92 related articles for article (PubMed ID: 41571)
1. Development of a method for the incorporation of substitution-inert metal ions into proteins. Site-specific modification of arsanilazotyrosine-248 carboxypeptidase A with cobalt(III).
Urdea MS; Legg JI
Biochemistry; 1979 Oct; 18(22):4984-91. PubMed ID: 41571
[TBL] [Abstract][Full Text] [Related]
2. A peptidase-inactive derivative of carboxypeptidase A modified specifically at tyrosine 248. Cobalt(III) (ethylenediamine-N,N'-diacetato) (arsanilazotyrosinato 248 carboxypeptidase A).
Urdea MS; Legg JI
J Biol Chem; 1979 Dec; 254(23):11868-74. PubMed ID: 574142
[No Abstract] [Full Text] [Related]
3. Interaction of zinc ions with arsanilazotyrosine-248 carboxypeptidase A.
Hirose J; Noji M; Kidani Y; Wilkins RG
Biochemistry; 1985 Jul; 24(14):3495-502. PubMed ID: 4041425
[TBL] [Abstract][Full Text] [Related]
4. Enzymatically inactive, exchange-inert Co(III)-carboxypeptidase A: role of inner sphere coordination in peptide and ester catalysis.
van Wart HE; Vallee BL
Biochemistry; 1978 Aug; 17(16):3385-94. PubMed ID: 210789
[TBL] [Abstract][Full Text] [Related]
5. Conformations of arsanilazotyrosine-248 carboxypeptidase A alpha, beta, gamma, comparison of crystals and solution.
Johansen JT; Vallee BL
Proc Natl Acad Sci U S A; 1973 Jul; 70(7):2006-10. PubMed ID: 4516200
[TBL] [Abstract][Full Text] [Related]
6. Spectral properties of cobalt carboxypeptidase A. Interaction of the metal atom with anions.
Geoghegan KF; Holmquist B; Spilburg CA; Vallee BL
Biochemistry; 1983 Apr; 22(8):1847-52. PubMed ID: 6849891
[TBL] [Abstract][Full Text] [Related]
7. Metal ion effects on target sites of modification in metallocarboxypeptidase B.
Zisapel N; Blank T; Sokolovsky M
J Inorg Biochem; 1983 Jun; 18(3):253-62. PubMed ID: 6875538
[TBL] [Abstract][Full Text] [Related]
8. Environment and conformation dependent sensitivity of the arsanilazotyrosine-248 carboxypeptidase A chromophore.
Johansen JT; Vallee BL
Biochemistry; 1975 Feb; 14(4):649-60. PubMed ID: 234737
[TBL] [Abstract][Full Text] [Related]
9. Similarities between the conformation of arsanilazotyrosine 248 of carboxypeptidase A in the crystalline state and in solution.
Quiocho FA; McMurray CH; Lipscomb WN
Proc Natl Acad Sci U S A; 1972 Oct; 69(10):2850-4. PubMed ID: 4507609
[TBL] [Abstract][Full Text] [Related]
10. Effects of mechanism-based reversible inhibitors on the metal environment of cobalt(II)carboxypeptidase A: an electronic spectral study.
Martin MT; Holmquist B; Riordan JF
J Inorg Biochem; 1989 May; 36(1):27-37. PubMed ID: 2746219
[TBL] [Abstract][Full Text] [Related]
11. Circular dichroism-inhibitor titrations of arsanilazotyrosine-248 carboxypeptidase A.
Johansen JT; Klyosov AA; Vallee BL
Biochemistry; 1976 Jan; 15(2):296-303. PubMed ID: 1247518
[TBL] [Abstract][Full Text] [Related]
12. Kinetics of substrate and product interactions with arsanilazotyrosine-248 carboxypeptidase A.
Harrison LW; Vallee BL
Biochemistry; 1978 Oct; 17(21):4359-63. PubMed ID: 718842
[TBL] [Abstract][Full Text] [Related]
13. Cobalt substitution studies on bovine erythrocyte superoxide dismutase: evidence for a novel cobalt-superoxide dismutase derivative.
Salvato B; Beltramini M; Ricchelli F; Tallandini L
Biochim Biophys Acta; 1989 Sep; 998(1):14-20. PubMed ID: 2790051
[TBL] [Abstract][Full Text] [Related]
14. Differences between the conformation of arsanilazotyrosine 248 of carboxypeptidase A in the crystalline state and in solution.
Johansen JT; Vallee BL
Proc Natl Acad Sci U S A; 1971 Oct; 68(10):2532-5. PubMed ID: 5289887
[TBL] [Abstract][Full Text] [Related]
15. Cobalt(III) complexes of bidentate azotyrosine analogs.
White WI; Legg JI
Bioinorg Chem; 1976; 6(2):163-77. PubMed ID: 1053538
[TBL] [Abstract][Full Text] [Related]
16. Site-specific substituted cobalt(II) horse liver alcohol dehydrogenases. Preparation and characterization in solution, crystalline and immobilized state.
Maret W; Andersson I; Dietrich H; Schneider-Bernlöhr H; Einarsson R; Zeppezauer M
Eur J Biochem; 1979 Aug; 98(2):501-12. PubMed ID: 488110
[TBL] [Abstract][Full Text] [Related]
17. Metal-coordinating substrate analogs as inhibitors of metalloenzymes.
Holmquist B; Vallee BL
Proc Natl Acad Sci U S A; 1979 Dec; 76(12):6216-20. PubMed ID: 230502
[TBL] [Abstract][Full Text] [Related]
18. Exchange-inert metal ions as probes of enzyme structure-function relationships. Cobalt(III), cobalt(II), and zinc(II), azophenol complexes as models for enzyme azotyrosine complexes.
White WI; Legg JI
J Am Chem Soc; 1975 Jul; 97(14):3937-41. PubMed ID: 1159207
[No Abstract] [Full Text] [Related]
19. Theoretical analysis of the influence of chelate-ring size and vicinal effects on electronic circular dichroism spectra of cobalt(III) EDDA-type complexes.
Wang A; Wang Y; Jia J; Feng L; Zhang C; Liu L
J Phys Chem A; 2013 Jun; 117(24):5061-72. PubMed ID: 23713886
[TBL] [Abstract][Full Text] [Related]
20. Formation and characterization of an active phosphoenolpyruvate carboxykinase-cobalt(III) complex.
Hlavaty JJ; Nowak T
Biochemistry; 1997 Mar; 36(11):3389-403. PubMed ID: 9116019
[TBL] [Abstract][Full Text] [Related]
[Next] [New Search]