 65-69. PMID 8427635 DOI: 10.1007/Bf01024916 |
0.367 |
|
| 1993 |
Dungan JM, Horowitz PM. Thermally perturbed rhodanese can be protected from inactivation by self-association Journal of Protein Chemistry. 12: 311-321. PMID 8397789 DOI: 10.1007/Bf01028193 |
0.41 |
|
| 1993 |
Zardeneta G, Horowitz PM. Physical characterization of a reactivatable liposome-bound rhodanese folding intermediate Biochemistry. 32: 13941-13948. PMID 8268170 DOI: 10.1021/bi00213a025 |
0.372 |
|
| 1993 |
Tsalkova T, Zardeneta G, Kudlicki W, Kramer G, Horowitz PM, Hardesty B. GroEL and GroES increase the specific enzymatic activity of newly-synthesized rhodanese if present during in vitro transcription/translation. Biochemistry. 32: 3377-80. PMID 8096394 DOI: 10.1021/Bi00064A022 |
0.376 |
|
| 1992 |
Miller DM, Kurzban GP, Mendoza JA, Chirgwin JM, Hardies SC, Horowitz PM. Recombinant bovine rhodanese: purification and comparison with bovine liver rhodanese Biochimica Et Biophysica Acta (Bba)/Protein Structure and Molecular. 1121: 286-292. PMID 1627606 DOI: 10.1016/0167-4838(92)90158-A |
0.426 |
|
| 1992 |
Zardeneta G, Horowitz PM. Cardiolipin liposomes sequester a reactivatable partially folded rhodanese intermediate European Journal of Biochemistry. 210: 831-837. PMID 1483467 DOI: 10.1111/J.1432-1033.1992.Tb17486.X |
0.467 |
|
| 1992 |
Yeh LCC, Horowitz PM, Lee JC. Yeast 5S rRNA binding to ribosomal protein L1a alters the fluorescence of tryptophan residues lying outside the binding site Biochimie. 74: 1025-1030. PMID 1477137 DOI: 10.1016/0300-9084(92)90023-8 |
0.387 |
|
| 1992 |
Merrill GA, Miller D, Chirgwin J, Horowitz PM. Immunological evidence for a conformational difference between recombinant bovine rhodanese and rhodanese purified from bovine liver Journal of Protein Chemistry. 11: 193-199. PMID 1382437 DOI: 10.1007/Bf01025225 |
0.377 |
|
| 1992 |
Mendoza JA, Horowitz PM. 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. 11: 589-594. PMID 1361328 DOI: 10.1007/Bf01024958 |
0.394 |
|
| 1992 |
Zardeneta G, Horowitz P. Micelle-assisted protein folding. Denatured rhodanese binding to cardiolipin-containing lauryl maltoside micelles results in slower refolding kinetics but greater enzyme reactivation. Journal of Biological Chemistry. 267: 5811-5816. DOI: 10.1016/s0021-9258(18)42625-7 |
0.368 |
|
| 1991 |
Kurzban GP, Horowitz PM. Purification of bovine liver rhodanese by low-pH column chromatography Protein Expression and Purification. 2: 379-384. PMID 1821812 DOI: 10.1016/1046-5928(91)90097-3 |
0.314 |
|
| 1991 |
Lee JC, Yeh LCC, Horowitz PM. 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. 73: 1245-1247. PMID 1747389 DOI: 10.1016/0300-9084(91)90010-X |
0.41 |
|
| 1990 |
Mock DM, Horowitz P. Fluorometric assay for avidin-biotin interaction Methods in Enzymology. 184: 234-240. PMID 2388573 DOI: 10.1016/0076-6879(90)84279-P |
0.387 |
|
| 1990 |
Nishimura JS, Mann CJ, Ybarra J, Mitchell T, Horowitz PM. Intrinsic fluorescence of succinyl-CoA synthetase and four tryptophan mutants. Tryptophan 76 and tryptophan 248 of the β-subunit are responsive to CoA binding Biochemistry. 29: 862-865. PMID 2340278 DOI: 10.1021/Bi00456A002 |
0.329 |
|
| 1990 |
Aird BA, Horowitz PM. A physical characterization of sulfane sulfurtransferase Biochimica Et Biophysica Acta (Bba)/Protein Structure and Molecular. 1038: 10-17. PMID 2317511 DOI: 10.1016/0167-4838(90)90003-X |
0.43 |
|
| 1990 |
Kurzban GP, Gitlin G, Bayer EA, Wilchek M, Horowitz PM. Biotin binding changes the conformation and decreases tryptophan accessibility of streptavidin Journal of Protein Chemistry. 9: 673-682. PMID 2073320 DOI: 10.1007/Bf01024762 |
0.394 |
|
| 1989 |
King RJ, Simon D, Horowitz PM. Aspects of secondary and quaternary structure of surfactant protein A from canine lung. Biochimica Et Biophysica Acta. 1001: 294-301. PMID 2917154 DOI: 10.1016/0005-2760(89)90114-8 |
0.349 |
|
| 1989 |
Kurzban GP, Gitlin G, Bayer EA, Wilchek M, Horowitz PM. Shielding of tryptophan residues of avidin by the binding of biotin Biochemistry. 28: 8537-8542. PMID 2605203 DOI: 10.1021/Bi00447A040 |
0.392 |
|
| 1988 |
Mock DM, Lankford G, Horowitz P. A study of the interaction of avidin with 2-anilinonaphthalene-6-sulfonic acid as a probe of the biotin binding site Biochimica Et Biophysica Acta (Bba)/Protein Structure and Molecular. 956: 23-29. PMID 3408737 DOI: 10.1016/0167-4838(88)90293-2 |
0.379 |
|
| 1988 |
Tandon S, Horowitz P. The effects of lauryl maltoside on the reactivation of several enzymes after treatment with guanidinium chloride. Biochimica Et Biophysica Acta. 955: 19-25. PMID 3382670 DOI: 10.1016/0167-4838(88)90175-6 |
0.413 |
|
| 1988 |
Nishimura JS, Ybarra J, Mitchell T, Horowitz PM. Isolation, amino acid analyses and refolding of subunits of pig heart succinyl-CoA synthetase Biochemical Journal. 250: 429-434. PMID 3281664 DOI: 10.1042/Bj2500429 |
0.4 |
|
| 1988 |
Aird BA, Horowitz PM. The differential functional stability of various forms of bovine liver rhodanese Biochimica Et Biophysica Acta (Bba)/Protein Structure and Molecular. 956: 30-38. PMID 3165676 DOI: 10.1016/0167-4838(88)90294-4 |
0.418 |
|
| 1987 |
Prasad ARS, Prasad V, Ludueña RF, Horowitz PM. Interaction of tubulin with the macromolecular apolar probe, octyl sepharose Biochemical and Biophysical Research Communications. 145: 949-955. PMID 3593381 DOI: 10.1016/0006-291X(87)91057-6 |
0.366 |
|
| 1987 |
Lee JC, Horowitz P. Tritium exchange kinetics of yeast ribosomal subunits. Biochimica Et Biophysica Acta. 908: 109-112. PMID 3545296 DOI: 10.1016/0167-4781(87)90049-2 |
0.305 |
|
| 1987 |
Prasad ARS, Horowitz PM. Chemical modification of bovine liver rhodanese with tetrathionate: differential effects or the sulfur-free and sulfur-containing catalytic intermediates Biochimica Et Biophysica Acta (Bba)/Protein Structure and Molecular. 911: 102-108. PMID 3466649 DOI: 10.1016/0167-4838(87)90275-5 |
0.438 |
|
| 1987 |
Horowitz PM, Bowman S. Ion-enhanced fluorescence staining of sodium dodecyl sulfate-polyacrylamide gels using bis(8-p-toluidino-1-naphthalenesulfonate) Analytical Biochemistry. 165: 430-434. PMID 3425913 DOI: 10.1016/0003-2697(87)90292-2 |
0.361 |
|
| 1986 |
Mock DM, Langford G, Dubois D, Criscimagna N, Horowitz P. A fluorometric assay for the biotin-avidin interaction based on displacement of the fluorescent probe 2-anilinonaphthalene-6-sulfonic acid. Analytical Biochemistry. 151: 178-81. PMID 4091277 DOI: 10.1016/0003-2697(85)90068-5 |
0.416 |
|
| 1986 |
Prasad ARS, Luduena RF, Horowitz PM. Bis(8-anilinonaphthalene-1-sulfonate) as a probe for tubulin decay Biochemistry. 25: 739-742. PMID 3955027 DOI: 10.1021/Bi00351A035 |
0.386 |
|
| 1986 |
King RJ, Phillips MC, Horowitz PM, Dang SC. Interaction between the 35 kDa apolipoprotein of pulmonary surfactant and saturated phosphatidylcholines. Effects of temperature. Biochimica Et Biophysica Acta. 879: 1-13. PMID 3768381 DOI: 10.1016/0005-2760(86)90259-6 |
0.351 |
|
| 1986 |
Prasad ARS, Luduena RF, Horowitz PM. 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 Biochemistry. 25: 3536-3540. PMID 3718942 DOI: 10.1021/Bi00360A010 |
0.408 |
|
| 1986 |
Luduena RF, Roach MC, Horowitz P. The effects of the anilinonaphthalenesulfonates on the alkylation of tubulin: correlation between the appearance of sulfhydryl groups and apolar binding sites Biochimica Et Biophysica Acta (Bba)/Protein Structure and Molecular. 873: 143-146. PMID 3509976 DOI: 10.1016/0167-4838(86)90200-1 |
0.34 |
|
| 1986 |
Horowitz P, Muhobereac BB, Falksen K, Wharton DC. Perturbation of Pseudomonas cytochrome oxidase by guanidine hydrochloride to detec differential stabilization of the heme d1 and heme c moieties Biochimica Et Biophysica Acta. 871: 142-148. PMID 3011097 DOI: 10.1016/0167-4838(86)90167-6 |
0.357 |
|
| 1986 |
Hill BC, Horowitz PM, Robinson NC. Detection, characterization, and quenching of the intrinsic fluorescence of bovine heart cytochrome c oxidase Biochemistry. 25: 2287-2292. PMID 3011084 DOI: 10.1021/Bi00356A065 |
0.411 |
|
| 1985 |
Horowitz PM. Rapid fluorescamine based protein assay usable in the presence of interfering substances Journal of Chromatography A. 319: 446-449. PMID 3998003 DOI: 10.1016/S0021-9673(01)90588-6 |
0.325 |
|
| 1985 |
Griess GA, Serwer P, Horowitz PM. Binding of ethidium to bacteriophage T7 and T7 deletion mutants Biopolymers - Peptide Science Section. 24: 1635-1646. PMID 3899209 DOI: 10.1002/Bip.360240816 |
0.304 |
|
| 1985 |
Wasylewski Z, Criscimagna NL, Horowitz PM. A fluorescence study of thermally induced conformational changes in yeast hexokinase Biochimica Et Biophysica Acta (Bba)/Protein Structure and Molecular. 831: 201-206. PMID 3899179 DOI: 10.1016/0167-4838(85)90036-6 |
0.431 |
|
| 1985 |
Lee JC, Anderson R, Yeh YC, Horowitz P. Extraction of proteins from Saccharomyces cerevisiae ribosomes under nondenaturing conditions. Archives of Biochemistry and Biophysics. 237: 292-299. PMID 3883901 DOI: 10.1016/0003-9861(85)90280-2 |
0.343 |
|
| 1985 |
Horowitz PM, Criscimagna NL. Differential binding of the fluorescent probe 8-anilinonaphthalene-2-sulfonic acid to rhodanese catalytic intermediates Biochemistry. 24: 2587-2593. PMID 3861197 DOI: 10.1021/Bi00332A001 |
0.411 |
|
| 1985 |
Boggaram V, Horowitz P, Waterman MR. Studies on rhodanese synthesis in bovine adrenocortical cells. Biochemical and Biophysical Research Communications. 130: 407-411. PMID 2992467 DOI: 10.1016/0006-291X(85)90431-0 |
0.301 |
|
| 1984 |
Horowitz PM, Lee JC, Williams GA, Williams RF, Barnes LD. Electrophoresis of proteins and nucleic acids on acrylamide-agarose gels lacking covalent crosslinking. Analytical Biochemistry. 143: 333-40. PMID 6085222 DOI: 10.1016/0003-2697(84)90672-9 |
0.336 |
|
| 1983 |
Barnes LD, Robinson AK, Williams RF, Horowitz PM. Binding of colchicine to renal tubulin at 5 degrees C. Biochemical and Biophysical Research Communications. 116: 866-72. PMID 6651851 DOI: 10.1016/S0006-291X(83)80222-8 |
0.307 |
|
| 1983 |
Horowitz P, Falksen K. The use of tritium exchange to detect conformational differences between intermediates in catalysis by the enzyme rhodanese. Biochimica Et Biophysica Acta. 747: 37-41. PMID 6576809 DOI: 10.1016/0167-4838(83)90118-8 |
0.351 |
|
| 1983 |
Horowitz PM, Criscimagna NL. A study of the apolar interaction of the enzyme rhodanese with octyl substituted agarose gel Biochemical and Biophysical Research Communications. 111: 595-601. PMID 6573162 DOI: 10.1016/0006-291X(83)90348-0 |
0.45 |
|
| 1983 |
Prasad ARS, Nishimura JS, Horowitz PM. A study of the quenching of the intrinsic fluorescence of succinyl-CoA synthetase from Escherichia coli by acrylamide, iodide, and coenzyme A Biochemistry. 22: 4272-4275. PMID 6354251 DOI: 10.1021/Bi00287A017 |
0.371 |
|
| 1982 |
Horowitz P, Criscimagna NL. The specificity of active-site alkylation by iodoacetic acid in the enzyme thiosulfate sulfurtransferase Biochimica Et Biophysica Acta. 702: 173-177. PMID 6952939 DOI: 10.1016/0167-4838(82)90499-X |
0.406 |
|
| 1982 |
Wasylewski Z, Horowitz PM. A Fluorescence study of conformational changes induced by substrate and temperature in bovine liver thiosulfate sulfurtransferase Biochimica Et Biophysica Acta (Bba)/Protein Structure and Molecular. 701: 12-18. PMID 6948580 DOI: 10.1016/0167-4838(82)90305-3 |
0.427 |
|
| 1982 |
Prasad ARS, Nishimura JS, Horowitz PM. Fluorescence detection of increased local flexibility induced by coenzyme A in succinyl-coA synthetase from Escherichia coli. Biochemistry. 21: 5142-5147. PMID 6756468 DOI: 10.1021/Bi00264A006 |
0.323 |
|
| 1980 |
Horowitz PM, Wasylewski Z, Kolb WP. Fluorometric detection of low temperature thermal transitions in the C1Q component of human complement Biochemical and Biophysical Research Communications. 96: 382-387. PMID 6969077 DOI: 10.1016/0006-291X(80)91226-7 |
0.31 |
|
| 1980 |
Horowitz PM, Patel K. Some comparisons between solution and crystal properties of thiosulfate sulfurtransferase Biochemical and Biophysical Research Communications. 94: 419-423. PMID 6930969 DOI: 10.1016/0006-291X(80)91247-4 |
0.374 |
|
| 1978 |
Horowitz PM. Purification of thiosulfate sulfurtransferase by selective immobilization on blue agarose Analytical Biochemistry. 86: 751-753. PMID 655428 DOI: 10.1016/0003-2697(78)90803-5 |
0.343 |
|
| 1977 |
Guido K, Horowitz P. Studies of the N-bromosuccinimide inactivation of the enzyme rhodanese Biochimica Et Biophysica Acta. 485: 95-100. PMID 911868 DOI: 10.1016/0005-2744(77)90196-6 |
0.368 |
|
| 1977 |
Michaels GA, Whitlock SD, Horowitz P, Levin P. Binding of concanavalin A to nuclei of unsynchronized and synchronized HeLa cells. Biochemical and Biophysical Research Communications. 75: 480-7. PMID 851450 DOI: 10.1016/0006-291X(77)91067-1 |
0.303 |
|
| 1976 |
Guido K, Baillie RD, Horowitz PM. Spectral studies of the tryptophan exposure in the enzyme rhodanese Bba - Protein Structure. 427: 600-607. PMID 1268221 DOI: 10.1016/0005-2795(76)90203-8 |
0.419 |
|
| 1976 |
Baillie RD, Horowitz PM. The aromatic residue content of the enzyme rhodanese Bba - Protein Structure. 427: 594-599. PMID 1268220 DOI: 10.1016/0005-2795(76)90202-6 |
0.372 |
|
| 1976 |
Horowitz PM, Phillips PG. A sensitive competency assay for concanavalin A binding Analytical Biochemistry. 74: 171-174. PMID 962071 DOI: 10.1016/0003-2697(76)90321-3 |
0.311 |
|
| 1976 |
Baillie RD, Horowitz PM. A Reexamination of the postulated charge transfer interactions at the active site of the enzyme rhodanese Bba - Enzymology. 429: 402-408. PMID 130934 DOI: 10.1016/0005-2744(76)90288-6 |
0.353 |
|
| 1976 |
Baillie RD, Horowitz PM. Denaturation-induced disulfide formation in the enzyme rhodanese Bba - Enzymology. 429: 383-390. PMID 4128 DOI: 10.1016/0005-2744(76)90286-2 |
0.349 |
|
| 1976 |
Crawford JM, Horowitz PM. A study of the single polypeptide nature of rhodanese a comparison of different preparations Bba - Enzymology. 429: 173-181. PMID 4117 DOI: 10.1016/0005-2744(76)90039-5 |
0.369 |
|
| 1976 |
Pelley R, Horowitz P. Fluorimetric studies of tryptophyl exposure in concanavalin A. Biochimica Et Biophysica Acta. 427: 359-363. PMID 4111 DOI: 10.1016/0005-2795(76)90311-1 |
0.408 |
|
| 1975 |
Guido K, Horowitz PM. Contact versus energy transfer fluorescence quenching in the sulfur substituted form of the enzyme rhodanese: A study using cesium ion resolved emission spectra Biochemical and Biophysical Research Communications. 67: 670-676. PMID 1201046 DOI: 10.1016/0006-291X(75)90864-5 |
0.413 |
|
| 1975 |
Kim SK, Horowitz PM. A study of dithiothreitol inactivation of the enzyme rhodanese Biochemical and Biophysical Research Communications. 67: 433-439. PMID 1201034 DOI: 10.1016/0006-291X(75)90334-4 |
0.379 |
|
| 1974 |
Trumpower BL, Katki A, Horowitz P. Enhancement of rhodanese activity during controlled digestion with trypsin Biochemical and Biophysical Research Communications. 57: 523-528. PMID 4857284 DOI: 10.1016/0006-291X(74)90965-6 |
0.337 |
|
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