Modrich P - Search Results

1

Modification of Escherichia coli DNA ligase by cleavage with trypsin.

Panasenko SM, Modrich P, Lehman IR. Panasenko SM, et al. Among authors: modrich p. J Biol Chem. 1976 Jun 10;251(11):3432-5. J Biol Chem. 1976. PMID: 179997 Free article.

2

Deoxyribonucleic acid ligase. Isolation and physical characterization of the homogeneous enzyme from Escherichia coli.

Modrich P, Anraku Y, Lehman IR. Modrich P, et al. J Biol Chem. 1973 Nov 10;248(21):7495-501. J Biol Chem. 1973. PMID: 4355584 Free article. No abstract available.

3

Enzymatic joining of polynucleotides. XI. Reversal of Escherichia coli deoxyribonucleic acid ligase reaction.

Modrich P, Lehman IR, Wang JC. Modrich P, et al. J Biol Chem. 1972 Oct 10;247(19):6370-2. J Biol Chem. 1972. PMID: 4568616 Free article. No abstract available.

4

Genetic and enzymatic characterization of a conditional lethal mutant of Escherichia coli K12 with a temperature-sensitive DNA ligase.

Konrad EB, Modrich P, Lehman IR. Konrad EB, et al. Among authors: modrich p. J Mol Biol. 1973 Jul 15;77(4):519-29. doi: 10.1016/0022-2836(73)90220-9. J Mol Biol. 1973. PMID: 4353283 No abstract available.

5

DNA synthesis in strains of Escherichia coli K12 with temperature-sensitive DNA ligase and DNA polymerase I.

Konrad EB, Modrich P, Lehman IR. Konrad EB, et al. Among authors: modrich p. J Mol Biol. 1974 Nov 25;90(1):115-26. doi: 10.1016/0022-2836(74)90260-5. J Mol Biol. 1974. PMID: 4616094 No abstract available.

6

Enzymatic joining of polynucleotides. IX. A simple and rapid assay of polynucleotide joining (ligase) activity by measurement of circle formation from linear deoxyadenylate-deoxythymidylate copolymer.

Modrich P, Lehman IR. Modrich P, et al. J Biol Chem. 1970 Jul 25;245(14):3626-31. J Biol Chem. 1970. PMID: 4919213 Free article. No abstract available.

7

Enzymatic characterization of a mutant of Escherichia coli with an altered DNA ligase.

Modrich P, Lehman IR. Modrich P, et al. Proc Natl Acad Sci U S A. 1971 May;68(5):1002-5. doi: 10.1073/pnas.68.5.1002. Proc Natl Acad Sci U S A. 1971. PMID: 4995816 Free PMC article.

8

Recognition sequence of the dam methylase of Escherichia coli K12 and mode of cleavage of Dpn I endonuclease.

Geier GE, Modrich P. Geier GE, et al. Among authors: modrich p. J Biol Chem. 1979 Feb 25;254(4):1408-13. J Biol Chem. 1979. PMID: 368070 Free article.

9

Partial NH2- and COOH-terminal sequence and cyanogen bromide peptide analysis of Escherichia coli sn-glycerol-3-phosphate acyltransferase.

Green PR, Vanaman TC, Modrich P, Bell RM. Green PR, et al. Among authors: modrich p. J Biol Chem. 1983 Sep 25;258(18):10862-6. J Biol Chem. 1983. PMID: 6350296 Free article.

The sn-glycerol-3-phosphate acyltransferase from Escherichia coli, an integral membrane protein whose activity is dependent on phospholipids, was purified to near homogeneity (Green, P. R., Merrill, A. H., Jr., and Bell, R. M., (1981) J. Biol. Chem. 256, 11151-11159). Dete …

The sn-glycerol-3-phosphate acyltransferase from Escherichia coli, an integral membrane protein whose activity is dependent on phospholipids …

10

Isolation and characterization of the Escherichia coli mutH gene product.

Welsh KM, Lu AL, Clark S, Modrich P. Welsh KM, et al. Among authors: modrich p. J Biol Chem. 1987 Nov 15;262(32):15624-9. J Biol Chem. 1987. PMID: 2824465 Free article.

The Escherichia coli mutH gene product has been isolated in near homogeneous form using an in vitro complementation assay for DNA mismatch correction (Lu, A.-L., Clark, S., and Modrich, P. (1983) Proc. Natl. Acad. Sci. U.S.A. 80, 4639-4643) which is dependent on mut …

The Escherichia coli mutH gene product has been isolated in near homogeneous form using an in vitro complementation assay for DNA mismatch c …

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