| Year |
Citation |
Score |
| 2010 |
Markowitz MA, Seykora JT, Kézdy FJ. The Substrate Specificity of Phospholipase A2: The Reaction of the Enzyme with 3-Octanoyloxy-4-Nitrobenzoic Acid Bulletin Des SociéTéS Chimiques Belges. 94: 1033-1037. DOI: 10.1002/Bscb.19850941124 |
0.321 |
|
| 1995 |
Chou KC, Zhang CT, Kézdy FJ, Poorman RA. A vector projection method for predicting the specificity of GalNAc-transferase. Proteins. 21: 118-26. PMID 7777486 DOI: 10.1002/Prot.340210205 |
0.313 |
|
| 1991 |
Cho W, Kezdy FJ. Chromogenic substrates and assay of phospholipases A2 Methods in Enzymology. 197: 75-79. PMID 2051947 DOI: 10.1016/0076-6879(91)97134-K |
0.514 |
|
| 1988 |
Farooqui JZ, Wohl RC, Kézdy FJ, Scanu AM. Identification of the active-site serine in human lecithin: Cholesterol acyltransferase Archives of Biochemistry and Biophysics. 261: 330-335. PMID 3128170 DOI: 10.1016/0003-9861(88)90348-7 |
0.304 |
|
| 1988 |
Cho W, Markowitz MA, Kezdy FJ. A new class of phospholipase A2 substrates: kinetics of the phospholipase A2 catalyzed hydrolysis of 3-(acyloxy)-4-nitrobenzoic acids Journal of the American Chemical Society. 110: 5166-5171. DOI: 10.1021/Ja00223A043 |
0.489 |
|
| 1988 |
CHO W, MARKOWITZ MA, KEZDY FJ. ChemInform Abstract: A New Class of Phospholipase A2 Substrates: Kinetics of the Phospholipase A2 Catalyzed Hydrolysis of 3-(Acyloxy)-4-nitrobenzoic Acids (I). Cheminform. 19. DOI: 10.1002/chin.198846328 |
0.441 |
|
| 1986 |
Reddy MN, Maraganore JM, Meredith SC, Heinrikson RL, Kézdy FJ. Isolation of an active-site peptide of lipoprotein lipase from bovine milk and determination of its amino acid sequence. The Journal of Biological Chemistry. 261: 9678-83. PMID 3525532 |
0.488 |
|
| 1985 |
Retzinger GS, Meredith SC, Lau SH, Kaiser ET, Kézdy FJ. A method for probing the affinity of peptides for amphiphilic surfaces. Analytical Biochemistry. 150: 131-40. PMID 4083474 DOI: 10.1016/0003-2697(85)90451-8 |
0.52 |
|
| 1985 |
OSTERMAN D, MORA R, KEZDY FJ, KAISER ET, MEREDITH SC. ChemInform Abstract: A SYNTHETIC AMPHIPHILIC β-STRAND TRIDECAPEPTIDE: A MODEL FOR APOLIPOPROTEIN B Chemischer Informationsdienst. 16. DOI: 10.1002/chin.198508312 |
0.447 |
|
| 1984 |
Osterman D, Mora R, Kezdy FJ, Kaiser ET, Meredith SC. A synthetic amphiphilic .beta.-strand tridecapeptide: a model for apolipoprotein B Journal of the American Chemical Society. 106: 6845-6847. DOI: 10.1021/Ja00334A065 |
0.485 |
|
| 1982 |
Retzinger GS, Meredith SC, Hunter RL, Takayama K, Kézdy FJ. Identification of the physiologically active state of the mycobacterial glycolipid trehalose 6,6'-dimycolate and the role of fibrinogen in the biologic activities of trehalose 6,6'-dimycolate monolayers. Journal of Immunology (Baltimore, Md. : 1950). 129: 735-44. PMID 6806381 |
0.44 |
|
| 1981 |
Retzinger GS, Meredith SC, Takayama K, Hunter RL, Kézdy FJ. The role of surface in the biological activities of trehalose 6,6'-dimycolate. Surface properties and development of a model system. The Journal of Biological Chemistry. 256: 8208-16. PMID 7263645 |
0.443 |
|
| 1981 |
Meredith SC, Kézdy FJ. The chromatographic purification of native types I, II, and III collagens Bba - Protein Structure. 668: 357-369. PMID 7236712 DOI: 10.1016/0005-2795(81)90169-0 |
0.5 |
|
| 1976 |
Cohen H, Shen BW, Snyder WR, Law JH, Kézdy FJ. The surface pressure dependency of the enzymatic hydrolysis of lipid monolayers enzyme denaturation at the air-water interface Journal of Colloid and Interface Science. 56: 240-250. DOI: 10.1016/0021-9797(76)90249-6 |
0.303 |
|
| 1975 |
Silverstein RM, Kezdy FJ. Characterization of the pineapple stem proteases (bromelains). Archives of Biochemistry and Biophysics. 167: 678-86. PMID 1124936 DOI: 10.1016/0003-9861(75)90512-3 |
0.311 |
|
| 1975 |
Neumann H, Kezdy F, Hsu J, Rosenberg IH. The reaction of tris (hydroxymethyl) aminomethane with calf intestinal alkaline phosphatase. Biochimica Et Biophysica Acta. 391: 292-300. PMID 238598 DOI: 10.1016/0005-2744(75)90253-3 |
0.352 |
|
| 1971 |
Frankfater A, Kézdy FJ. Kinetics of hydrolysis of p-nitrophenyl thiolacetate by chymotrypsin Journal of the American Chemical Society. 93: 4039-4043. PMID 5138306 |
0.658 |
|
| 1971 |
FRANKFATER A, KEZDY FJ. ChemInform Abstract: KINETIK DER HYDROLYSE VON P-NITRO-PHENYLTHIOLACETAT DURCH CHYMOTRYPSIN Chemischer Informationsdienst. Organische Chemie. 2. DOI: 10.1002/chin.197144117 |
0.623 |
|
| 1970 |
Hall RL, Kézdy FJ. Glyoxylate carboligase from E. coli: specificity of the enzyme for unhydrated glyoxylate. Archives of Biochemistry and Biophysics. 138: 551-6. PMID 4914900 DOI: 10.1016/0003-9861(70)90380-2 |
0.33 |
|
| 1967 |
Ko SH, Kézdy FJ. The kinetics of the Escherichia coli alkaline phosphatase catalyzed hydrolysis of 2,4-dinitrophenyl phosphate. Journal of the American Chemical Society. 89: 7139-40. PMID 4863557 DOI: 10.1021/Ja01002A068 |
0.319 |
|
| 1965 |
KEZDY FJ, BENDER ML. THE ACYL-ENZYME DIMER OF CHYMOTRYPISM. Biochemistry. 4: 104-13. PMID 14285226 DOI: 10.1021/Bi00877A018 |
0.3 |
|
| 1965 |
Bender ML, Kézdy FJ, Feder J. The kinetics of the trypsin-catalyzed hydrolysis of p-nitrophenyl alpha-N-benzyloxycarbonyl-L-lysinate hydrochloride. Journal of the American Chemical Society. 87: 4953-4. PMID 5844467 DOI: 10.1021/Ja00949A048 |
0.314 |
|
| 1964 |
Kezdy FJ, Clement GE, Bender ML. The Observation of Acyl-Enzyme Intermediates in the α-Chymotrypsin-Catalyzed Reactions of N-Acetyl-L-tryptophan Derivatives at Low pH Journal of the American Chemical Society. 86: 3690-3696. DOI: 10.1021/Ja01072A018 |
0.344 |
|
| 1964 |
Kezdy FJ, Bender ML. The Observation of Acyl-Enzyme Intermediates in the α-Chymotrypsin-Catalyzed Hydrolysis of Specific Ester Substrates at Low pH Journal of the American Chemical Society. 86: 937-938. DOI: 10.1021/Ja01059A048 |
0.354 |
|
| 1963 |
Bender ML, Kezdy FJ, Zerner B. Intramolecular Catalysis in the Hydrolysis ofp-Nitrophenyl Salicylates Journal of the American Chemical Society. 85: 3017-3024. DOI: 10.1021/Ja00902A032 |
0.331 |
|
| 1962 |
KEZDY FJ, BENDER ML. The kinetics of the alpha-chymotrypsin-catalyzed hydrolysis of p-nitrophenyl acetate. Biochemistry. 1: 1097-106. PMID 14032227 DOI: 10.1021/Bi00912A021 |
0.319 |
|
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