| Year |
Citation |
Score |
| 2018 |
Shanbhag V, Sachdev S, Flores JA, Modak MJ, Singh K. Family A and B DNA Polymerases in Cancer: Opportunities for Therapeutic Interventions. Biology. 7. PMID 29301327 DOI: 10.3390/Biology7010005 |
0.479 |
|
| 2010 |
Sandalli C, Canakci S, Demir İ, Modak MJ, Belduz AO. Comparison of DIG-11-dUTP utilization by Geobacillus caldoxylosilyticus TK4, Mycobacterium tuberculosis and Escherichia coli DNA polymerases World Journal of Microbiology & Biotechnology. 26: 459-464. DOI: 10.1007/S11274-009-0189-X |
0.523 |
|
| 2009 |
Sandalli C, Singh K, Modak MJ, Ketkar A, Canakci S, Demir I, Belduz AO. A new DNA polymerase I from Geobacillus caldoxylosilyticus TK4: cloning, characterization, and mutational analysis of two aromatic residues. Applied Microbiology and Biotechnology. 84: 105-17. PMID 19365630 DOI: 10.1007/S00253-009-1962-3 |
0.527 |
|
| 2008 |
Kukreti P, Singh K, Ketkar A, Modak MJ. Identification of a new motif required for the 3'-5' exonuclease activity of Escherichia coli DNA polymerase I (Klenow fragment): the RRRY motif is necessary for the binding of single-stranded DNA substrate and the template strand of the mismatched duplex. The Journal of Biological Chemistry. 283: 17979-90. PMID 18448432 DOI: 10.1074/Jbc.M801053200 |
0.572 |
|
| 2007 |
Singh K, Srivastava A, Patel SS, Modak MJ. Participation of the fingers subdomain of Escherichia coli DNA polymerase I in the strand displacement synthesis of DNA. The Journal of Biological Chemistry. 282: 10594-604. PMID 17259182 DOI: 10.1074/Jbc.M611242200 |
0.526 |
|
| 2007 |
Kukreti P, Singh K, Modak MJ. Identification of R/KRRY motif in Klenow Fragment of E. coli DNA polymerase I: Its role in coordinating polymerase and exonuclease activity The Faseb Journal. 21. DOI: 10.1096/Fasebj.21.5.A656-E |
0.427 |
|
| 2005 |
Singh K, Modak MJ. Contribution of polar residues of the J-helix in the 3'-5' exonuclease activity of Escherichia coli DNA polymerase I (Klenow fragment): Q677 regulates the removal of terminal mismatch. Biochemistry. 44: 8101-10. PMID 15924429 DOI: 10.1021/Bi050140R |
0.571 |
|
| 2003 |
Srivastava A, Singh K, Modak MJ. Phe 771 of Escherichia coli DNA polymerase I (Klenow fragment) is the major site for the interaction with the template overhang and the stabilization of the pre-polymerase ternary complex. Biochemistry. 42: 3645-54. PMID 12667054 DOI: 10.1021/Bi026699Y |
0.467 |
|
| 2003 |
Singh K, Modak MJ. Presence of 18-A long hydrogen bond track in the active site of Escherichia coli DNA polymerase I (Klenow fragment). Its requirement in the stabilization of enzyme-template-primer complex. The Journal of Biological Chemistry. 278: 11289-302. PMID 12522214 DOI: 10.1074/Jbc.M211496200 |
0.48 |
|
| 2002 |
Shi Q, Singh K, Srivastava A, Kaushik N, Modak MJ. Lysine 152 of MuLV reverse transcriptase is required for the integrity of the active site. Biochemistry. 41: 14831-42. PMID 12475231 DOI: 10.1021/Bi0258389 |
0.452 |
|
| 2002 |
Gangurde R, Modak MJ. Participation of active-site carboxylates of Escherichia coli DNA polymerase I (Klenow fragment) in the formation of a prepolymerase ternary complex. Biochemistry. 41: 14552-9. PMID 12463755 DOI: 10.1021/Bi0264216 |
0.478 |
|
| 2002 |
Arrigo CJ, Singh K, Modak MJ. DNA polymerase I of Mycobacterium tuberculosis: functional role of a conserved aspartate in the hinge joining the M and N helices. The Journal of Biological Chemistry. 277: 1653-61. PMID 11677239 DOI: 10.1074/Jbc.M108536200 |
0.439 |
|
| 2000 |
Singh K, Kaushik N, Jin J, Madhusudanan M, Modak MJ. Role of Q190 of MuLV RT in ddNTP resistance and fidelity of DNA synthesis: a molecular model of interactions with substrates Protein Engineering. 13: 635-643. PMID 11054458 DOI: 10.1093/Protein/13.9.635 |
0.472 |
|
| 2000 |
Kaushik N, Chowdhury K, Pandey VN, Modak MJ. Valine of the YVDD Motif of Moloney Murine Leukemia Virus Reverse Transcriptase: Role in the Fidelity of DNA Synthesis † Biochemistry. 39: 5155-5165. PMID 10819983 DOI: 10.1021/Bi992223B |
0.548 |
|
| 2000 |
Tuske S, Singh K, Kaushik N, Modak MJ. The J-helix of Escherichia coli DNA Polymerase I (Klenow Fragment) Regulates Polymerase and 3′– 5′-Exonuclease Functions Journal of Biological Chemistry. 275: 23759-23768. PMID 10818095 DOI: 10.1074/Jbc.M001804200 |
0.509 |
|
| 2000 |
Gangurde R, Kaushik N, Singh K, Modak MJ. A carboxylate triad is essential for the polymerase activity of Escherichia coli DNA polymerase I (Klenow fragment). Presence of two functional triads at the catalytic center. Journal of Biological Chemistry. 275: 19685-19692. PMID 10779513 DOI: 10.1074/Jbc.M002307200 |
0.484 |
|
| 1999 |
Jin J, Kaushik N, Singh K, Modak MJ. Analysis of the Role of Glutamine 190 in the Catalytic Mechanism of Murine Leukemia Virus Reverse Transcriptase Journal of Biological Chemistry. 274: 20861-20868. PMID 10409628 DOI: 10.1074/Jbc.274.30.20861 |
0.468 |
|
| 1999 |
Kaushik N, Singh K, Alluru I, Modak MJ. Tyrosine 222, a member of the YXDD motif of MuLV RT, is catalytically essential and is a major component of the fidelity center. Biochemistry. 38: 2617-2627. PMID 10052931 DOI: 10.1021/Bi9824285 |
0.485 |
|
| 1998 |
Singh K, Modak MJ. A unified DNA- and dNTP-binding mode for DNA polymerases Trends in Biochemical Sciences. 23: 277-281. PMID 9757823 DOI: 10.1016/S0968-0004(98)01250-X |
0.487 |
|
| 1998 |
Misra HS, Pandey PK, Modak MJ, Vinayak R, Pandey VN. Polyamide Nucleic Acid−DNA Chimera Lacking the Phosphate Backbone Are Novel Primers for Polymerase Reaction Catalyzed by DNA Polymerases† Biochemistry. 37: 1917-1925. PMID 9485318 DOI: 10.1021/Bi971524N |
0.578 |
|
| 1998 |
Lee R, Kaushik N, Modak MJ, Vinayak R, Pandey VN. Polyamide Nucleic Acid Targeted to the Primer Binding Site of the HIV-1 RNA Genome Blocks in Vitro HIV-1 Reverse Transcription† Biochemistry. 37: 900-910. PMID 9454580 DOI: 10.1021/Bi972197M |
0.413 |
|
| 1998 |
Yadav PNS, Das K, Ding J, Arnold E, Yadav JS, Modak MJ. Structure-based design of inhibitors of HIV-1 reverse transcriptase: a potential class of bidentate nonnucleoside inhibitors Journal of Molecular Structure-Theochem. 423: 101-111. DOI: 10.1016/S0166-1280(96)04996-2 |
0.338 |
|
| 1997 |
Kaushik N, Harris D, Rege N, Modak MJ, Yadav PNS, Pandey VN. Role of glutamine-151 of human immunodeficiency virus type-1 reverse transcriptase in RNA-directed DNA synthesis. Biochemistry. 36: 14430-14438. PMID 9398161 DOI: 10.1021/Bi970645K |
0.511 |
|
| 1996 |
Chowdhury K, Kaushik N, Pandey VN, Modak MJ. Elucidation of the Role of Arg 110 of Murine Leukemia Virus Reverse Transcriptase in the Catalytic Mechanism: Biochemical Characterization of Its Mutant Enzymes† Biochemistry. 35: 16610-16620. PMID 8987996 DOI: 10.1021/Bi961462L |
0.508 |
|
| 1996 |
Sarafianos SG, Kortz U, Pope MT, Modak MJ. Mechanism of polyoxometalate-mediated inactivation of DNA polymerases: an analysis with HIV-1 reverse transcriptase indicates specificity for the DNA-binding cleft. The Biochemical Journal. 619-26. PMID 8912703 DOI: 10.1042/Bj3190619 |
0.487 |
|
| 1996 |
Kaushik N, Rege N, Yadav PNS, Sarafianos SG, Modak MJ, Pandey VN. Biochemical analysis of catalytically crucial aspartate mutants of human immunodeficiency virus type 1 reverse transcriptase. Biochemistry. 35: 11536-11546. PMID 8794733 DOI: 10.1021/Bi960364X |
0.436 |
|
| 1996 |
Kaushik N, Pandey VN, Modak MJ. Significance of the O-Helix Residues of Escherichia coli DNA Polymerase I in DNA Synthesis: Dynamics of the dNTP Binding Pocket† Biochemistry. 35: 7256-7266. PMID 8679555 DOI: 10.1021/Bi960537I |
0.502 |
|
| 1996 |
Pandey VN, Kaushik N, Rege N, Sarafianos SG, Yadav PNS, Modak MJ. Role Of Methionine 184 Of Human Immunodeficiency Virus Type-1 Reverse Transcriptase In The Polymerase Function And Fidelity Of Dna Synthesis Biochemistry. 35: 2168-2179. PMID 8652558 DOI: 10.1021/Bi9516642 |
0.546 |
|
| 1995 |
Sarafianos SG, Pandey VN, Kaushik N, Modak MJ. Site-directed Mutagenesis of Arginine 72 of HIV-1 Reverse Transcriptase CATALYTIC ROLE AND INHIBITOR SENSITIVITY Journal of Biological Chemistry. 270: 19729-19735. PMID 7544345 DOI: 10.1074/Jbc.270.34.19729 |
0.385 |
|
| 1995 |
Sarafianos SG, Pandey VN, Kaushik N, Modak MJ. Glutamine 151 participates in the substrate dNTP binding function of HIV-1 reverse transcriptase. Biochemistry. 34: 7207-7216. PMID 7539293 DOI: 10.1021/Bi00021A036 |
0.517 |
|
| 1995 |
Pandey VN, Kaushik N, Modak MJ. Photoaffinity labeling of DNA template-primer binding site in Escherichia coli DNA polymerase I. Identification of involved amino acids. Journal of Biological Chemistry. 269: 21828-21834. DOI: 10.1074/Jbc.270.6.2879 |
0.497 |
|
| 1994 |
Desai SD, Pandey VN, Modak MJ. Properties of tyrosine 766-->serine mutant of Escherichia coli DNA polymerase I: template-specific effects. Biochemistry. 33: 11868-11874. PMID 7918405 DOI: 10.1021/Bi00205A024 |
0.553 |
|
| 1993 |
Pandey VN, Kaushik N, Sanzgiri RP, Patil MS, Modak MJ, Barik S. Site directed mutagenesis of DNA polymerase I (Klenow) from Escherichia coli. The significance of Arg682 in catalysis. European Journal of Biochemistry / Febs. 214: 59-65. PMID 8508807 DOI: 10.1111/J.1432-1033.1993.Tb17896.X |
0.551 |
|
| 1993 |
Basu S, Basu A, Modak MJ. Sulphydryl groups in the template-primer-binding domain of murine leukaemia virus reverse transcriptase. Identification and functional analysis of cysteine-90. Biochemical Journal. 296: 577-583. PMID 7506526 DOI: 10.1042/Bj2960577 |
0.511 |
|
| 1992 |
Yadav PNS, Yadav JS, Modak MJ. A molecular model of the complete three-dimensional structure of the Klenow fragment of Escherichia coli DNA polymerase. I: Binding of the dNTP substrate and template-primer Biochemistry. 31: 2879-2886. PMID 1550814 DOI: 10.1021/Bi00126A006 |
0.489 |
|
| 1992 |
Yadav PNS, Yadav JS, Modak MJ. Binding of DNA to large fragment of DNA polymerase. I : Identification of strong and weak electrostatic forces and their biological implications Journal of Biomolecular Structure & Dynamics. 10: 311-316. PMID 1466811 DOI: 10.1080/07391102.1992.10508649 |
0.518 |
|
| 1992 |
Basu A, Basu S, Modak MJ. Structure-activity analyses of HIV-1 reverse transcriptase. Biochemical and Biophysical Research Communications. 183: 1131-1138. PMID 1373608 DOI: 10.1016/S0006-291X(05)80308-0 |
0.371 |
|
| 1992 |
Basu A, Ahluwalia KK, Basu S, Modak MJ. Identification of the primer binding domain in human immunodeficiency virus reverse transcriptase Biochemistry. 31: 616-623. PMID 1370632 DOI: 10.1021/Bi00117A045 |
0.411 |
|
| 1991 |
Pandey VN, Dave VP, Amrute SB, Rosenbach K, Modak MJ. Thymic nuclear matrix associated activity is not V(D)J recombinase. Biochemical and Biophysical Research Communications. 181: 95-9. PMID 1958223 DOI: 10.1016/S0006-291X(05)81386-5 |
0.309 |
|
| 1991 |
Reddy G, Nanduri VB, Basu A, Modak MJ. Ferrate oxidation of murine leukemia virus reverse transcriptase: identification of the template-primer binding domain. Biochemistry. 30: 8195-201. PMID 1714300 DOI: 10.1021/Bi00247A015 |
0.41 |
|
| 1991 |
Tirumalai RS, Modak MJ. Photoaffinity labeling of the primer binding domain in murine leukemia virus reverse transcriptase. Biochemistry. 30: 6436-6443. PMID 1711370 DOI: 10.1021/Bi00240A014 |
0.398 |
|
| 1990 |
Pandey VN, Dave VP, Patil MS, Pradhan DS, Amrute SB, Modak MJ. Terminal deoxynucleotidyltransferase containing megadalton complex from young rat thymus nuclei: identification and characterization. Biochemistry. 29: 4037-41. PMID 2361129 DOI: 10.1021/Bi00469A002 |
0.378 |
|
| 1990 |
Nanduri VB, Modak MJ. Lysine-329 of murine leukemia virus reverse transcriptase: possible involvement in the template-primer binding function. Biochemistry. 29: 5258-64. PMID 1696496 DOI: 10.1021/Bi00474A006 |
0.495 |
|
| 1989 |
Basu A, Kedar P, Wilson SH, Modak MJ. Active-site modification of mammalian DNA polymerase β with pyridoxal 5′-phosphate: Mechanism of inhibition and identification of lysine 71 in the deoxynucleoside triphosphate binding pocket Biochemistry. 28: 6305-6309. PMID 2506925 DOI: 10.1021/Bi00441A023 |
0.539 |
|
| 1988 |
Mohan PM, Basu A, Basu S, Abraham KI, Modak MJ. DNA binding domain of Escherichia coli DNA polymerase I: identification of arginine-841 as an essential residue. Biochemistry. 27: 226-233. PMID 3280017 DOI: 10.1021/Bi00401A034 |
0.489 |
|
| 1988 |
Basu S, Basu A, Modak MJ. Pyridoxal 5'-phosphate mediated inactivation of Escherichia coli DNA polymerase I: identification of lysine-635 as an essential residue for the processive mode of DNA synthesis. Biochemistry. 27: 6710-6716. PMID 3143402 DOI: 10.1021/Bi00418A011 |
0.547 |
|
| 1988 |
Pandey VN, Modak MJ. Purification of nucleotide-linked peptide Journal of Chromatography A. 444: 133-139. PMID 3060474 DOI: 10.1016/S0021-9673(01)94016-6 |
0.353 |
|
| 1987 |
Pandey VN, Amrute SB, Satav JG, Modak MJ. Inhibition of terminal deoxynucleotidyl transferase by adenine dinucleotides. Unique inhibitory action of Ap5A. Febs Letters. 213: 204-8. PMID 3556577 DOI: 10.1016/0014-5793(87)81492-8 |
0.394 |
|
| 1987 |
Pandey V, Modak MJ. Purification of high molecular mass species of calf thymus terminal deoxynucleotidyltransferase Preparative Biochemistry. 17: 359-377. PMID 3438251 DOI: 10.1080/00327488708062502 |
0.357 |
|
| 1987 |
Pandey VN, Williams KR, Stone KL, Modak MJ. Photoaffinity labeling of the thymidine triphosphate binding domain in Escherichia coli DNA polymerase I: Identification of histidine-881 as the site of cross-linking Biochemistry. 26: 7744-7748. PMID 3322406 DOI: 10.1021/Bi00398A031 |
0.44 |
|
| 1987 |
Basu A, Modak MJ. Identification and amino acid sequence of the deoxynucleoside triphosphate binding site in Escherichia coli DNA polymerase I Biochemistry. 26: 1704-1709. PMID 3297133 DOI: 10.1021/Bi00380A032 |
0.521 |
|
| 1987 |
Pandey V, Modak MJ. Biochemistry of terminal deoxynucleotidyltransferase (TdT): Characterization and mechanism of inhibition of TdT by P1,P5-bis(5′-adenosyl) pentaphosphate Biochemistry. 26: 2033-2038. PMID 2439117 DOI: 10.1021/Bi00381A036 |
0.472 |
|
| 1984 |
Abraham KI, Modak MJ. Affinity Labeling of Escherichia coli DNA Polymerase I with Thymidine 5′-Triphosphate and 8-Azidoadenosine 5′-Triphosphate: Conditions for Optimum Labeling, Specificity, and Identification of the Labeling Site Biochemistry. 23: 1176-1182. DOI: 10.1021/Bi00301A023 |
0.401 |
|
| 1983 |
Ikehara S, Good RA, Modak MJ, Pahwa RN. Adenosine 5′-triphosphate (ATP)-mediated stimulation and suppression of DNA synthesis in lymphoid cells. II. Suppressive effect of ATP on murine T-cell functions International Journal of Immunopharmacology. 5: 567-573. PMID 6363311 DOI: 10.1016/0192-0561(83)90050-4 |
0.304 |
|
| 1983 |
Basu M, Hegde MV, Modak MJ. Synthesis of compositionally unique DNA by terminal deoxynucleotidyl transferase Biochemical and Biophysical Research Communications. 111: 1105-1112. PMID 6301484 DOI: 10.1016/0006-291X(83)91413-4 |
0.494 |
|
| 1983 |
Srivastava SK, Abraham KI, Modak MJ. The mechanism of inhibition of avian myeloblastosis virus reverse transcriptase by a dialdehyde derivative of ATP Inactivation of essential sulfhydryl group function Biochimica Et Biophysica Acta. 745: 194-201. PMID 6189518 DOI: 10.1016/0167-4838(83)90049-3 |
0.496 |
|
| 1982 |
Modak MJ, Rao K, Marcus SL. The mechanism of inorganic phosphate-mediated inhibition of calf thymus DNA polymerase beta and Rauscher leukemia virus dna polymerase. Biochemical and Biophysical Research Communications. 107: 811-9. PMID 7138520 DOI: 10.1016/0006-291X(82)90595-2 |
0.466 |
|
| 1982 |
Srivastava SK, Modak MJ. Rose Bengal mediated inhibition of DNA polymerases: mechanism of inhibition of avian myeloblastosis virus reverse transcriptase under nonoxidative conditions Biochemistry. 21: 2283-2288. PMID 6190509 DOI: 10.1021/Bi00278A035 |
0.49 |
|
| 1981 |
Modak MJ, Dumaswala UJ. Divalent cation-dependent pyridoxal 5′-phosphate inhibition of Rauscher leukemia virus DNA polymerase. Characterization and mechanism of action Biochimica Et Biophysica Acta. 654: 227-235. PMID 7284379 DOI: 10.1016/0005-2787(81)90176-3 |
0.543 |
|
| 1981 |
Srivastava SK, Gillerman E, Modak MJ. The artifactual nature of fluoride inhibition of reverse transcriptase and associated ribonuclease H Biochemical and Biophysical Research Communications. 101: 183-188. PMID 6169342 DOI: 10.1016/S0006-291X(81)80028-9 |
0.426 |
|
| 1980 |
Srivastava A, Modak MJ. Biochemistry of terminal deoxynucleotidyltransferase: identification, characterization, requirements, and active-site involvement in the catalysis of associated pyrophosphate exchange and pyrophosphorolytic activity. Biochemistry. 19: 3270-3275. PMID 6250559 DOI: 10.1021/Bi00555A026 |
0.377 |
|
| 1980 |
Modak MJ, Srivastava A, Gillerman E. Observations on the phosphonoformic acid inhibition of RNA dependent DNA polymerases. Biochemical and Biophysical Research Communications. 96: 931-938. PMID 6158948 DOI: 10.1016/0006-291X(80)91444-8 |
0.568 |
|
| 1979 |
Modak MJ. Biochemistry of terminal deoxynucleotidyltransferase. Mechanism of manganese-dependent inhibition by deoxyadenosine 5'-triphosphate and biological implications Biochemistry. 18: 2679-2684. PMID 444488 DOI: 10.1021/Bi00579A039 |
0.303 |
|
| 1979 |
Srivastava A, Modak MJ. Reverse transcriptase-associated RNase H. Part IV. Pyrophosphate does not inhibit RNase H activity of AMV DNA polymerase. Biochemical and Biophysical Research Communications. 91: 892-899. PMID 93479 DOI: 10.1016/0006-291X(79)91963-6 |
0.489 |
|
| 1978 |
Modak MJ. Biochemistry of terminal deoxynucleotidyltransferase: mechanism of inhibition by adenosine 5'-triphosphate Biochemistry. 17: 3116-3120. PMID 698189 DOI: 10.1021/Bi00608A027 |
0.436 |
|
| 1978 |
Modak MJ, Bhatt H, Seidner S, Hahn EC, Gupta S, Good RA. DNA polymerases of human tonsil and chicken bursa: Absence of a distinct B cell specific terminal deoxynucleotidyl transferase Biochemical and Biophysical Research Communications. 83: 266-273. PMID 308805 DOI: 10.1016/0006-291X(78)90426-6 |
0.372 |
|
| 1978 |
Marcus SL, Smith SW, Modak MJ. Reverse transcriptase-associated RNase H activity. II. Inhibition by natural and synthetic RNA. Journal of Virology. 27: 576-81. PMID 81313 DOI: 10.1128/Jvi.27.3.576-581.1978 |
0.456 |
|
| 1978 |
Marcus SL, Sarkar NH, Modak MJ. Template-specific requirements for DNA synthesis by the Mason-Pfizer monkey virus DNA polymerase: unique aspects. Biochimica Et Biophysica Acta. 519: 317-30. PMID 78724 DOI: 10.1016/0005-2787(78)90085-0 |
0.455 |
|
| 1977 |
Bhalla RB, Schwartz MK, Modak MJ. Selective inhibition of terminal deoxynucleotidyl transferase (TdT) by adenosine ribonucleoside triphosphate (ATP) and its application in the detection of TdT in human leukemia. Biochemical and Biophysical Research Communications. 76: 1056-1061. PMID 268958 DOI: 10.1016/0006-291X(77)90963-9 |
0.366 |
|
| 1977 |
Hadidi A, Diener TO, Modak M. Synthesis of DNA transcripts of potato spindle tuber viroid Febs Letters. 75: 123-127. PMID 67055 DOI: 10.1016/0014-5793(77)80067-7 |
0.483 |
|
| 1976 |
Marcus SL, Smith SW, Jarowski CI, Modak MJ. Terminal deoxyribonucleotidyl transferase activity in acute undifferentiated leukemia. Biochemical and Biophysical Research Communications. 70: 37-44. PMID 1275943 DOI: 10.1016/0006-291X(76)91105-0 |
0.406 |
|
| 1976 |
Bhalla RB, Geraci D, Modak MJ, Prensky W, Marcus SL. Preparation of (125I)-dCTP and its use as a substrate for RNA- and DNA-directed DNA synthesis. Biochemical and Biophysical Research Communications. 72: 513-21. PMID 62576 DOI: 10.1016/S0006-291X(76)80071-X |
0.512 |
|
| 1976 |
Marcus SL, Modak MJ. Observations on template-specific conditions for DNA synthesis by avian myeloblastosis virus DNA polymerase. Nucleic Acids Research. 3: 1473-86. PMID 60740 DOI: 10.1093/Nar/3.6.1473 |
0.506 |
|
| 1976 |
Modak MJ. Observations on the pyridoxal 5'-phosphate inhibition of DNA polymerases. Biochemistry. 15: 3620-3626. PMID 60130 DOI: 10.1021/Bi00661A033 |
0.506 |
|
| 1976 |
Marcus SL, Sarkar NH, Modak MJ. Purification and properties of murine mammary tumor virus DNA polymerase. Virology. 71: 242-54. PMID 58470 DOI: 10.1016/0042-6822(76)90109-4 |
0.538 |
|
| 1974 |
Marcus SL, Modak MJ, Cavalieri LF. Purification of avian myeloblastosis virus DNA polymerase by affinity chromatography on polycytidylate-agarose. Journal of Virology. 14: 853-9. PMID 4138457 DOI: 10.1128/Jvi.14.4.853-859.1974 |
0.523 |
|
| 1974 |
Cavalieri LF, Modak MJ, Marcus SL. Evidence for allosterism in in vitro DNA synthesis on RNA templates. Proceedings of the National Academy of Sciences of the United States of America. 71: 858-62. PMID 4132534 DOI: 10.1073/Pnas.71.3.858 |
0.531 |
|
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