Walter F. Mangel - Publications

Stony Brook University, Stony Brook, NY, United States 
Pharmacology, Biochemistry

58 high-probability publications. We are testing a new system for linking publications to authors. You can help! If you notice any inaccuracies, please sign in and mark papers as correct or incorrect matches. If you identify any major omissions or other inaccuracies in the publication list, please let us know.

Year Citation  Score
2016 Turkin A, Zhang L, Marcozzi A, Mangel WF, Herrmann A, van Oijen AM. Speeding up biomolecular interactions by molecular sledding. Chemical Science (Royal Society of Chemistry : 2010). 7: 916-920. PMID 26913169 DOI: 10.1039/C5Sc03063C  0.342
2016 Mangel WF, McGrath WJ, Xiong K, Graziano V, Blainey PC. Molecular sled is an eleven-amino acid vehicle facilitating biochemical interactions via sliding components along DNA. Nature Communications. 7: 10202. PMID 26831565 DOI: 10.1038/Ncomms10202  0.43
2015 Geertsema HJ, Schulte AC, Spenkelink LM, McGrath WJ, Morrone SR, Sohn J, Mangel WF, Robinson A, van Oijen AM. Single-molecule imaging at high fluorophore concentrations by local activation of dye. Biophysical Journal. 108: 949-56. PMID 25692599 DOI: 10.1016/J.Bpj.2014.12.019  0.344
2014 Mangel WF, San Martín C. Structure, function and dynamics in adenovirus maturation. Viruses. 6: 4536-70. PMID 25421887 DOI: 10.3390/V6114536  0.369
2014 Pérez-Berná AJ, Mangel WF, McGrath WJ, Graziano V, Flint J, San Martín C. Processing of the l1 52/55k protein by the adenovirus protease: a new substrate and new insights into virion maturation. Journal of Virology. 88: 1513-24. PMID 24227847 DOI: 10.1128/Jvi.02884-13  0.372
2013 Baniecki ML, McGrath WJ, Mangel WF. Regulation of a viral proteinase by a peptide and DNA in one-dimensional space: III. atomic resolution structure of the nascent form of the adenovirus proteinase. The Journal of Biological Chemistry. 288: 2081-91. PMID 23043139 DOI: 10.1074/Jbc.M112.407429  0.74
2013 Blainey PC, Graziano V, Pérez-Berná AJ, McGrath WJ, Flint SJ, San Martín C, Xie XS, Mangel WF. Regulation of a viral proteinase by a peptide and DNA in one-dimensional space: IV. viral proteinase slides along DNA to locate and process its substrates. The Journal of Biological Chemistry. 288: 2092-102. PMID 23043138 DOI: 10.1074/Jbc.M112.407460  0.42
2013 Graziano V, Luo G, Blainey PC, Pérez-Berná AJ, McGrath WJ, Flint SJ, San Martín C, Xie XS, Mangel WF. Regulation of a viral proteinase by a peptide and DNA in one-dimensional space: II. adenovirus proteinase is activated in an unusual one-dimensional biochemical reaction. The Journal of Biological Chemistry. 288: 2068-80. PMID 23043137 DOI: 10.1074/Jbc.M112.407312  0.475
2013 Graziano V, McGrath WJ, Suomalainen M, Greber UF, Freimuth P, Blainey PC, Luo G, Xie XS, Mangel WF. Regulation of a viral proteinase by a peptide and DNA in one-dimensional space: I. binding to DNA AND to hexon of the precursor to protein VI, pVI, of human adenovirus. The Journal of Biological Chemistry. 288: 2059-67. PMID 23043136 DOI: 10.1074/Jbc.M112.377150  0.431
2013 Turkin A, Mangel WF, van Oijen AM. Single-Molecule Studies of Adenovirus Maturation Biophysical Journal. 104: 178a-179a. DOI: 10.1016/J.Bpj.2012.11.1004  0.391
2009 Blainey PC, Luo G, Kou SC, Mangel WF, Verdine GL, Bagchi B, Xie XS. Nonspecifically bound proteins spin while diffusing along DNA. Nature Structural & Molecular Biology. 16: 1224-9. PMID 19898474 DOI: 10.1038/Nsmb.1716  0.364
2009 Pérez-Berná AJ, Marabini R, Scheres SH, Menéndez-Conejero R, Dmitriev IP, Curiel DT, Mangel WF, Flint SJ, San Martín C. Structure and uncoating of immature adenovirus. Journal of Molecular Biology. 392: 547-57. PMID 19563809 DOI: 10.1016/J.Jmb.2009.06.057  0.366
2007 Mangel WF, McGrath WJ. Cofactors of the adenovirus proteinase: measuring equilibrium dissociation constants and stoichiometries of binding. Methods in Molecular Medicine. 131: 269-80. PMID 17656790 DOI: 10.1385/1-59745-277-7:269  0.494
2007 Mangel WF, McGrath WJ. Assay for the adenovirus proteinase: purification of the enzyme and synthesis of a fluorogenic substrate. Methods in Molecular Medicine. 131: 257-67. PMID 17656789 DOI: 10.1385/1-59745-277-7:257  0.371
2006 Graziano V, McGrath WJ, Yang L, Mangel WF. SARS CoV main proteinase: The monomer-dimer equilibrium dissociation constant. Biochemistry. 45: 14632-41. PMID 17144656 DOI: 10.1021/Bi061746Y  0.347
2006 Graziano V, McGrath WJ, DeGruccio AM, Dunn JJ, Mangel WF. Enzymatic activity of the SARS coronavirus main proteinase dimer. Febs Letters. 580: 2577-83. PMID 16647061 DOI: 10.1016/J.Febslet.2006.04.004  0.356
2005 Bajpayee NS, McGrath WJ, Mangel WF. Interaction of the adenovirus proteinase with protein cofactors with high negative charge densities. Biochemistry. 44: 8721-9. PMID 15952779 DOI: 10.1021/Bi0502240  0.455
2005 Gupta S, Mangel WF, Sullivan M, Takamoto K, Chance MR. Technical Reports: Mapping a Functional Viral Protein in Solution Using Synchrotron X-ray Footprinting Technology Synchrotron Radiation News. 18: 25-34. DOI: 10.1080/08940880500457537  0.303
2004 Gupta S, Mangel WF, McGrath WJ, Perek JL, Lee DW, Takamoto K, Chance MR. DNA binding provides a molecular strap activating the adenovirus proteinase. Molecular & Cellular Proteomics : McP. 3: 950-9. PMID 15220401 DOI: 10.1074/Mcp.M400037-Mcp200  0.453
2004 Brown MT, Mangel WF. Interaction of actin and its 11-amino acid C-terminal peptide as cofactors with the adenovirus proteinase. Febs Letters. 563: 213-8. PMID 15063751 DOI: 10.1016/S0014-5793(04)00285-6  0.452
2003 Mangel WF, Baniecki ML, McGrath WJ. Specific interactions of the adenovirus proteinase with the viral DNA, an 11-amino-acid viral peptide, and the cellular protein actin. Cellular and Molecular Life Sciences : Cmls. 60: 2347-55. PMID 14625681 DOI: 10.1007/S00018-003-2318-2  0.75
2003 Cao W, Baniecki ML, McGrath WJ, Bao C, Deming CB, Rade JJ, Lowenstein CJ, Mangel WF. Nitric oxide inhibits the adenovirus proteinase in vitro and viral infectivity in vivo. Faseb Journal : Official Publication of the Federation of American Societies For Experimental Biology. 17: 2345-6. PMID 14525937 DOI: 10.1096/Fj.03-0396Fje  0.703
2003 McGrath WJ, Ding J, Didwania A, Sweet RM, Mangel WF. Crystallographic structure at 1.6-A resolution of the human adenovirus proteinase in a covalent complex with its 11-amino-acid peptide cofactor: insights on a new fold. Biochimica Et Biophysica Acta. 1648: 1-11. PMID 12758141 DOI: 10.1016/S1570-9639(03)00024-4  0.379
2002 Baniecki ML, McGrath WJ, Dauter Z, Mangel WF. Adenovirus proteinase: crystallization and preliminary X-ray diffraction studies to atomic resolution. Acta Crystallographica. Section D, Biological Crystallography. 58: 1462-4. PMID 12198302 DOI: 10.1107/S0907444902008429  0.721
2002 Brown MT, McBride KM, Baniecki ML, Reich NC, Marriott G, Mangel WF. Actin can act as a cofactor for a viral proteinase in the cleavage of the cytoskeleton. The Journal of Biological Chemistry. 277: 46298-303. PMID 12191991 DOI: 10.1074/Jbc.M202988200  0.708
2002 McGrath WJ, Aherne KS, Mangel WF. In the virion, the 11-amino-acid peptide cofactor pVIc is covalently linked to the adenovirus proteinase. Virology. 296: 234-40. PMID 12069522 DOI: 10.1006/Viro.2002.1394  0.369
2001 McGrath WJ, Baniecki ML, Peters E, Green DT, Mangel WF. Roles of two conserved cysteine residues in the activation of human adenovirus proteinase. Biochemistry. 40: 14468-74. PMID 11724559 DOI: 10.1021/Bi011562D  0.737
2001 McGrath WJ, Baniecki ML, Li C, McWhirter SM, Brown MT, Toledo DL, Mangel WF. Human adenovirus proteinase: DNA binding and stimulation of proteinase activity by DNA. Biochemistry. 40: 13237-45. PMID 11683632 DOI: 10.1021/Bi0111653  0.73
2001 Baniecki ML, McGrath WJ, McWhirter SM, Li C, Toledo DL, Pellicena P, Barnard DL, Thorn KS, Mangel WF. Interaction of the human adenovirus proteinase with its 11-amino acid cofactor pVIc. Biochemistry. 40: 12349-56. PMID 11591154 DOI: 10.1021/Bi0109008  0.747
2001 Pang YP, Xu K, Kollmeyer TM, Perola E, McGrath WJ, Green DT, Mangel WF. Discovery of a new inhibitor lead of adenovirus proteinase: Steps toward selective, irreversible inhibitors of cysteine proteinases Febs Letters. 502: 93-97. PMID 11583118 DOI: 10.1016/S0014-5793(01)02672-2  0.315
2001 Mangel WF, Brown MT, Baniecki ML, Barnard D, McGrath WJ. Prevention of viral drug resistance by novel combination therapy. Current Opinion in Investigational Drugs (London, England : 2000). 2: 613-6. PMID 11569932  0.68
2001 Mangel WF, McGrath WJ, Brown MT, Baniecki ML, Barnard DL, Pang YP. A new form of antiviral combination therapy predicted to prevent resistance from arising, and a model system to test it. Current Medicinal Chemistry. 8: 933-9. PMID 11375760 DOI: 10.2174/0929867013372742  0.707
2000 Williams J, McGrath WJ, Mangel WF. Sensitive method to identify and characterize proteinases in situ after SDS-PAGE Biotechniques. 29: 1108-1113. PMID 11084874 DOI: 10.2144/00295Rr07  0.308
1997 Mangel WF, Toledo DL, Ding J, Sweet RM, McGrath WJ. Temporal and spatial control of the adenovirus proteinase by both a peptide and the viral DNA Trends in Biochemical Sciences. 22: 393-398. PMID 9357315 DOI: 10.1016/S0968-0004(97)01123-7  0.436
1996 Brown MT, McGrath WJ, Toledo DL, Mangel WF. Different modes of inhibition of human adenovirus proteinase, probably a cysteine proteinase, by bovine pancreatic trypsin inhibitor. Febs Letters. 388: 233-7. PMID 8690094 DOI: 10.1016/0014-5793(96)00569-8  0.425
1996 Ding J, McGrath WJ, Sweet RM, Mangel WF. Crystal structure of the human adenovirus proteinase with its 11 amino acid cofactor Embo Journal. 15: 1778-1783. PMID 8617222 DOI: 10.1002/J.1460-2075.1996.Tb00526.X  0.438
1996 McGrath WJ, Abola AP, Toledo DL, Brown MT, Mangel WF. Characterization of human adenovirus proteinase activity in disrupted virus particles. Virology. 217: 131-8. PMID 8599197 DOI: 10.1006/Viro.1996.0100  0.431
1996 Mangel WF, Toledo DL, Brown MT, Martin JH, McGrath WJ. Characterization of three components of human adenovirus proteinase activity in vitro. The Journal of Biological Chemistry. 271: 536-43. PMID 8550615 DOI: 10.1074/Jbc.271.1.536  0.449
1994 Mangel WF, Toledo DL, Brown MT, Worzalla K, Lee M, Dunn JJ. Omptin: an Escherichia coli outer membrane proteinase that activates plasminogen. Methods in Enzymology. 244: 384-99. PMID 7845221 DOI: 10.1016/0076-6879(94)44029-8  0.372
1993 Mangel WF, McGrath WJ, Toledo DL, Anderson CW. Viral DNA and a viral peptide can act as cofactors of adenovirus virion proteinase activity Nature. 361: 274-275. PMID 8423855 DOI: 10.1038/361274A0  0.459
1992 Rothe G, Klingel S, Assfalg-Machleidt I, Machleidt W, Zirkelbach C, Banati RB, Mangel WF, Valet G. Flow cytometric analysis of protease activities in vital cells. Biological Chemistry Hoppe-Seyler. 373: 547-54. PMID 1381188 DOI: 10.1515/Bchm3.1992.373.2.547  0.306
1991 Ramakrishnan V, Patthy L, Mangel WF. Conformation of Lys-plasminogen and the kringle 1-3 fragment of plasminogen analyzed by small-angle neutron scattering Biochemistry. 30: 3963-3969. PMID 2018765 DOI: 10.1021/Bi00230A023  0.381
1990 Mangel WF, Singer PT, Cyr DM, Umland TC, Toledo DL, Stroud RM, Pflugrath JW, Sweet RM. Structure of an acyl-enzyme intermediate during catalysis: (Guanidinobenzoyl)trypsint Biochemistry®. 29: 8351-8357. PMID 2252895 DOI: 10.1021/Bi00488A022  0.36
1990 Mangel WF, Lin B, Ramakrishnan V. Characterization of an extremely large, ligand-induced conformational change in plasminogen Science. 248: 69-73. PMID 2108500 DOI: 10.1126/Science.2108500  0.339
1987 Morliere P, Mangel WF, Santus R, Huppe G, Reyftmann JP, Kohen E. Interactionof tetrapyrrolic rings with rhodamine 110 and 123 and with rhodamine 110 derivatives bearing a peptidic side chain Biochemical and Biophysical Research Communications. 146: 107-113. PMID 3038101 DOI: 10.1016/0006-291X(87)90697-8  0.3
1985 Bok RA, Mangel WF. Quantitative characterization of the binding of plasminogen to intact fibrin clots, lysine-sepharose, and fibrin cleaved by plasmin Biochemistry. 24: 3279-3286. PMID 3161540 DOI: 10.1021/Bi00334A031  0.391
1984 Leytus SP, Toledo DL, Mangel WF. Theory and experimental method for determining individual kinetic constants of fast-acting, irreversible proteinase inhibitors Biochimica Et Biophysica Acta (Bba)/Protein Structure and Molecular. 788: 74-86. PMID 6204689 DOI: 10.1016/0167-4838(84)90299-1  0.302
1983 Leytus SP, Melhado LL, Mangel WF. Rhodamine-based compounds as fluorogenic substrates for serine proteinases Biochemical Journal. 209: 299-307. PMID 6342611 DOI: 10.1042/Bj2090299  0.333
1983 Leytus SP, Peltz SW, Mangel WF. Adaptation of acyl-enzyme kinetic theory and an experimental method for evaluating the kinetics of fast-acting, irreversible protease inhibitors Biochimica Et Biophysica Acta (Bba)/Protein Structure and Molecular. 742: 409-418. PMID 6337638 DOI: 10.1016/0167-4838(83)90328-X  0.323
1983 Leytus SP, Patterson WL, Mangel WF. New class of sensitive and selective fluorogenic substrates for serine proteinases. Amino acid and dipeptide derivatives of rhodamine Biochemical Journal. 215: 253-260. PMID 6228222 DOI: 10.1042/Bj2150253  0.352
1982 Peltz SW, Hardt TA, Mangel WF. Positive regulation of activation of plasminogen by urokinase: Differences in Km for (glutamic acid)-plasminogen and lysine-plasminogen and effect of certain α,ω-amino acids Biochemistry. 21: 2798-2804. PMID 6212078 DOI: 10.1021/Bi00540A035  0.409
1982 Lee Melhado L, Peltz SW, Leytus SP, Mangel WF. p-Guanidinobenzoic acid esters of fluorescein as active-site titrants of serine proteases Journal of the American Chemical Society. 104: 7299-7306. DOI: 10.1002/Chin.198312365  0.352
1981 Mangel WF, Campbell Livingston D, Brocklehurst JR, Cannon JF, Leytus SP, Peltz SW, Peltz GA, Liu HY. [34] A new active-site titrant of serine proteases Methods in Enzymology. 80: 414-424. PMID 7043196 DOI: 10.1016/S0076-6879(81)80036-5  0.363
1981 Livingston DC, Brocklehurst JR, Cannon JF, Leytus SP, Wehrly JA, Peltz SW, Peltz GA, Mangel WF. Synthesis and characterization of a new fluorogenic active-site titrant of serine proteases Biochemistry. 20: 4298-4306. PMID 6456760 DOI: 10.1021/Bi00518A010  0.315
1981 Leytus SP, Bowles LK, Konisky J, Mangel WF. Activation of plasminogen to plasmin by a protease associated with the outer membrane of Escherichia coli Proceedings of the National Academy of Sciences of the United States of America. 78: 1485-1489. PMID 6453346 DOI: 10.1073/Pnas.78.3.1485  0.315
1980 Liu HY, Peltz GA, Leytus SP, Livingston C, Brocklehurst J, Mangel WF. Sensitive assay for plasminogen activator of transformed cells Proceedings of the National Academy of Sciences of the United States of America. 77: 3796-3800. PMID 6449002 DOI: 10.1073/Pnas.77.7.3796  0.315
1974 Mangel WF. Initial steps in the large-scale purification of Escherichia coli deoxyribonucleic acid-dependent ribonucleic acid polymerase Archives of Biochemistry and Biophysics. 163: 172-177. PMID 4604619 DOI: 10.1016/0003-9861(74)90466-4  0.308
1972 Hinkle DC, Mangel WF, Chamberlin MJ. Studies of the binding of Escherichia coli RNA polymerase to DNA. IV. The effect of rifampicin on binding and on RNA chain initiation. Journal of Molecular Biology. 70: 209-20. PMID 4562315 DOI: 10.1016/0022-2836(72)90534-7  0.327
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