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Results: 1-11 |
Results: 11
THE PHAGE-LAMBDA TERMINASE ENZYME - 1 - RECONSTITUTION OF THE HOLOENZYME FROM THE INDIVIDUAL SUBUNITS ENHANCES THE THERMAL-STABILITY OF THESMALL-SUBUNIT
Authors: MEYER JD HANAGAN A MANNING MC CATALANO CE
Citation: Jd. Meyer et al., THE PHAGE-LAMBDA TERMINASE ENZYME - 1 - RECONSTITUTION OF THE HOLOENZYME FROM THE INDIVIDUAL SUBUNITS ENHANCES THE THERMAL-STABILITY OF THESMALL-SUBUNIT, International journal of biological macromolecules, 23(1), 1998, pp. 27-36
THE PHAGE-LAMBDA TERMINASE ENZYME - 2 - REFOLDING OF THE GPNU1 SUBUNIT FROM THE DETERGENT-DENATURED AND GUANIDINIUM HYDROCHLORIDE-DENATUREDSTATE YIELDS DIFFERENT OLIGOMERIZATION STATES AND ALTERED PROTEIN STABILITIES
Authors: HANAGAN A MEYER JD JOHNSON L MANNING MC CATALANO CE
Citation: A. Hanagan et al., THE PHAGE-LAMBDA TERMINASE ENZYME - 2 - REFOLDING OF THE GPNU1 SUBUNIT FROM THE DETERGENT-DENATURED AND GUANIDINIUM HYDROCHLORIDE-DENATUREDSTATE YIELDS DIFFERENT OLIGOMERIZATION STATES AND ALTERED PROTEIN STABILITIES, International journal of biological macromolecules, 23(1), 1998, pp. 37-48
THE DNA PACKAGING ENZYME OF PHAGE-LAMBDA - DIMERIZATION AND OLIGOMERIZATION OF THE SMALL-SUBUNIT MAY INVOLVE A HYDROPHOBIC INTERFACE AND ANINTERMOLECULAR DISULFIDE BOND
Authors: MEYER JD HANAGAN A MANNING MC CATALANO CE
Citation: Jd. Meyer et al., THE DNA PACKAGING ENZYME OF PHAGE-LAMBDA - DIMERIZATION AND OLIGOMERIZATION OF THE SMALL-SUBUNIT MAY INVOLVE A HYDROPHOBIC INTERFACE AND ANINTERMOLECULAR DISULFIDE BOND, Biophysical journal, 74(2), 1998, pp. 72-72
KINETIC CHARACTERIZATION OF THE STRAND SEPARATION (HELICASE) ACTIVITYOF THE DNA PACKAGING ENZYME FROM BACTERIOPHAGE-LAMBDA
Authors: YANG Q CATALANO CE
Citation: Q. Yang et Ce. Catalano, KINETIC CHARACTERIZATION OF THE STRAND SEPARATION (HELICASE) ACTIVITYOF THE DNA PACKAGING ENZYME FROM BACTERIOPHAGE-LAMBDA, Biochemistry, 36(35), 1997, pp. 10638-10645
KINETIC-ANALYSIS OF THE ENDONUCLEASE ACTIVITY OF PHAGE-LAMBDA TERMINASE - ASSEMBLY OF A CATALYTICALLY COMPETENT NICKING COMPLEX IS RATE-LIMITING
Authors: WOODS L TERPENING C CATALANO CE
Citation: L. Woods et al., KINETIC-ANALYSIS OF THE ENDONUCLEASE ACTIVITY OF PHAGE-LAMBDA TERMINASE - ASSEMBLY OF A CATALYTICALLY COMPETENT NICKING COMPLEX IS RATE-LIMITING, Biochemistry, 36(19), 1997, pp. 5777-5785
ASSEMBLY OF A NUCLEOPROTEIN COMPLEX REQUIRED FOR DNA PACKAGING BY BACTERIOPHAGE-LAMBDA
Authors: YANG Q HANAGAN A CATALANO CE
Citation: Q. Yang et al., ASSEMBLY OF A NUCLEOPROTEIN COMPLEX REQUIRED FOR DNA PACKAGING BY BACTERIOPHAGE-LAMBDA, Biochemistry, 36(10), 1997, pp. 2744-2752
KINETIC AND MUTATIONAL DISSECTION OF THE 2 ATPASE ACTIVITIES OF TERMINASE, THE DNA PACKAGING ENZYME OF BACTERIOPHAGE-LAMBDA
Authors: HWANG Y CATALANO CE FEISS M
Citation: Y. Hwang et al., KINETIC AND MUTATIONAL DISSECTION OF THE 2 ATPASE ACTIVITIES OF TERMINASE, THE DNA PACKAGING ENZYME OF BACTERIOPHAGE-LAMBDA, Biochemistry, 35(8), 1996, pp. 2796-2803
VIRUS-DNA PACKAGING - THE STRATEGY USED BY PHAGE-LAMBDA
Authors: CATALANO CE CUE D FEISS M
Citation: Ce. Catalano et al., VIRUS-DNA PACKAGING - THE STRATEGY USED BY PHAGE-LAMBDA, Molecular microbiology, 16(6), 1995, pp. 1075-1086
ROLE OF GPFI PROTEIN IN DNA PACKAGING BY BACTERIOPHAGE-LAMBDA
Authors: CATALANO CE TOMKA MA
Citation: Ce. Catalano et Ma. Tomka, ROLE OF GPFI PROTEIN IN DNA PACKAGING BY BACTERIOPHAGE-LAMBDA, Biochemistry, 34(31), 1995, pp. 10036-10042
INACTIVATION OF DNA-POLYMERASE ALPHA-PRIMASE BY ACROLEIN - LOSS OF ACTIVITY DEPENDS ON THE DNA SUBSTRATE
Authors: CATALANO CE KUCHTA RD
Citation: Ce. Catalano et Rd. Kuchta, INACTIVATION OF DNA-POLYMERASE ALPHA-PRIMASE BY ACROLEIN - LOSS OF ACTIVITY DEPENDS ON THE DNA SUBSTRATE, Biochemical and biophysical research communications, 214(3), 1995, pp. 971-977
KINETIC CHARACTERIZATION OF THE ATPASE ACTIVITY OF THE DNA PACKAGING ENZYME FROM BACTERIOPHAGE-LAMBDA
Authors: TOMKA MA CATALANO CE
Citation: Ma. Tomka et Ce. Catalano, KINETIC CHARACTERIZATION OF THE ATPASE ACTIVITY OF THE DNA PACKAGING ENZYME FROM BACTERIOPHAGE-LAMBDA, Biochemistry, 32(45), 1993, pp. 11992-11997
Risultati: 1-11 |