Year |
Citation |
Score |
2013 |
Christensen KE, Deng L, Leung KY, Arning E, Bottiglieri T, Malysheva OV, Caudill MA, Krupenko NI, Greene ND, Jerome-Majewska L, MacKenzie RE, Rozen R. A novel mouse model for genetic variation in 10-formyltetrahydrofolate synthetase exhibits disturbed purine synthesis with impacts on pregnancy and embryonic development Human Molecular Genetics. 22: 3705-3719. PMID 23704330 DOI: 10.1093/Hmg/Ddt223 |
0.363 |
|
2009 |
Christensen KE, Rohlicek CV, Andelfinger GU, Michaud J, Bigras JL, Richter A, Mackenzie RE, Rozen R. The MTHFD1 p.Arg653Gln variant alters enzyme function and increases risk for congenital heart defects. Human Mutation. 30: 212-20. PMID 18767138 DOI: 10.1002/Humu.20830 |
0.386 |
|
2008 |
Christensen KE, MacKenzie RE. Chapter 14 Mitochondrial Methylenetetrahydrofolate Dehydrogenase, Methenyltetrahydrofolate Cyclohydrolase, and Formyltetrahydrofolate Synthetases Vitamins and Hormones. 79: 393-410. PMID 18804703 DOI: 10.1016/S0083-6729(08)00414-7 |
0.505 |
|
2006 |
Christensen KE, MacKenzie RE. Mitochondrial one-carbon metabolism is adapted to the specific needs of yeast, plants and mammals Bioessays. 28: 595-605. PMID 16700064 DOI: 10.1002/Bies.20420 |
0.392 |
|
2005 |
Patel H, Di Pietro E, Mejia N, MacKenzie RE. NAD- and NADP-dependent mitochondrially targeted methylenetetrahydrofolate dehydrogenase-cyclohydrolases can rescue mthfd2 null fibroblasts Archives of Biochemistry and Biophysics. 442: 133-139. PMID 16150419 DOI: 10.1016/J.Abb.2005.07.022 |
0.672 |
|
2005 |
Christensen KE, Mirza IA, Berghuis AM, MacKenzie RE. Magnesium and phosphate ions enable NAD binding to methylenetetrahydrofolate dehydrogenase-methenyltetrahydrofolate cyclohydrolase Journal of Biological Chemistry. 280: 34316-34323. PMID 16100107 DOI: 10.1074/Jbc.M505210200 |
0.363 |
|
2005 |
Christensen KE, Patel H, Kuzmanov U, Mejia NR, MacKenzie RE. Disruption of the Mthfd1 gene reveals a monofunctional 10- formyltetrahydrofolate synthetase in mammalian mitochondria Journal of Biological Chemistry. 280: 7597-7602. PMID 15611115 DOI: 10.1074/Jbc.M409380200 |
0.475 |
|
2004 |
Di Pietro E, Wang XL, MacKenzie RE. The expression of mitochondrial methylenetetrahydrofolate dehydrogenase-cyclohydrolase supports a role in rapid cell growth Biochimica Et Biophysica Acta - General Subjects. 1674: 78-84. PMID 15342116 DOI: 10.1016/J.Bbagen.2004.06.014 |
0.631 |
|
2003 |
Baggott JE, MacKenzie RE. 5,10-Methenyltetrahydrofolate cyclohydrolase, rat liver and chemically catalysed formation of 5-formyltetrahydrofolate Biochemical Journal. 374: 773-778. PMID 12793858 DOI: 10.1042/Bj20021970 |
0.301 |
|
2003 |
Patel H, Di Pietro E, MacKenzie RE. Mammalian fibroblasts lacking mitochondrial NAD+-dependent methylenetetrahydrofolate dehydrogenase-cyclohydrolase are glycine auxotrophs Journal of Biological Chemistry. 278: 19436-19441. PMID 12646567 DOI: 10.1074/Jbc.M301718200 |
0.64 |
|
2002 |
Gao YS, Vrielink A, MacKenzie R, Sztul E. A novel type of regulation of the vimentin intermediate filament cytoskeleton by a Golgi protein. European Journal of Cell Biology. 81: 391-401. PMID 12160147 DOI: 10.1078/0171-9335-00260 |
0.304 |
|
2002 |
Patel H, Christensen KE, Mejia N, MacKenzie RE. Mammalian mitochondrial methylenetetrahydrofolate dehydrogenase-cyclohydrolase derived from a trifunctional methylenetetrahydrofolate dehydrogenase-cyclohydrolase-synthetase Archives of Biochemistry and Biophysics. 403: 145-148. PMID 12061812 DOI: 10.1016/S0003-9861(02)00203-5 |
0.329 |
|
2002 |
Di Pietro E, Sirois J, Tremblay ML, MacKenzie RE. Mitochondrial NAD-dependent methylenetetrahydrofolate dehydrogenase-methenyltetrahydrofolate cyclohydrolase is essential for embryonic development Molecular and Cellular Biology. 22: 4158-4166. PMID 12024029 DOI: 10.1128/Mcb.22.12.4158-4166.2002 |
0.651 |
|
2002 |
Sundararajan S, MacKenzie RE. Residues involved in the mechanism of the bifunctional methylenetetrahydrofolate dehydrogenase-cyclohydrolase: The roles of glutamine 100 and aspartate 125 Journal of Biological Chemistry. 277: 18703-18709. PMID 11904299 DOI: 10.1074/Jbc.M200127200 |
0.438 |
|
2000 |
Pawelek PD, Allaire M, Cygler M, MacKenzie RE. Channeling efficiency in the bifunctional methylenetetrahydrofolate dehydrogenase/cyclohydrolase domain: The effects of site-directed mutagenesis of NADP binding residues Biochimica Et Biophysica Acta - Protein Structure and Molecular Enzymology. 1479: 59-68. PMID 11004530 DOI: 10.1016/S0167-4838(00)00058-3 |
0.398 |
|
2000 |
Schmidt A, Wu H, Mackenzie RE, Chen VJ, Bewly JR, Ray JE, Toth JE, Cygler M. Structures of three inhibitor complexes provide insight into the reaction mechanism of the human methylenetetrahydrofolate dehydrogenase/cyclohydrolase Biochemistry. 39: 6325-6335. PMID 10828945 DOI: 10.1021/Bi992734Y |
0.475 |
|
2000 |
Kohls D, Sulea T, Purisima EO, MacKenzie RE, Vrielink A. The crystal structure of the formiminotransferase domain of formiminotransferase-cyclodeaminase: Implications for substrate channeling in a bifunctional enzyme Structure. 8: 35-46. PMID 10673422 DOI: 10.1016/S0969-2126(00)00078-2 |
0.462 |
|
1999 |
Kohls D, Croteau N, Mejia N, MacKenzie RE, Vrielink A. Crystallization and preliminary X-ray analysis of the formiminotransferase domain from the bifunctional enzyme formiminotransferase-cyclodeaminase Acta Crystallographica Section D: Biological Crystallography. 55: 1206-1208. PMID 10329787 DOI: 10.1107/S0907444999003601 |
0.443 |
|
1998 |
Allaire M, Li Y, MacKenzie RE, Cygler M. The 3-D structure of a folate-dependent dehydrogenase/cyclohydrolase bifunctional enzyme at 1.5 Å resolution Structure. 6: 173-182. PMID 9519408 DOI: 10.1016/S0969-2126(98)00019-7 |
0.452 |
|
1998 |
Pawelek PD, MacKenzie RE. Methenyltetrahydrofolate cyclohydrolase is rate limiting for the enzymatic conversion of 10-formyltetrahydrofolate to 5,10- methylenetetrahydrofolate in bifunctional dehydrogenase-cyclohydrolase enzymes Biochemistry. 37: 1109-1115. PMID 9454603 DOI: 10.1021/Bi971906T |
0.503 |
|
1997 |
Mackenzie RE. Mitochondrial NAD-dependent methylenetetrahydrofolate dehydrogenase- methenyltetrahydrofolate cyclohydrolase Methods in Enzymology. 281: 171-177. PMID 9250981 DOI: 10.1016/S0076-6879(97)81023-3 |
0.489 |
|
1997 |
Murley LL, MacKenzie RE. Monofunctional domains of formiminotransferase-cyclodeaminase retain similar conformational stabilities outside the bifunctional octamer Biochimica Et Biophysica Acta - Protein Structure and Molecular Enzymology. 1338: 223-232. PMID 9128140 DOI: 10.1016/S0167-4838(96)00208-7 |
0.372 |
|
1996 |
Allaire M, Li Y, Mejia NR, Pelletier JN, MacKenzie RE, Cygler M. Crystallization of the bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase domain of the human trifunctional enzyme Proteins: Structure, Function and Genetics. 26: 479-480. PMID 8990501 DOI: 10.1002/(Sici)1097-0134(199612)26:4<479::Aid-Prot9>3.0.Co;2-6 |
0.614 |
|
1996 |
Pawelek PD, MacKenzie RE. Methylenetetrahydrofolate dehydrogenase-cyclohydrolase from Photobacterium phosphoreum shares properties with a mammalian mitochondrial homologue Biochimica Et Biophysica Acta - Protein Structure and Molecular Enzymology. 1296: 47-54. PMID 8765228 DOI: 10.1016/0167-4838(96)00052-0 |
0.507 |
|
1996 |
Pelletier JN, Mackenzie RE. Methenyltetrahydrofolate cyclohydrolase catalyzes the synthesis of (6S)-5-formyltetrahydrofolate Bioorganic Chemistry. 24: 220-228. DOI: 10.1006/Bioo.1996.0020 |
0.622 |
|
1995 |
Tremblay GB, MacKenzie RE. Primary structure of a folate-dependent trifunctional enzyme from Spodoptera frugiperda Bba - Gene Structure and Expression. 1261: 129-133. PMID 7893749 DOI: 10.1016/0167-4781(95)00004-Z |
0.428 |
|
1995 |
Murley LL, MacKenzie RE. The two monofunctional domains of octameric formiminotransferase- cyclodeaminase exist as dimers Biochemistry. 34: 10358-10364. PMID 7654689 DOI: 10.1021/Bi00033A006 |
0.412 |
|
1995 |
Tremblay GB, Sohi SS, Retnakaran A, MacKenzie RE. NAD-dependent methylenetetrahydrofolate dehydrogenase-methenyltetrahydrofolate cyclohydrolase is targeted to the cytoplasm in insect cell lines Febs Letters. 368: 177-182. PMID 7615077 DOI: 10.1016/0014-5793(95)00640-U |
0.449 |
|
1995 |
Pelletier JN, MacKenzie RE. Binding and interconversion of tetrahydrofolates at a single site in the bifunctional methylenetetrahydrofolate dehydrogenase/cyclohydrolase Biochemistry. 34: 12673-12680. PMID 7548019 DOI: 10.1021/Bi00039A025 |
0.642 |
|
1994 |
Pelletier JN, MacKenzie RE. Binding to the 2′,5′-ADP subsite stimulates cyclohydrolase activity of human NADP+-dependent methylenetetrahydrofolate dehydrogenase/cyclohydrolase Biochemistry. 33: 1900-1906. PMID 8110794 DOI: 10.1021/Bi00173A037 |
0.652 |
|
1993 |
Peri KG, MacKenzie RE. NAD+-dependent methylenetetrahydrofolate dehydrogenase-cyclohydrolase: Detection of the mRNA in normal murine tissues and transcriptional regulation of the gene in cell lines Bba - Gene Structure and Expression. 1171: 281-287. PMID 8424951 DOI: 10.1016/0167-4781(93)90066-M |
0.403 |
|
1993 |
MacKenzie RE. NAD-Dependent Methylenetetrahydrofolate Dehydrogenase-Methenyltetrahydrofolate Cyclohydrolase Is the Mammalian Homolog of the Mitochondrial Enzyme Encoded by the Yeast MIS1 Gene Biochemistry. 32: 11118-11123. PMID 8218174 DOI: 10.1021/Bi00092A022 |
0.525 |
|
1993 |
Murley LL, Mejia NR, MacKenzie RE. The nucleotide sequence of porcine formiminotransferase cyclodeaminase. Expression and purification from Escherichia coli Journal of Biological Chemistry. 268: 22820-22824. PMID 7901203 |
0.369 |
|
1992 |
Tremblay GB, Mejia NR, MacKenzie RE. The NADP-dependent methylenetetrahydrofolate dehydrogenase- methenyltetrahydrofolate cyclohydrolase-formyltetrahydrofolate synthetase is not expressed in Spodoptera frugiperda cells Journal of Biological Chemistry. 267: 8281-8285. PMID 1569082 |
0.412 |
|
1992 |
Yang XM, MacKenzie RE. Expression of human NAD-dependent methylenetetrahydrofolate dehydrogenase-methenyltetrahydrofolate cyclohydrolase in Escherichia coli: Purification and partial characterization Protein Expression and Purification. 3: 256-262. PMID 1392622 DOI: 10.1016/1046-5928(92)90022-O |
0.512 |
|
1991 |
Bélanger C, MacKenzie RE. Structural organization of the murine gene encoding NAD-dependent methylenetetrahydrofolate dehydrogenase-methenyltetrahydrofolate cyclohydrolase Gene. 97: 283-288. PMID 1999293 DOI: 10.1016/0378-1119(91)90064-I |
0.385 |
|
1991 |
Hum DW, MacKenzie RE. Expression of active domains of a human folate-dependent trifunctional enzyme in Escherichia coli Protein Engineering. 4: 493-500. PMID 1881876 DOI: 10.1093/Protein/4.4.493 |
0.462 |
|
1991 |
Peri KG, MacKenzie RE. Transcriptional regulation of murine NADP+-dependent methylenetetrahydrofolate dehydrogenase-cyclohydrolase-synthetase Febs Letters. 294: 113-115. PMID 1720740 DOI: 10.1016/0014-5793(91)81354-B |
0.349 |
|
1989 |
Peri KG, Belanger C, Mackenzie RE. Nucleotide sequence of the human NAD-dependent methylene tetrahydrofolate dehydrogenase-cyclohydrolase Nucleic Acids Research. 17: 8853. PMID 2587219 DOI: 10.1093/Nar/17.21.8853 |
0.308 |
|
1989 |
Findlay WA, Zarkadas CG, MacKenzie RE. An improved procedure for the purification of formiminotransferase-cyclodeaminase from pig liver. Kinetics of the transferase activity with tetrahydropteroylpolyglutamates Biochimica Et Biophysica Acta (Bba)/Protein Structure and Molecular. 999: 52-57. PMID 2572277 DOI: 10.1016/0167-4838(89)90029-0 |
0.385 |
|
1988 |
Findlay WA, MacKenzie RE. Renaturation of formiminotransferase - cyclodeaminase from guanidine hydrochloride. Quaternary structure requirements for the activities and polyglutamate specificity Biochemistry. 27: 3404-3408. PMID 3390440 DOI: 10.1021/Bi00409A042 |
0.481 |
|
1988 |
Green JM, MacKenzie RE, Matthews RG. Substrate flux through methylenetetrahydrofolate dehydrogenase: Predicted effects of the concentration of methylenetetrahydrofolate on its partitioning into pathways leading to nucleotide biosynthesis or methionine regeneration Biochemistry. 27: 8014-8022. PMID 3266075 DOI: 10.1021/Bi00421A007 |
0.44 |
|
1988 |
Mejia NR, MacKenzie RE. NAD-dependent methylenetetrahydrofolate dehydrogenase-methenyltetrahydrofolate cyclohydrolase in transformed cells is a mitochondrial enzyme Biochemical and Biophysical Research Communications. 155: 1-6. PMID 3261979 DOI: 10.1016/S0006-291X(88)81040-4 |
0.477 |
|
1988 |
Rios-Orlandi EM, MacKenzie RE. The activities of the NAD-dependent methylenetetrahydrofolate dehydrogenase-methenyltetrahydrofolate cyclohydrolase from ascites tumor cells are kinetically independent Journal of Biological Chemistry. 263: 4662-4667. PMID 3258307 |
0.42 |
|
1988 |
MacKenzie RE, Mejia N, Yang XM. Methylenetetrahydrofolate dehydrogenases in normal and transformed mammalian cells Advances in Enzyme Regulation. 27: 15-24,in3-in6,25-29. PMID 3074630 DOI: 10.1016/0065-2571(88)90007-6 |
0.508 |
|
1988 |
Hum DW, Bell AW, Rozen R, MacKenzie RE. Primary structure of a human trifunctional enzyme. Isolation of a cDNA encoding methylenetetrahydrofolate dehydrogenase-methenyltetrahydrofolate cyclohydrolase-formyltetrahydrofolate synthetase Journal of Biological Chemistry. 263: 15946-15950. PMID 3053686 |
0.345 |
|
1988 |
Gardam MA, Mejia NR, MacKenzie RE. The NADP-dependent trifunctional methylenetetrahydrofolate dehydrogenase purified from mouse liver is immunologically distinct from the mouse NADP-dependent bifunctional enzyme Biochemistry and Cell Biology. 66: 66-70. PMID 2453205 DOI: 10.1139/O88-008 |
0.432 |
|
1987 |
Bertrand R, MacKenzie RE, Jolivet J. Human liver methenyltetrahydrofolate synthetase: improved purification and increased affinity for folate polyglutamate substrates Biochimica Et Biophysica Acta (Bba)/Protein Structure and Molecular. 911: 154-161. PMID 3801490 DOI: 10.1016/0167-4838(87)90004-5 |
0.453 |
|
1987 |
Findlay WA, MacKenzie RE. Dissociation of the octameric bifunctional enzyme formiminotransferase-cyclodeaminase in urea. Isolation of two monofunctional dimers Biochemistry. 26: 1948-1954. PMID 3593701 DOI: 10.1021/Bi00381A024 |
0.418 |
|
1986 |
Rios-Orlandi EM, Zarkadas CG, MacKenzie RE. Formyltetrahydrofolate dehydrogenase-hydrolase from pig liver: Simultaneous assay of the activities Biochimica Et Biophysica Acta (Bba)/Protein Structure and Molecular. 871: 24-35. PMID 3697368 DOI: 10.1016/0167-4838(86)90129-9 |
0.459 |
|
1986 |
Mejia NR, Rios-Orlandi EM, MacKenzie RE. NAD-dependent methylenetetrahydrofolate dehydrogenase-methenyltetrahydrofolate cyclohydrolase from ascites tumor cells. Purification and properties Journal of Biological Chemistry. 261: 9509-9513. PMID 3487546 |
0.371 |
|
1985 |
Paquin J, Baugh CM, MacKenzie RE. Preparation of tritium-labeled tetrahydropteroylpolyglutamates of high specific radioactivity Analytical Biochemistry. 146: 52-58. PMID 3993943 DOI: 10.1016/0003-2697(85)90394-X |
0.366 |
|
1985 |
Mejia NR, MacKenzie RE. NAD-dependent methylenetetrahydrofolate dehydrogenase is expressed by immortal cells Journal of Biological Chemistry. 260: 14616-14620. PMID 3877056 |
0.352 |
|
1985 |
Smith DD, MacKenzie RE. Methylenetetrahydrofolate dehydrogenase-methenyltetrahydrofolate-cyclohydrolase-formyltetrahy dro folate synthetase. Affinity labelling of the dehydrogenase-cyclohydrolase active site. Biochemical and Biophysical Research Communications. 128: 148-54. PMID 3872659 DOI: 10.1016/0006-291X(85)91657-2 |
0.398 |
|
1984 |
Ross J, Green J, Baugh CM, MacKenzie RE, Matthews RG. Studies on the polyglutamate specificity of methylenetetrahydrofolate dehydrogenase from pig liver Biochemistry. 23: 1796-1801. PMID 6609718 DOI: 10.1021/Bi00303A033 |
0.385 |
|
1983 |
Drummond D, Smith S, MacKenzie RE. Methylenetetrahydrofolate dehydrogenase - methenyltetrahydrofolate cyclohydrolase - formyltetrahydrofolate synthetase from porcine liver: Evidence to support a common dehydrogenase-cyclohydrolase site Canadian Journal of Biochemistry and Cell Biology. 61: 1166-1171. PMID 6607769 |
0.4 |
|
1983 |
MacKenzie RE, Baugh CM. Interaction of tetrahydropteroylpolyglutamates with two folate-dependent multifunctional enzymes. Advances in Experimental Medicine and Biology. 163: 19-34. PMID 6412522 DOI: 10.1007/978-1-4757-5241-0_2 |
0.519 |
|
1981 |
MacKenzie RE, Paquin J, Aldridge M. FOLATE DEPENDEND MULTIFUNCTIONAL ENZYMES Biochemical Society Transactions. 9: 45P-45P. DOI: 10.1042/Bst009045Pa |
0.432 |
|
1980 |
MacKenzie RE, Aldridge M, Paquin J. The bifunctional enzyme formiminotransferase-cyclodeaminase is a tetramer of dimers. Journal of Biological Chemistry. 255: 9474-9478. PMID 7410436 |
0.372 |
|
1980 |
MacKenzie RE. Formiminotransferase-cyclodeaminase: a bifunctional enzyme from porcine liver. Methods in Enzymology. 66: 626-30. PMID 7374505 DOI: 10.1016/0076-6879(80)66516-1 |
0.428 |
|
1980 |
MacKenzie RE, Baugh CM. Tetrahydropteroylpolyglutamate derivatives as substrates of two multifunctional proteins with folate-dependent enzyme activities Bba - Enzymology. 611: 187-195. PMID 7350916 DOI: 10.1016/0005-2744(80)90054-6 |
0.487 |
|
1979 |
Tan LU, MacKenzie RE. Methylenetetrahydrofolate dehydrogenase-methenyltetrahydrofolate cyclohydrolase-formyltetrahydrofolate synthetase from porcine liver. Location of the activities in two domains of the multifunctional polypeptide. Canadian Journal of Biochemistry. 57: 806-812. PMID 476523 |
0.362 |
|
1978 |
Cohen L, MacKenzie RE. Methylenetetrahydrofolate dehydrogenase-methenyltetrahydrofolate cyclohydrolase-formyltetrahydrofolate synthetase from porcine liver. Interaction between the dehydrogenase and cyclohydrolase activities of the multifunctional enzyme Bba - Enzymology. 522: 311-317. PMID 23838 DOI: 10.1016/0005-2744(78)90065-7 |
0.457 |
|
1977 |
Tan LUL, Mackenzie RE. Methylenetetrahydrofolate dehydrogenase, methenyltetrahydrofolate cyclohydrolase and formyltetrahydrofolate synthetase from porcine liver. Isolation of a dehydrogenase-cyclohydrolase fragment from the multifunctional enzyme Bba - Enzymology. 485: 52-59. PMID 562190 DOI: 10.1016/0005-2744(77)90192-9 |
0.47 |
|
1977 |
Drury EJ, MacKenzie RE. Formiminotransferase-cyclodeaminase from porcine liver. A sulfhydryl essential for the deaminase activity of the bifunctional enzyme Canadian Journal of Biochemistry. 55: 919-923. PMID 561642 DOI: 10.1139/O77-137 |
0.488 |
|
1976 |
Beaudet R, Mackenzie RE. Formiminotransferase·cyclodeaminase from porcine liver An octomeric enzyme containing bifunctional polypeptides Bba - Protein Structure. 453: 151-161. PMID 999878 DOI: 10.1016/0005-2795(76)90259-2 |
0.36 |
|
1975 |
Beaudet R, Mackenzie R. Kinetic mechanism of formiminotransferase from porcine liver Bba - Enzymology. 410: 252-261. PMID 1239299 DOI: 10.1016/0005-2744(75)90227-2 |
0.41 |
|
1975 |
Drury EJ, Bazar LS, MacKenzie RE. Formiminotransferase-cyclodeaminase from porcine liver. Purification and physical properties of the enzyme complex Archives of Biochemistry and Biophysics. 169: 662-668. PMID 241297 DOI: 10.1016/0003-9861(75)90210-6 |
0.448 |
|
1973 |
Meighen EA, MacKenzie RE. Flavine specificity of enzyme-substrate intermediates in the bacterial bioluminescent reaction. Structural requirements of the flavine side chain Biochemistry. 12: 1482-1491. PMID 4699979 |
0.317 |
|
1973 |
MacKenzie RE. Co-purification of three folate enzymes from porcine liver. Biochemical and Biophysical Research Communications. 53: 1088-95. PMID 4147884 DOI: 10.1016/0006-291X(73)90576-7 |
0.47 |
|
1972 |
Mackenzie RE, Straus LD, Rabinowitz JC. Photooxidation of formyltetrahydrofolate synthetase in the presence of methylene blue. Archives of Biochemistry and Biophysics. 150: 421-7. PMID 5044034 DOI: 10.1016/0003-9861(72)90058-6 |
0.328 |
|
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