| Year |
Citation |
Score |
| 2023 |
Marszalek J, De Los Rios P, Cyr D, Mayer MP, Adupa V, Andréasson C, Blatch GL, Braun JEA, Brodsky JL, Bukau B, Chapple JP, Conz C, Dementin S, Genevaux P, Genest O, et al. J-domain proteins: From molecular mechanisms to diseases. Cell Stress & Chaperones. 29: 21-33. PMID 38320449 DOI: 10.1016/j.cstres.2023.12.002 |
0.32 |
|
| 2023 |
Sopha P, Meerod T, Chantrathonkul B, Phutubtim N, Cyr DM, Govitrapong P. Novel functions of the ER-located Hsp40s DNAJB12 and DNAJB14 on proteins at the outer mitochondrial membrane under stress mediated by CCCP. Molecular and Cellular Biochemistry. PMID 37851175 DOI: 10.1007/s11010-023-04866-1 |
0.346 |
|
| 2022 |
Kennedy A, Cyr DM. DNAJB12 and Hsp70 Mediate Triage of Misfolded Membrane Proteins for Proteasomal versus Lysosomal Degradation. Autophagy Reports. 1: 559-562. PMID 36743458 DOI: 10.1080/27694127.2022.2139335 |
0.383 |
|
| 2022 |
Cyr DM, Ramos CH. Specification of Hsp70 Function by Hsp40 Co-chaperones. Sub-Cellular Biochemistry. 101: 127-139. PMID 36520305 DOI: 10.1007/978-3-031-14740-1_4 |
0.438 |
|
| 2022 |
Zhang R, Malinverni D, Cyr DM, Rios PL, Nillegoda NB. J-domain protein chaperone circuits in proteostasis and disease. Trends in Cell Biology. PMID 35729039 DOI: 10.1016/j.tcb.2022.05.004 |
0.368 |
|
| 2019 |
Singh AK, Fan Y, Balut C, Alani S, Manelli A, Swensen AM, Jia Y, Neelands TR, Vortherms TA, Liu B, Searle XB, Wang X, Gao W, Hwang TC, Ren H, ... Cyr D, et al. Biological characterization of F508delCFTR protein processing by the CFTR Corrector ABBV-2222/GLPG2222. The Journal of Pharmacology and Experimental Therapeutics. PMID 31732698 DOI: 10.1124/Jpet.119.261800 |
0.353 |
|
| 2018 |
Kampinga HH, Andreasson C, Barducci A, Cheetham ME, Cyr D, Emanuelsson C, Genevaux P, Gestwicki JE, Goloubinoff P, Huerta-Cepas J, Kirstein J, Liberek K, Mayer MP, Nagata K, Nillegoda NB, et al. Function, evolution, and structure of J-domain proteins. Cell Stress & Chaperones. PMID 30478692 DOI: 10.1007/S12192-018-0948-4 |
0.457 |
|
| 2015 |
Vermulst M, Denney AS, Lang MJ, Hung CW, Moore S, Moseley MA, Thompson JW, Madden V, Gauer J, Wolfe KJ, Summers DW, Schleit J, Sutphin GL, Haroon S, Holczbauer A, ... ... Cyr D, et al. Corrigendum: Transcription errors induce proteotoxic stress and shorten cellular lifespan. Nature Communications. 6: 8738. PMID 26465398 DOI: 10.1038/Ncomms9738 |
0.724 |
|
| 2015 |
Vermulst M, Denney AS, Lang MJ, Hung CW, Moore S, Mosely AM, Thompson WJ, Madden V, Gauer J, Wolfe KJ, Summers DW, Schleit J, Sutphin GL, Haroon S, Holczbauer A, ... ... Cyr D, et al. Transcription errors induce proteotoxic stress and shorten cellular lifespan. Nature Communications. 6: 8065. PMID 26304740 DOI: 10.1038/Ncomms9065 |
0.75 |
|
| 2015 |
Cyr DM, Ramos CH. Specification of Hsp70 function by Type I and Type II Hsp40. Sub-Cellular Biochemistry. 78: 91-102. PMID 25487017 DOI: 10.1007/978-3-319-11731-7_4 |
0.421 |
|
| 2014 |
Wolfe KJ, Ren HY, Trepte P, Cyr DM. Polyglutamine-rich suppressors of huntingtin toxicity act upstream of Hsp70 and Sti1 in spatial quality control of amyloid-like proteins. Plos One. 9: e95914. PMID 24828240 DOI: 10.1371/Journal.Pone.0095914 |
0.76 |
|
| 2014 |
Houck SA, Ren HY, Madden VJ, Bonner JN, Conlin MP, Janovick JA, Conn PM, Cyr DM. Quality control autophagy degrades soluble ERAD-resistant conformers of the misfolded membrane protein GnRHR. Molecular Cell. 54: 166-79. PMID 24685158 DOI: 10.1016/j.molcel.2014.02.025 |
0.353 |
|
| 2013 |
Wolfe KJ, Ren HY, Trepte P, Cyr DM. The Hsp70/90 cochaperone, Sti1, suppresses proteotoxicity by regulating spatial quality control of amyloid-like proteins. Molecular Biology of the Cell. 24: 3588-602. PMID 24109600 DOI: 10.1091/Mbc.E13-06-0315 |
0.759 |
|
| 2013 |
Summers DW, Wolfe KJ, Ren HY, Cyr DM. The Type II Hsp40 Sis1 cooperates with Hsp70 and the E3 ligase Ubr1 to promote degradation of terminally misfolded cytosolic protein. Plos One. 8: e52099. PMID 23341891 DOI: 10.1371/Journal.Pone.0052099 |
0.799 |
|
| 2012 |
Borges JC, Seraphim TV, Mokry DZ, Almeida FC, Cyr DM, Ramos CH. Identification of regions involved in substrate binding and dimer stabilization within the central domains of yeast Hsp40 Sis1. Plos One. 7: e50927. PMID 23227221 DOI: 10.1371/Journal.Pone.0050927 |
0.321 |
|
| 2012 |
Houck SA, Singh S, Cyr DM. Cellular responses to misfolded proteins and protein aggregates. Methods in Molecular Biology (Clifton, N.J.). 832: 455-61. PMID 22350905 DOI: 10.1007/978-1-61779-474-2_32 |
0.396 |
|
| 2012 |
Houck SA, Cyr DM. Mechanisms for quality control of misfolded transmembrane proteins. Biochimica Et Biophysica Acta. 1818: 1108-14. PMID 22100602 DOI: 10.1016/j.bbamem.2011.11.007 |
0.371 |
|
| 2011 |
Ren HY, Patterson C, Cyr DM, Rosser MF. Reconstitution of CHIP E3 ubiquitin ligase activity. Methods in Molecular Biology (Clifton, N.J.). 787: 93-103. PMID 21898230 DOI: 10.1007/978-1-61779-295-3_8 |
0.646 |
|
| 2011 |
Grove DE, Rosser MF, Watkins RL, Cyr DM. Analysis of CFTR folding and degradation in transiently transfected cells. Methods in Molecular Biology (Clifton, N.J.). 741: 219-32. PMID 21594788 DOI: 10.1007/978-1-61779-117-8_15 |
0.636 |
|
| 2011 |
Wolfe KJ, Cyr DM. Amyloid in neurodegenerative diseases: friend or foe? Seminars in Cell & Developmental Biology. 22: 476-81. PMID 21458579 DOI: 10.1016/J.Semcdb.2011.03.011 |
0.749 |
|
| 2011 |
Mayo KJ, Cyr DM. Protein aggregation and neurodegeneration. Methods (San Diego, Calif.). 53: 185-6. PMID 21377577 DOI: 10.1016/j.ymeth.2011.02.009 |
0.374 |
|
| 2011 |
Grove DE, Fan CY, Ren HY, Cyr DM. The endoplasmic reticulum-associated Hsp40 DNAJB12 and Hsc70 cooperate to facilitate RMA1 E3-dependent degradation of nascent CFTRDeltaF508. Molecular Biology of the Cell. 22: 301-14. PMID 21148293 DOI: 10.1091/Mbc.E10-09-0760 |
0.339 |
|
| 2011 |
Summers DW, Cyr DM. Use of yeast as a system to study amyloid toxicity. Methods (San Diego, Calif.). 53: 226-31. PMID 21115125 DOI: 10.1016/J.Ymeth.2010.11.007 |
0.665 |
|
| 2011 |
Summers DW, Wolfe KJ, Cyr DM. Chaperone-Dependent Amyloid Assembly and Prion Toxicity Protein Chaperones and Protection From Neurodegenerative Diseases. 261-276. DOI: 10.1002/9781118063903.ch8 |
0.761 |
|
| 2010 |
Nillegoda NB, Theodoraki MA, Mandal AK, Mayo KJ, Ren HY, Sultana R, Wu K, Johnson J, Cyr DM, Caplan AJ. Ubr1 and Ubr2 function in a quality control pathway for degradation of unfolded cytosolic proteins. Molecular Biology of the Cell. 21: 2102-16. PMID 20462952 DOI: 10.1091/Mbc.E10-02-0098 |
0.39 |
|
| 2010 |
Douglas PM, Cyr DM. Interplay between protein homeostasis networks in protein aggregation and proteotoxicity. Biopolymers. 93: 229-36. PMID 19768782 DOI: 10.1002/Bip.21304 |
0.694 |
|
| 2009 |
Cyr DM, Hebert DN. Protein quality control--linking the unfolded protein response to disease. Conference on 'From Unfolded Proteins in the Endoplasmic Reticulum to Disease'. Embo Reports. 10: 1206-10. PMID 19851332 DOI: 10.1038/Embor.2009.224 |
0.335 |
|
| 2009 |
Douglas PM, Summers DW, Ren HY, Cyr DM. Reciprocal efficiency of RNQ1 and polyglutamine detoxification in the cytosol and nucleus. Molecular Biology of the Cell. 20: 4162-73. PMID 19656852 DOI: 10.1091/Mbc.E09-02-0170 |
0.767 |
|
| 2009 |
Grove DE, Rosser MF, Ren HY, Naren AP, Cyr DM. Mechanisms for rescue of correctable folding defects in CFTRDelta F508. Molecular Biology of the Cell. 20: 4059-69. PMID 19625452 DOI: 10.1091/Mbc.E08-09-0929 |
0.579 |
|
| 2009 |
Kota P, Summers DW, Ren HY, Cyr DM, Dokholyan NV. Identification of a consensus motif in substrates bound by a Type I Hsp40. Proceedings of the National Academy of Sciences of the United States of America. 106: 11073-8. PMID 19549854 DOI: 10.1073/Pnas.0900746106 |
0.679 |
|
| 2009 |
Summers DW, Douglas PM, Cyr DM. Prion propagation by Hsp40 molecular chaperones. Prion. 3: 59-64. PMID 19535913 DOI: 10.4161/Pri.3.2.9062 |
0.78 |
|
| 2009 |
Douglas PM, Summers DW, Cyr DM. Molecular chaperones antagonize proteotoxicity by differentially modulating protein aggregation pathways. Prion. 3: 51-8. PMID 19421006 DOI: 10.4161/Pri.3.2.8587 |
0.776 |
|
| 2009 |
Treusch S, Cyr DM, Lindquist S. Amyloid deposits: protection against toxic protein species? Cell Cycle (Georgetown, Tex.). 8: 1668-74. PMID 19411847 DOI: 10.4161/Cc.8.11.8503 |
0.355 |
|
| 2009 |
Summers DW, Douglas PM, Ramos CH, Cyr DM. Polypeptide transfer from Hsp40 to Hsp70 molecular chaperones. Trends in Biochemical Sciences. 34: 230-3. PMID 19359181 DOI: 10.1016/J.Tibs.2008.12.009 |
0.759 |
|
| 2009 |
Summers DW, Douglas PM, Ren HY, Cyr DM. The type I Hsp40 Ydj1 utilizes a farnesyl moiety and zinc finger-like region to suppress prion toxicity. The Journal of Biological Chemistry. 284: 3628-39. PMID 19056735 DOI: 10.1074/Jbc.M807369200 |
0.767 |
|
| 2009 |
Rosser MFN, Grove DE, Cyr DM. The use of small molecules to correct defects in CFTR folding, maturation, and channel activity Current Chemical Biology. 3: 100-111. |
0.542 |
|
| 2008 |
Ramos CH, Oliveira CL, Fan CY, Torriani IL, Cyr DM. Conserved central domains control the quaternary structure of type I and type II Hsp40 molecular chaperones. Journal of Molecular Biology. 383: 155-66. PMID 18723025 DOI: 10.1016/j.jmb.2008.08.019 |
0.315 |
|
| 2008 |
Rosser MF, Grove DE, Chen L, Cyr DM. Assembly and misassembly of cystic fibrosis transmembrane conductance regulator: folding defects caused by deletion of F508 occur before and after the calnexin-dependent association of membrane spanning domain (MSD) 1 and MSD2. Molecular Biology of the Cell. 19: 4570-9. PMID 18716059 DOI: 10.1091/mbc.E08-04-0357 |
0.644 |
|
| 2008 |
Douglas PM, Treusch S, Ren HY, Halfmann R, Duennwald ML, Lindquist S, Cyr DM. Chaperone-dependent amyloid assembly protects cells from prion toxicity. Proceedings of the National Academy of Sciences of the United States of America. 105: 7206-11. PMID 18480252 DOI: 10.1073/Pnas.0802593105 |
0.722 |
|
| 2008 |
Hirayama S, Yamazaki Y, Kitamura A, Oda Y, Morito D, Okawa K, Kimura H, Cyr DM, Kubota H, Nagata K. MKKS is a centrosome-shuttling protein degraded by disease-causing mutations via CHIP-mediated ubiquitination. Molecular Biology of the Cell. 19: 899-911. PMID 18094050 DOI: 10.1091/mbc.E07-07-0631 |
0.32 |
|
| 2007 |
Turnbull EL, Rosser MF, Cyr DM. The role of the UPS in cystic fibrosis. Bmc Biochemistry. 8: S11. PMID 18047735 DOI: 10.1186/1471-2091-8-S1-S11 |
0.642 |
|
| 2007 |
Rosser MF, Washburn E, Muchowski PJ, Patterson C, Cyr DM. Chaperone functions of the E3 ubiquitin ligase CHIP. The Journal of Biological Chemistry. 282: 22267-77. PMID 17545168 DOI: 10.1074/Jbc.M700513200 |
0.678 |
|
| 2006 |
Younger JM, Chen L, Ren HY, Rosser MF, Turnbull EL, Fan CY, Patterson C, Cyr DM. Sequential quality-control checkpoints triage misfolded cystic fibrosis transmembrane conductance regulator. Cell. 126: 571-82. PMID 16901789 DOI: 10.1016/J.Cell.2006.06.041 |
0.685 |
|
| 2006 |
Qian SB, McDonough H, Boellmann F, Cyr DM, Patterson C. CHIP-mediated stress recovery by sequential ubiquitination of substrates and Hsp70. Nature. 440: 551-5. PMID 16554822 DOI: 10.1038/Nature04600 |
0.373 |
|
| 2005 |
Dai Q, Qian SB, Li HH, McDonough H, Borchers C, Huang D, Takayama S, Younger JM, Ren HY, Cyr DM, Patterson C. Regulation of the cytoplasmic quality control protein degradation pathway by BAG2. The Journal of Biological Chemistry. 280: 38673-81. PMID 16169850 DOI: 10.1074/Jbc.M507986200 |
0.664 |
|
| 2005 |
Younger JM, Fan CY, Chen L, Rosser MF, Patterson C, Cyr DM. Cystic fibrosis transmembrane conductance regulator as a model substrate to study endoplasmic reticulum protein quality control in mammalian cells. Methods in Molecular Biology (Clifton, N.J.). 301: 293-303. PMID 15917641 DOI: 10.1385/1-59259-895-1:293 |
0.724 |
|
| 2005 |
Fan CY, Ren HY, Lee P, Caplan AJ, Cyr DM. The type I Hsp40 zinc finger-like region is required for Hsp70 to capture non-native polypeptides from Ydj1. The Journal of Biological Chemistry. 280: 695-702. PMID 15496404 DOI: 10.1074/Jbc.M410645200 |
0.381 |
|
| 2004 |
Younger JM, Ren HY, Chen L, Fan CY, Fields A, Patterson C, Cyr DM. A foldable CFTR{Delta}F508 biogenic intermediate accumulates upon inhibition of the Hsc70-CHIP E3 ubiquitin ligase. The Journal of Cell Biology. 167: 1075-85. PMID 15611333 DOI: 10.1083/Jcb.200410065 |
0.586 |
|
| 2004 |
Walsh P, Bursać D, Law YC, Cyr D, Lithgow T. The J-protein family: modulating protein assembly, disassembly and translocation. Embo Reports. 5: 567-71. PMID 15170475 DOI: 10.1038/Sj.Embor.7400172 |
0.455 |
|
| 2004 |
Fan CY, Lee S, Ren HY, Cyr DM. Exchangeable chaperone modules contribute to specification of type I and type II Hsp40 cellular function. Molecular Biology of the Cell. 15: 761-73. PMID 14657253 DOI: 10.1091/mbc.E03-03-0146 |
0.373 |
|
| 2004 |
Dalal S, Rosser MF, Cyr DM, Hanson PI. Distinct roles for the AAA ATPases NSF and p97 in the secretory pathway. Molecular Biology of the Cell. 15: 637-48. PMID 14617820 DOI: 10.1091/Mbc.E03-02-0097 |
0.619 |
|
| 2003 |
Fan CY, Lee S, Cyr DM. Mechanisms for regulation of Hsp70 function by Hsp40. Cell Stress & Chaperones. 8: 309-16. PMID 15115283 DOI: 10.1379/1466-1268(2003)008<0309:MFROHF>2.0.CO;2 |
0.393 |
|
| 2003 |
Dai Q, Zhang C, Wu Y, McDonough H, Whaley RA, Godfrey V, Li HH, Madamanchi N, Xu W, Neckers L, Cyr D, Patterson C. CHIP activates HSF1 and confers protection against apoptosis and cellular stress. The Embo Journal. 22: 5446-58. PMID 14532117 DOI: 10.1093/Emboj/Cdg529 |
0.39 |
|
| 2003 |
Jiang J, Cyr D, Babbitt RW, Sessa WC, Patterson C. Chaperone-dependent regulation of endothelial nitric-oxide synthase intracellular trafficking by the co-chaperone/ubiquitin ligase CHIP. The Journal of Biological Chemistry. 278: 49332-41. PMID 14507928 DOI: 10.1074/Jbc.M304738200 |
0.451 |
|
| 2002 |
Cyr DM, Höhfeld J, Patterson C. Protein quality control: U-box-containing E3 ubiquitin ligases join the fold. Trends in Biochemical Sciences. 27: 368-75. PMID 12114026 DOI: 10.1016/S0968-0004(02)02125-4 |
0.442 |
|
| 2002 |
Lee S, Fan CY, Younger JM, Ren H, Cyr DM. Identification of essential residues in the type II Hsp40 Sis1 that function in polypeptide binding. The Journal of Biological Chemistry. 277: 21675-82. PMID 11919183 DOI: 10.1074/jbc.M111075200 |
0.627 |
|
| 2001 |
Höhfeld J, Cyr DM, Patterson C. From the cradle to the grave: Molecular chaperones that may choose between folding and degradation Embo Reports. 2: 885-890. PMID 11600451 DOI: 10.1093/Embo-Reports/Kve206 |
0.434 |
|
| 2001 |
Jiang J, Ballinger CA, Wu Y, Dai Q, Cyr DM, Höhfeld J, Patterson C. CHIP is a U-box-dependent E3 ubiquitin ligase: Identification of Hsc70 as a target for ubiquitylation Journal of Biological Chemistry. 276: 42938-42944. PMID 11557750 DOI: 10.1074/jbc.M101968200 |
0.351 |
|
| 2001 |
Meacham GC, Patterson C, Zhang W, Younger JM, Cyr DM. The Hsc70 co-chaperone CHIP targets immature CFTR for proteasomal degradation. Nature Cell Biology. 3: 100-5. PMID 11146634 DOI: 10.1038/35050509 |
0.617 |
|
| 2000 |
Sha B, Lee S, Cyr DM. The crystal structure of the peptide-binding fragment from the yeast Hsp40 protein Sis1 Structure. 8: 799-807. PMID 10997899 DOI: 10.1016/S0969-2126(00)00170-2 |
0.359 |
|
| 1999 |
Meacham GC, Browne BL, Zhang W, Kellermayer R, Bedwell DM, Cyr DM. Mutations in the yeast Hsp40 chaperone protein Ydj1 cause defects in Axl1 biogenesis and pro-a-factor processing. The Journal of Biological Chemistry. 274: 34396-402. PMID 10567418 DOI: 10.1074/Jbc.274.48.34396 |
0.312 |
|
| 1999 |
Sha B, Cyr D. Purification, crystallization and preliminary X-ray crystallographic studies of S. cerevisiae Hsp40 Sis1 Acta Crystallographica Section D: Biological Crystallography. 55: 1234-1236. PMID 10329795 DOI: 10.1107/S090744499900476X |
0.32 |
|
| 1998 |
Lu Z, Cyr DM. Protein folding activity of Hsp70 is modified differentially by the Hsp40 co-chaperones Sis1 and Ydj1 Journal of Biological Chemistry. 273: 27824-27830. PMID 9774392 DOI: 10.1074/jbc.273.43.27824 |
0.425 |
|
| 1998 |
Lu Z, Cyr DM. The conserved carboxyl terminus and zinc finger-like domain of the co- chaperone Ydj1 assist Hsp70 in protein folding Journal of Biological Chemistry. 273: 5970-5978. PMID 9488737 DOI: 10.1074/jbc.273.10.5970 |
0.405 |
|
| 1996 |
Cyr DM, Neupert W. Roles for hsp70 in protein translocation across membranes of organelles. Exs. 77: 25-40. PMID 8856967 |
0.584 |
|
| 1996 |
Ungermann C, Guiard B, Neupert W, Cyr DM. The delta psi- and Hsp70/MIM44-dependent reaction cycle driving early steps of protein import into mitochondria. The Embo Journal. 15: 735-44. PMID 8631295 DOI: 10.1002/J.1460-2075.1996.Tb00409.X |
0.478 |
|
| 1995 |
Cyr DM, Ungermann C, Neupert W. Analysis of mitochondrial protein import pathway in Saccharomyces cerevisiae with translocation intermediates. Methods in Enzymology. 260: 241-52. PMID 8592449 DOI: 10.1016/0076-6879(95)60142-2 |
0.524 |
|
| 1994 |
Stuart RA, Cyr DM, Craig EA, Neupert W. Mitochondrial molecular chaperones: their role in protein translocation. Trends in Biochemical Sciences. 19: 87-92. PMID 8160272 DOI: 10.1016/0968-0004(94)90041-8 |
0.508 |
|
| 1994 |
Cyr DM, Douglas MG. Differential regulation of Hsp70 subfamilies by the eukaryotic DnaJ homologue Ydj1 Journal of Biological Chemistry. 269: 9798-9804. PMID 8144572 |
0.351 |
|
| 1994 |
Cyr DM, Langer T, Douglas MG. DnaJ-like proteins: molecular chaperones and specific regulators of Hsp70 Trends in Biochemical Sciences. 19: 176-181. PMID 8016869 DOI: 10.1016/0968-0004(94)90281-X |
0.413 |
|
| 1994 |
Stuart RA, Cyr DM, Neupert W. Hsp70 in mitochondrial biogenesis: from chaperoning nascent polypeptide chains to facilitation of protein degradation. Experientia. 50: 1002-11. PMID 7988658 DOI: 10.1007/BF01923454 |
0.591 |
|
| 1994 |
Ungermann C, Neupert W, Cyr DM. The role of Hsp70 in conferring unidirectionality on protein translocation into mitochondria. Science (New York, N.Y.). 266: 1250-3. PMID 7973708 DOI: 10.1126/Science.7973708 |
0.515 |
|
| 1993 |
Caplan AJ, Cyr DM, Douglas MG. Eukaryotic homologues of escherichia coli dnaJ: A diverse protein family that functions with HSP70 stress proteins Molecular Biology of the Cell. 4: 555-563. PMID 8374166 DOI: 10.1091/Mbc.4.6.555 |
0.321 |
|
| 1993 |
Cyr DM, Stuart RA, Neupert W. A matrix ATP requirement for presequence translocation across the inner membrane of mitochondria. The Journal of Biological Chemistry. 268: 23751-4. PMID 8226903 |
0.45 |
|
| 1992 |
Caplan AJ, Cyr DM, Douglas MG. YDJ1p facilitates polypeptide translocation across different intracellular membranes by a conserved mechanism Cell. 71: 1143-1155. PMID 1473150 DOI: 10.1016/S0092-8674(05)80063-7 |
0.309 |
|
| 1992 |
Cyr DM, Lu X, Douglas MG. Regulation of Hsp70 function by a eukaryotic DnaJ homolog Journal of Biological Chemistry. 267: 20927-20931. PMID 1400408 |
0.322 |
|
| 1991 |
Cyr DM, Egan SG, Brini CM, Tremblay GC. On the mechanism of inhibition of gluconeogenesis and ureagenesis by sodium benzoate. Biochemical Pharmacology. 42: 645-54. PMID 1677573 DOI: 10.1016/0006-2952(91)90328-3 |
0.453 |
|
| 1989 |
Cyr DM, Tremblay GC. Potentiation of benzoate toxicity by glyoxylate. Inhibition of pyruvate carboxylase and the urea cycle. Biochemical Pharmacology. 38: 2919-23. PMID 2775312 DOI: 10.1016/0006-2952(89)90450-4 |
0.451 |
|
| 1989 |
Cyr DM, Tremblay GC. On combination therapy with benzoate and piridoxilate. American Journal of Diseases of Children (1960). 143: 1392. PMID 2589268 DOI: 10.1001/archpedi.1989.02150240014006 |
0.374 |
|
| 1989 |
Griffith AD, Cyr DM, Egan SG, Tremblay GC. Inhibition of pyruvate carboxylase by sequestration of coenzyme A with sodium benzoate. Archives of Biochemistry and Biophysics. 269: 201-7. PMID 2492793 DOI: 10.1016/0003-9861(89)90101-X |
0.451 |
|
| 1986 |
Maswoswe SM, Cyr DM, Griffith AD, Tremblay GC. The effect of sodium benzoate on ammonia toxicity in rats. Biochemical and Biophysical Research Communications. 138: 369-73. PMID 3741416 DOI: 10.1016/0006-291X(86)90290-1 |
0.423 |
|
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