메뉴 건너뛰기




Volumn 86, Issue 5, 2008, Pages 437-447

Kinetics of human peptidylarginine deiminase 2 (hPAD2) - Reduction of Ca2+ dependence by phospholipids and assessment of proposed inhibition by paclitaxel side chains

Author keywords

Citrulline; Deimination; Multiple sclerosis; Myelin; Myelin basic protein; Paclitaxel; Paclitaxel side chain; Peptidylarginine deiminase; Post translational modifications

Indexed keywords

AMINO ACIDS; CALCIUM; CELL MEMBRANES; ENZYMES; ESTERIFICATION; ESTERS; ORGANIC COMPOUNDS; PHOSPHOLIPIDS; PROTEINS;

EID: 54249134964     PISSN: 08298211     EISSN: None     Source Type: Journal    
DOI: 10.1139/O08-124     Document Type: Article
Times cited : (15)

References (56)
  • 1
    • 0032885575 scopus 로고    scopus 로고
    • Localization of peptidylarginine deiminase type II in a stage-specific immature oligodendrocyte from rat cerebral hemisphere
    • PMID:10530518, doi:10.1016/S0304-3940(99)00678-3
    • Akiyama, K., Sakurai, Y., Asou, H., and Senshu, T. 1999. Localization of peptidylarginine deiminase type II in a stage-specific immature oligodendrocyte from rat cerebral hemisphere. Neurosci. Lett. 274: 53-55. doi:10.1016/S0304-3940(99)00678-3. PMID:10530518.
    • (1999) Neurosci. Lett , vol.274 , pp. 53-55
    • Akiyama, K.1    Sakurai, Y.2    Asou, H.3    Senshu, T.4
  • 2
    • 0347062153 scopus 로고    scopus 로고
    • Crystallization and preliminary X-ray crystallographic analysis of human peptidylarginine deiminase V
    • PMID:14646111, doi:10.1107/S0907444903022741
    • Arita, K., Hashimoto, H., Shimizu, T., Yamada, M., and Sato, M. 2003. Crystallization and preliminary X-ray crystallographic analysis of human peptidylarginine deiminase V. Acta Crystallogr. Sect. D: Biol. Crystallogr. 59: 2332-2333. doi:10.1107/S0907444903022741. PMID:14646111.
    • (2003) Acta Crystallogr. Sect. D: Biol. Crystallogr , vol.59 , pp. 2332-2333
    • Arita, K.1    Hashimoto, H.2    Shimizu, T.3    Yamada, M.4    Sato, M.5
  • 4
    • 33645793778 scopus 로고    scopus 로고
    • Structural basis for histone N-terminal recognition by human peptidylarginine deiminase 4
    • PMID:16567635, doi:10.1073/pnas. 0509639103
    • Arita, K., Shimizu, T., Hashimoto, H., Hidaka, Y., Yamada, M., and Sato, M. 2006. Structural basis for histone N-terminal recognition by human peptidylarginine deiminase 4. Proc. Natl. Acad. Sci. U.S.A. 103: 5291-5296. doi:10.1073/pnas. 0509639103. PMID:16567635.
    • (2006) Proc. Natl. Acad. Sci. U.S.A , vol.103 , pp. 5291-5296
    • Arita, K.1    Shimizu, T.2    Hashimoto, H.3    Hidaka, Y.4    Yamada, M.5    Sato, M.6
  • 5
    • 38049181261 scopus 로고    scopus 로고
    • Microglial expression of peptidylarginine deiminase 2 in the prenatal rat brain
    • PMID:17579814, doi:10.2478/s11658-007-0025-y
    • Asaga, H., and Ishigami, A. 2007. Microglial expression of peptidylarginine deiminase 2 in the prenatal rat brain. Cell. Mol. Biol. Lett. 12: 536-544. doi:10.2478/s11658-007-0025-y. PMID:17579814.
    • (2007) Cell. Mol. Biol. Lett , vol.12 , pp. 536-544
    • Asaga, H.1    Ishigami, A.2
  • 6
    • 0037189068 scopus 로고    scopus 로고
    • Increased and type II-specific expression of peptidylarginine deiminase in activated microglia but not hyperplastic astrocytes following kainic acid-evoked neurodegeneration in the rat brain
    • PMID:12057845, doi:10.1016/S0304- 3940(02)00334-8
    • Asaga, H., Akiyama, K., Ohsawa, T., and Ishigami, A. 2002. Increased and type II-specific expression of peptidylarginine deiminase in activated microglia but not hyperplastic astrocytes following kainic acid-evoked neurodegeneration in the rat brain. Neurosci. Lett. 326: 129-132. doi:10.1016/S0304- 3940(02)00334-8. PMID:12057845.
    • (2002) Neurosci. Lett , vol.326 , pp. 129-132
    • Asaga, H.1    Akiyama, K.2    Ohsawa, T.3    Ishigami, A.4
  • 7
    • 27844536541 scopus 로고    scopus 로고
    • A rigorous method for multigenic families' functional annotation: The peptidyl arginine deiminase (PADs) proteins family example
    • PMID:16271148, doi:10.1186/1471-2164-6-153
    • Balandraud, N., Gouret, P., Danchin, E.G., Blanc, M., Zinn, D., Roudier, J., and Pontarotti, P. 2005. A rigorous method for multigenic families' functional annotation: the peptidyl arginine deiminase (PADs) proteins family example. BMC Genomics, 6: 153. doi:10.1186/1471-2164-6-153. PMID:16271148.
    • (2005) BMC Genomics , vol.6 , pp. 153
    • Balandraud, N.1    Gouret, P.2    Danchin, E.G.3    Blanc, M.4    Zinn, D.5    Roudier, J.6    Pontarotti, P.7
  • 9
    • 33845746183 scopus 로고    scopus 로고
    • Modulation of peptidyl arginine deiminase 2 and implication for neurodegeneration
    • PMID:17169845, doi:10.1080/02713680600991437
    • Bhattacharya, S.K., Bhat, M.B., and Takahara, H. 2006. Modulation of peptidyl arginine deiminase 2 and implication for neurodegeneration. Curr. Eye Res. 31: 1063-1071. doi:10.1080/02713680600991437. PMID:17169845.
    • (2006) Curr. Eye Res , vol.31 , pp. 1063-1071
    • Bhattacharya, S.K.1    Bhat, M.B.2    Takahara, H.3
  • 10
    • 33749327922 scopus 로고    scopus 로고
    • Peptidylarginine deiminases and deimination in biology and pathology: Relevance to skin homeostasis
    • PMID:16973334, doi:10.1016/j.jdermsci.2006.07.004
    • Chavanas, S., Mechin, M.C., Nachat, R., Adoue, V., Coudane, F., Serre, G., and Simon, M. 2006. Peptidylarginine deiminases and deimination in biology and pathology: relevance to skin homeostasis. J. Dermatol. Sci. 44: 63-72. doi:10.1016/j.jdermsci.2006.07.004. PMID:16973334.
    • (2006) J. Dermatol. Sci , vol.44 , pp. 63-72
    • Chavanas, S.1    Mechin, M.C.2    Nachat, R.3    Adoue, V.4    Coudane, F.5    Serre, G.6    Simon, M.7
  • 11
    • 4244120872 scopus 로고
    • Microdetermination of phosphorus
    • doi:10.1021/ac60119a033
    • Chen, P.S., Toribara, T.Y., and Warner, H. 1956. Microdetermination of phosphorus. Anal. Chem. 28: 1756-1758. doi:10.1021/ac60119a033.
    • (1956) Anal. Chem , vol.28 , pp. 1756-1758
    • Chen, P.S.1    Toribara, T.Y.2    Warner, H.3
  • 12
    • 84988115618 scopus 로고
    • Validation of the general-purpose Tripos 5.2 force-field
    • doi:10.1002/jcc.540100804
    • Clark, M., Cramer, R.D., and Vanopdenbosch, N. 1989. Validation of the general-purpose Tripos 5.2 force-field. J. Comput. Chem. 10: 982-1012. doi:10.1002/jcc.540100804.
    • (1989) J. Comput. Chem , vol.10 , pp. 982-1012
    • Clark, M.1    Cramer, R.D.2    Vanopdenbosch, N.3
  • 13
    • 33846926110 scopus 로고    scopus 로고
    • White matter rafting - membrane microdomains in myelin
    • PMID:17031566, doi:10.1007/s11064- 006-9137-4
    • DeBruin, L.S., and Harauz, G. 2007. White matter rafting - membrane microdomains in myelin. Neurochem. Res. 32: 213-228. doi:10.1007/s11064- 006-9137-4. PMID:17031566.
    • (2007) Neurochem. Res , vol.32 , pp. 213-228
    • DeBruin, L.S.1    Harauz, G.2
  • 14
    • 33947371742 scopus 로고    scopus 로고
    • Partitioning of myelin basic protein into membrane microdomains in a spontaneously demyelinating mouse model for multiple sclerosis
    • PMID:17215885, doi:10.1139/O06-180
    • DeBruin, L.S., Haines, J.D., Bienzle, D., and Harauz, G. 2006. Partitioning of myelin basic protein into membrane microdomains in a spontaneously demyelinating mouse model for multiple sclerosis. Biochem. Cell Biol. 84: 993-1005. doi:10.1139/O06-180. PMID:17215885.
    • (2006) Biochem. Cell Biol , vol.84 , pp. 993-1005
    • DeBruin, L.S.1    Haines, J.D.2    Bienzle, D.3    Harauz, G.4
  • 15
    • 1642291355 scopus 로고    scopus 로고
    • Micellar paclitaxel improves severe psoriasis in a prospective phase II pilot study
    • PMID: 15034502, doi:10.1016/j.jaad.2003.09.018
    • Ehrlich, A., Booher, S., Becerra, Y., Borris, D.L., Figg, W.D., Turner, M.L., and Blauvelt, A. 2004. Micellar paclitaxel improves severe psoriasis in a prospective phase II pilot study. J. Am. Acad. Dermatol. 50: 533-540. doi:10.1016/j.jaad.2003.09.018. PMID: 15034502.
    • (2004) J. Am. Acad. Dermatol , vol.50 , pp. 533-540
    • Ehrlich, A.1    Booher, S.2    Becerra, Y.3    Borris, D.L.4    Figg, W.D.5    Turner, M.L.6    Blauvelt, A.7
  • 16
    • 33846927285 scopus 로고    scopus 로고
    • A tale of two citrullines - Structural and functional aspects of myelin basic protein deimination in health and disease
    • PMID:16900293, doi:10.1007/s11064-006-9108-9
    • Harauz, G., and Musse, A.A. 2007. A tale of two citrullines - Structural and functional aspects of myelin basic protein deimination in health and disease. Neurochem. Res. 32: 137-158. doi:10.1007/s11064-006-9108-9. PMID:16900293.
    • (2007) Neurochem. Res , vol.32 , pp. 137-158
    • Harauz, G.1    Musse, A.A.2
  • 17
    • 0029878720 scopus 로고    scopus 로고
    • Humphrey, W., Dalke, A., and Schulten, K. 1996. VMD: visual molecular dynamics. J. Mol. Graph. 14: 33-38. doi:10.1016/0263-7855(96)00018-5. PMID:8744570.
    • Humphrey, W., Dalke, A., and Schulten, K. 1996. VMD: visual molecular dynamics. J. Mol. Graph. 14: 33-38. doi:10.1016/0263-7855(96)00018-5. PMID:8744570.
  • 18
    • 33745591928 scopus 로고    scopus 로고
    • Association between PADI4 and rheumatoid arthritis: A meta-analysis
    • PMID:16449362, doi:10.1093/ rheumatology/kel023
    • Iwamoto, T., Ikari, K., Nakamura, T., Kuwahara, M., Toyama, Y., Tomatsu, T., et al. 2006. Association between PADI4 and rheumatoid arthritis: a meta-analysis. Rheumatology (Oxford), 45: 804-807. doi:10.1093/ rheumatology/kel023. PMID:16449362.
    • (2006) Rheumatology (Oxford) , vol.45 , pp. 804-807
    • Iwamoto, T.1    Ikari, K.2    Nakamura, T.3    Kuwahara, M.4    Toyama, Y.5    Tomatsu, T.6
  • 19
    • 23244447251 scopus 로고    scopus 로고
    • Kinetic characterization of protein arginine deiminase 4: A transcriptional corepressor implicated in the onset and progression of rheumatoid arthritis
    • PMID:16060666, doi:10.1021/bi050292m
    • Kearney, P.L., Bhatia, M., Jones, N.G., Yuan, L., Glascock, M.C., Catchings, K.L., et al. 2005. Kinetic characterization of protein arginine deiminase 4: a transcriptional corepressor implicated in the onset and progression of rheumatoid arthritis. Biochemistry, 44: 10570-10582. doi:10.1021/bi050292m. PMID:16060666.
    • (2005) Biochemistry , vol.44 , pp. 10570-10582
    • Kearney, P.L.1    Bhatia, M.2    Jones, N.G.3    Yuan, L.4    Glascock, M.C.5    Catchings, K.L.6
  • 20
    • 0142234077 scopus 로고    scopus 로고
    • Multiple sclerosis: An important role for post-translational modifications of myelin basic protein in pathogenesis
    • PMID: 12832457, doi:10.1074/mcp.M200050-MCP200
    • Kim, J.K., Mastronardi, F.G., Wood, D.D., Lubman, D.M., Zand, R., and Moscarello, M.A. 2003. Multiple sclerosis: an important role for post-translational modifications of myelin basic protein in pathogenesis. Mol. Cell. Proteomics, 2: 453-462. doi:10.1074/mcp.M200050-MCP200. PMID: 12832457.
    • (2003) Mol. Cell. Proteomics , vol.2 , pp. 453-462
    • Kim, J.K.1    Mastronardi, F.G.2    Wood, D.D.3    Lubman, D.M.4    Zand, R.5    Moscarello, M.A.6
  • 21
    • 38549168544 scopus 로고    scopus 로고
    • Profiling protein arginine deiminase 4 (PAD4): A novel screen to identify PAD4 inhibitors
    • PMID:17964793, doi:10.1016/j.bmc.2007.10.021
    • Knuckley, B., Luo, Y., and Thompson, P.R. 2008. Profiling protein arginine deiminase 4 (PAD4): a novel screen to identify PAD4 inhibitors. Bioorg. Med. Chem. 16: 739-745. doi:10.1016/j.bmc.2007.10.021. PMID:17964793.
    • (2008) Bioorg. Med. Chem , vol.16 , pp. 739-745
    • Knuckley, B.1    Luo, Y.2    Thompson, P.R.3
  • 22
    • 0021114827 scopus 로고
    • Purification and properties of a brain enzyme which deiminates proteins
    • PMID:6860676
    • Kubilus, J., and Baden, H.P. 1983. Purification and properties of a brain enzyme which deiminates proteins. Biochim. Biophys. Acta, 745: 285-291. PMID:6860676.
    • (1983) Biochim. Biophys. Acta , vol.745 , pp. 285-291
    • Kubilus, J.1    Baden, H.P.2
  • 23
    • 0027317616 scopus 로고
    • Deimination of human myelin basic protein by a peptidylarginine deiminase from bovine brain
    • PMID:7689646, doi:10.1111/j.1471-4159.1993.tb03612.x
    • Lamensa, J.W., and Moscarello, M.A. 1993. Deimination of human myelin basic protein by a peptidylarginine deiminase from bovine brain. J. Neurochem. 61: 987-996. doi:10.1111/j.1471-4159.1993.tb03612.x. PMID:7689646.
    • (1993) J. Neurochem , vol.61 , pp. 987-996
    • Lamensa, J.W.1    Moscarello, M.A.2
  • 24
    • 33749359452 scopus 로고    scopus 로고
    • Inhibitors and inactivators of protein arginine deiminase 4: Functional and structural characterization
    • PMID: 17002273, doi:10.1021/bi061180d
    • Luo, Y., Arita, K., Bhatia, M., Knuckley, B., Lee, Y.H., Stallcup, M.R., et al. 2006a. Inhibitors and inactivators of protein arginine deiminase 4: functional and structural characterization. Biochemistry, 45: 11727-11736. doi:10.1021/bi061180d. PMID: 17002273.
    • (2006) Biochemistry , vol.45 , pp. 11727-11736
    • Luo, Y.1    Arita, K.2    Bhatia, M.3    Knuckley, B.4    Lee, Y.H.5    Stallcup, M.R.6
  • 25
    • 31944448153 scopus 로고    scopus 로고
    • A fluoroacetamidine-based inactivator of protein arginine deiminase 4: Design, synthesis, and in vitro and in vivo evaluation
    • PMID:16433522, doi:10.1021/ja0576233
    • Luo, Y., Knuckley, B., Lee, Y.H., Stallcup, M.R., and Thompson, P.R. 2006b. A fluoroacetamidine-based inactivator of protein arginine deiminase 4: design, synthesis, and in vitro and in vivo evaluation. J. Am. Chem. Soc. 128: 1092-1093. doi:10.1021/ja0576233. PMID:16433522.
    • (2006) J. Am. Chem. Soc , vol.128 , pp. 1092-1093
    • Luo, Y.1    Knuckley, B.2    Lee, Y.H.3    Stallcup, M.R.4    Thompson, P.R.5
  • 26
    • 20344365607 scopus 로고    scopus 로고
    • Molecules affecting myelin stability: A novel hypothesis regarding the pathogenesis of multiple sclerosis
    • PMID:15704220, doi:10.1002/jnr.20420
    • Mastronardi, F.G., and Moscarello, M.A. 2005. Molecules affecting myelin stability: a novel hypothesis regarding the pathogenesis of multiple sclerosis. J. Neurosci. Res. 80: 301-308. doi:10.1002/jnr.20420. PMID:15704220.
    • (2005) J. Neurosci. Res , vol.80 , pp. 301-308
    • Mastronardi, F.G.1    Moscarello, M.A.2
  • 27
    • 0029964486 scopus 로고    scopus 로고
    • Mastronardi, F.G., Ackerley, C.A., Roots, B.I., and Moscarello, M.A. 1996a. Loss of myelin basic protein cationicity in DM20 transgenic mice is dosage dependent. J. Neurosci. Res. 44: 301-307. doi:10.1002/(SICI) 1097-4547(19960515)44:4∠301::AID-JNR1〉3.0.CO;2-G. PMID:8739149.
    • Mastronardi, F.G., Ackerley, C.A., Roots, B.I., and Moscarello, M.A. 1996a. Loss of myelin basic protein cationicity in DM20 transgenic mice is dosage dependent. J. Neurosci. Res. 44: 301-307. doi:10.1002/(SICI) 1097-4547(19960515)44:4∠301::AID-JNR1〉3.0.CO;2-G. PMID:8739149.
  • 28
    • 0030032373 scopus 로고    scopus 로고
    • Modifications of myelin basic protein in DM20 transgenic mice are similar to those in myelin basic protein from multiple sclerosis
    • PMID:8567954, doi:10.1172/JCI118422
    • Mastronardi, F.G., Mak, B., Ackerley, C.A., Roots, B.I., and Moscarello, M.A. 1996b. Modifications of myelin basic protein in DM20 transgenic mice are similar to those in myelin basic protein from multiple sclerosis. J. Clin. Invest. 97: 349-358. doi:10.1172/JCI118422. PMID:8567954.
    • (1996) J. Clin. Invest , vol.97 , pp. 349-358
    • Mastronardi, F.G.1    Mak, B.2    Ackerley, C.A.3    Roots, B.I.4    Moscarello, M.A.5
  • 29
    • 33750957133 scopus 로고    scopus 로고
    • Increased citrullination of histone H3 in multiple sclerosis brain and animal models of demyelination: A role for tumor necrosis factor-induced peptidylarginine deiminase 4 translocation
    • PMID:17079667, doi:10.1523/JNEUROSCI.3349-06.2006
    • Mastronardi, F.G., Wood, D.D., Mei, J., Raijmakers, R., Tseveleki, V., Dosch, H.M., et al. 2006. Increased citrullination of histone H3 in multiple sclerosis brain and animal models of demyelination: a role for tumor necrosis factor-induced peptidylarginine deiminase 4 translocation. J. Neurosci. 26: 11387-11396. doi:10.1523/JNEUROSCI.3349-06.2006. PMID:17079667.
    • (2006) J. Neurosci , vol.26 , pp. 11387-11396
    • Mastronardi, F.G.1    Wood, D.D.2    Mei, J.3    Raijmakers, R.4    Tseveleki, V.5    Dosch, H.M.6
  • 30
    • 34250628007 scopus 로고    scopus 로고
    • Synergy between paclitaxel plus an exogenous methyl donor in the suppression of murine demyelinating diseases
    • PMID:17548438, doi:10.1177/1352458506072167
    • Mastronardi, F.G., Tsui, H., Winer, S., Wood, D.D., Selvanantham, T., Galligan, C., et al. 2007. Synergy between paclitaxel plus an exogenous methyl donor in the suppression of murine demyelinating diseases. Mult. Scler. 13: 596-609. doi:10.1177/1352458506072167. PMID:17548438.
    • (2007) Mult. Scler , vol.13 , pp. 596-609
    • Mastronardi, F.G.1    Tsui, H.2    Winer, S.3    Wood, D.D.4    Selvanantham, T.5    Galligan, C.6
  • 31
    • 44949151663 scopus 로고    scopus 로고
    • Optimization of taxane binding to microtubules: Binding affinity dissection and incremental construction of a high-affinity analog of paclitaxel
    • PMID:18559268, doi:10.1016/j.chembiol.2008.05.008
    • Matesanz, R., Barasoain, I., Yang, C.G., Wang, L., Li, X., de Ines, C., et al. 2008. Optimization of taxane binding to microtubules: binding affinity dissection and incremental construction of a high-affinity analog of paclitaxel. Chem. Biol. 15: 573-585. doi:10.1016/j.chembiol.2008.05.008. PMID:18559268.
    • (2008) Chem. Biol , vol.15 , pp. 573-585
    • Matesanz, R.1    Barasoain, I.2    Yang, C.G.3    Wang, L.4    Li, X.5    de Ines, C.6
  • 32
    • 34347384856 scopus 로고    scopus 로고
    • Update on peptidylarginine deiminases and deimination in skin physiology and severe human diseases
    • PMID:18489346, doi:10.1111/j.1467-2494.2007.00377.x
    • Mechin, M.C., Sebbag, M., Arnaud, J., Nachat, R., Foulquier, C., Adoue, V., et al. 2007. Update on peptidylarginine deiminases and deimination in skin physiology and severe human diseases. Int. J. Cosmet. Sci. 29: 147-168. doi:10.1111/j.1467-2494.2007.00377.x. PMID:18489346.
    • (2007) Int. J. Cosmet. Sci , vol.29 , pp. 147-168
    • Mechin, M.C.1    Sebbag, M.2    Arnaud, J.3    Nachat, R.4    Foulquier, C.5    Adoue, V.6
  • 33
    • 33644520285 scopus 로고    scopus 로고
    • NMDA receptors mediate calcium accumulation in myelin during chemical ischaemia
    • PMID:16372019
    • Micu, I., Jiang, Q., Coderre, E., Ridsdale, A., Zhang, L., Woulfe, J., et al. 2006. NMDA receptors mediate calcium accumulation in myelin during chemical ischaemia. Nature, 439: 988-992. PMID:16372019.
    • (2006) Nature , vol.439 , pp. 988-992
    • Micu, I.1    Jiang, Q.2    Coderre, E.3    Ridsdale, A.4    Zhang, L.5    Woulfe, J.6
  • 35
    • 11644261806 scopus 로고    scopus 로고
    • Morris, G.M., Goodsell, D.S., Halliday, R.S., Huey, R., Hart, W.E., Below, R.K., and Olson, A.J. 1998. Automated docking using a Lamarckian genetic algorithm and an empirical binding free energy function. J. Comput. Chem. 19: 1639-1662. doi:10.1002/(SICI)1096-987X(19981115)19:14〈1639::AID- JCC10〉3.0.CO;2-B.
    • Morris, G.M., Goodsell, D.S., Halliday, R.S., Huey, R., Hart, W.E., Below, R.K., and Olson, A.J. 1998. Automated docking using a Lamarckian genetic algorithm and an empirical binding free energy function. J. Comput. Chem. 19: 1639-1662. doi:10.1002/(SICI)1096-987X(19981115)19:14〈1639::AID- JCC10〉3.0.CO;2-B.
  • 36
    • 0036195791 scopus 로고    scopus 로고
    • Paclitaxel (Taxol) attenuates clinical disease in a spontaneously demyelinating transgenic mouse and induces remyelination
    • PMID:11990870, doi:10.1191/1352458502ms776oa
    • Moscarello, M.A., Mak, B., Nguyen, T.A., Wood, D.D., Mastronardi, F., and Ludwin, S.K. 2002a. Paclitaxel (Taxol) attenuates clinical disease in a spontaneously demyelinating transgenic mouse and induces remyelination. Mult. Scler. 8: 130-138. doi:10.1191/1352458502ms776oa. PMID:11990870.
    • (2002) Mult. Scler , vol.8 , pp. 130-138
    • Moscarello, M.A.1    Mak, B.2    Nguyen, T.A.3    Wood, D.D.4    Mastronardi, F.5    Ludwin, S.K.6
  • 37
    • 0036316687 scopus 로고    scopus 로고
    • Peptidylarginine deiminase: A candidate factor in demyelinating disease
    • PMID:12064481, doi:10.1046/j.1471-4159.2002.00834.x
    • Moscarello, M.A., Pritzker, L., Mastronardi, F.G., and Wood, D.D. 2002b. Peptidylarginine deiminase: a candidate factor in demyelinating disease. J. Neurochem. 81: 335-343. doi:10.1046/j.1471-4159.2002.00834.x. PMID:12064481.
    • (2002) J. Neurochem , vol.81 , pp. 335-343
    • Moscarello, M.A.1    Pritzker, L.2    Mastronardi, F.G.3    Wood, D.D.4
  • 38
    • 34248681263 scopus 로고    scopus 로고
    • Molecular "negativity" may underlie multiple sclerosis: Role of the myelin basic protein family in the pathogenesis of MS
    • PMID:17531841, doi:10.1016/S0074-7742(07)79007-4
    • Musse, A.A., and Harauz, G. 2007. Molecular "negativity" may underlie multiple sclerosis: role of the myelin basic protein family in the pathogenesis of MS. Int. Rev. Neurobiol. 79: 149-172. doi:10.1016/S0074-7742(07)79007-4. PMID:17531841.
    • (2007) Int. Rev. Neurobiol , vol.79 , pp. 149-172
    • Musse, A.A.1    Harauz, G.2
  • 39
    • 33645210449 scopus 로고    scopus 로고
    • Deimination of membrane-bound myelin basic protein in multiple sclerosis exposes an immunodominant epitope
    • PMID: 16537438, doi:10.1073/pnas.0509158103
    • Musse, A.A., Boggs, J.M., and Harauz, G. 2006. Deimination of membrane-bound myelin basic protein in multiple sclerosis exposes an immunodominant epitope. Proc. Natl. Acad. Sci. U.S.A. 103: 4422-4427. doi:10.1073/pnas.0509158103. PMID: 16537438.
    • (2006) Proc. Natl. Acad. Sci. U.S.A , vol.103 , pp. 4422-4427
    • Musse, A.A.1    Boggs, J.M.2    Harauz, G.3
  • 40
    • 54249146523 scopus 로고    scopus 로고
    • Peptidylarginine deiminase 2 (PAD2) expression in a transgenic mouse leads to specific central nervous system (CNS) myelin instability. Disease Models and Mechanisms
    • Accepted for publication
    • Musse, A.A., Li, Z., Ackerley, C.A., Bienzle, D., Lei, H., Poma, R., et al. 2008. Peptidylarginine deiminase 2 (PAD2) expression in a transgenic mouse leads to specific central nervous system (CNS) myelin instability. Disease Models and Mechanisms. Accepted for publication.
    • (2008)
    • Musse, A.A.1    Li, Z.2    Ackerley, C.A.3    Bienzle, D.4    Lei, H.5    Poma, R.6
  • 41
    • 12944329841 scopus 로고    scopus 로고
    • Peptidylarginine deiminase isoforms 1-3 are expressed in the epidermis and involved in the deimination of K1 and filaggrin
    • PMID:15675958, doi:10.1111/j.0022-202X.2004.23568.x
    • Nachat, R., Mechin, M.C., Takahara, H., Chavanas, S., Charveron, M., Serre, G., and Simon, M. 2005. Peptidylarginine deiminase isoforms 1-3 are expressed in the epidermis and involved in the deimination of K1 and filaggrin. J. Invest. Dermatol. 124: 384-393. doi:10.1111/j.0022-202X.2004.23568.x. PMID:15675958.
    • (2005) J. Invest. Dermatol , vol.124 , pp. 384-393
    • Nachat, R.1    Mechin, M.C.2    Takahara, H.3    Chavanas, S.4    Charveron, M.5    Serre, G.6    Simon, M.7
  • 42
    • 19944417554 scopus 로고    scopus 로고
    • Comparison of enzymatic properties between hPADI2 and hPADI4
    • PMID:15629448, doi:10.1016/j.bbrc. 2004.11.152
    • Nakayama-Hamada, M., Suzuki, A., Kubota, K., Takazawa, T., Ohsaka, M., Kawaida, R., et al. 2005. Comparison of enzymatic properties between hPADI2 and hPADI4. Biochem. Biophys. Res. Commun. 327: 192-200. doi:10.1016/j.bbrc. 2004.11.152. PMID:15629448.
    • (2005) Biochem. Biophys. Res. Commun , vol.327 , pp. 192-200
    • Nakayama-Hamada, M.1    Suzuki, A.2    Kubota, K.3    Takazawa, T.4    Ohsaka, M.5    Kawaida, R.6
  • 43
    • 34047223452 scopus 로고    scopus 로고
    • Sources of axonal calcium loading during in vitro ischemia of rat dorsal roots
    • PMID:17206661, doi:10.1002/mus.20731
    • Petrescu, N., Micu, I., Malek, S., Ouardouz, M., and Stys, P.K. 2007. Sources of axonal calcium loading during in vitro ischemia of rat dorsal roots. Muscle Nerve, 35: 451-457. doi:10.1002/mus.20731. PMID:17206661.
    • (2007) Muscle Nerve , vol.35 , pp. 451-457
    • Petrescu, N.1    Micu, I.2    Malek, S.3    Ouardouz, M.4    Stys, P.K.5
  • 44
    • 0032517246 scopus 로고    scopus 로고
    • A novel microtubule independent effect of paclitaxel: The inhibition of peptidylarginine deiminase from bovine brain
    • PMID:9774721
    • Pritzker, L.B., and Moscarello, M.A. 1998. A novel microtubule independent effect of paclitaxel: the inhibition of peptidylarginine deiminase from bovine brain. Biochim. Biophys. Acta, 1388: 154-160. PMID:9774721.
    • (1998) Biochim. Biophys. Acta , vol.1388 , pp. 154-160
    • Pritzker, L.B.1    Moscarello, M.A.2
  • 45
    • 0033553648 scopus 로고    scopus 로고
    • The developmental expression and activity of peptidylarginine deiminase in the mouse
    • PMID:10465698, doi:10.1016/S0304-3940(99)00276-1
    • Pritzker, L.B., Nguyen, T.A., and Moscarello, M.A. 1999. The developmental expression and activity of peptidylarginine deiminase in the mouse. Neurosci. Lett. 266: 161-164. doi:10.1016/S0304-3940(99)00276-1. PMID:10465698.
    • (1999) Neurosci. Lett , vol.266 , pp. 161-164
    • Pritzker, L.B.1    Nguyen, T.A.2    Moscarello, M.A.3
  • 46
    • 33746844946 scopus 로고    scopus 로고
    • Experimental autoimmune encephalomyelitis induction in peptidylarginine deiminase 2 knockout mice
    • PMID:16856138, doi:10.1002/cne.21055
    • Raijmakers, R., Vogelzangs, J., Raats, J., Panzenbeck, M., Corby, M., Jiang, H., et al. 2006. Experimental autoimmune encephalomyelitis induction in peptidylarginine deiminase 2 knockout mice. J. Comp. Neurol. 498: 217-226. doi:10.1002/cne.21055. PMID:16856138.
    • (2006) J. Comp. Neurol , vol.498 , pp. 217-226
    • Raijmakers, R.1    Vogelzangs, J.2    Raats, J.3    Panzenbeck, M.4    Corby, M.5    Jiang, H.6
  • 47
    • 33847759102 scopus 로고    scopus 로고
    • Methylation of arginine residues interferes with citrullination by peptidylarginine deiminases in vitro
    • PMID:17303166, doi:10.1016/j.jmb.2007.01.054
    • Raijmakers, R., Zendman, A.J., Egberts, W.V., Vossenaar, E.R., Raats, J., Soede-Huijbregts, C., et al. 2007. Methylation of arginine residues interferes with citrullination by peptidylarginine deiminases in vitro. J. Mol. Biol. 367: 1118-1129. doi:10.1016/j.jmb.2007.01.054. PMID:17303166.
    • (2007) J. Mol. Biol , vol.367 , pp. 1118-1129
    • Raijmakers, R.1    Zendman, A.J.2    Egberts, W.V.3    Vossenaar, E.R.4    Raats, J.5    Soede-Huijbregts, C.6
  • 48
    • 27144463085 scopus 로고    scopus 로고
    • Inactivation of two diverse enzymes in the amidinotransferase superfamily by 2-chloroacetamidine: Dimethylargininase and peptidylarginine deiminase
    • PMID:16229464, doi:10.1021/bi051341y
    • Stone, E.M., Schaller, T.H., Bianchi, H., Person, M.D., and Fast, W. 2005. Inactivation of two diverse enzymes in the amidinotransferase superfamily by 2-chloroacetamidine: dimethylargininase and peptidylarginine deiminase. Biochemistry, 44: 13744-13752. doi:10.1021/bi051341y. PMID:16229464.
    • (2005) Biochemistry , vol.44 , pp. 13744-13752
    • Stone, E.M.1    Schaller, T.H.2    Bianchi, H.3    Person, M.D.4    Fast, W.5
  • 49
    • 0042667153 scopus 로고    scopus 로고
    • Functional haplotypes of PADI4, encoding citrullinating enzyme peptidylarginine deiminase 4, are associated with rheumatoid arthritis
    • PMID:12833157, doi:10.1038/ng1206
    • Suzuki, A., Yamada, R., Chang, X., Tokuhiro, S., Sawada, T., Suzuki, M., et al. 2003. Functional haplotypes of PADI4, encoding citrullinating enzyme peptidylarginine deiminase 4, are associated with rheumatoid arthritis. Nat. Genet. 34: 395-402. doi:10.1038/ng1206. PMID:12833157.
    • (2003) Nat. Genet , vol.34 , pp. 395-402
    • Suzuki, A.1    Yamada, R.2    Chang, X.3    Tokuhiro, S.4    Sawada, T.5    Suzuki, M.6
  • 50
    • 33846917186 scopus 로고
    • Subcellular location of peptidylarginine deiminase in the mouse brain
    • Takahara, H., Koyama, M., and Sugawara, K. 1987. Subcellular location of peptidylarginine deiminase in the mouse brain. Agric. Biol. Chem. 51: 1471-1473.
    • (1987) Agric. Biol. Chem , vol.51 , pp. 1471-1473
    • Takahara, H.1    Koyama, M.2    Sugawara, K.3
  • 51
    • 0027968068 scopus 로고
    • CLUSTAL W: Improving the sensitivity of progressive multiple sequence alignment through sequence weighting, position-specific gap penalties, and weight matrix choice
    • PMID:7984417, doi:10.1093/nar/22.22.4673
    • Thompson, J.D., Higgins, D.G., and Gibson, T.J. 1994. CLUSTAL W: improving the sensitivity of progressive multiple sequence alignment through sequence weighting, position-specific gap penalties, and weight matrix choice. Nucleic Acids Res. 22: 4673-4680. doi:10.1093/nar/22.22.4673. PMID:7984417.
    • (1994) Nucleic Acids Res , vol.22 , pp. 4673-4680
    • Thompson, J.D.1    Higgins, D.G.2    Gibson, T.J.3
  • 52
    • 0026544923 scopus 로고
    • Immunohistochemical localization of peptidylarginine deiminase in the rat brain
    • PMID:1586471, doi:10.1016/0891-0618(92)90041-N
    • Vincent, S.R., Leung, E., and Watanabe, K. 1992. Immunohistochemical localization of peptidylarginine deiminase in the rat brain. J. Chem. Neuroanat. 5: 159-168. doi:10.1016/0891-0618(92)90041-N. PMID:1586471.
    • (1992) J. Chem. Neuroanat , vol.5 , pp. 159-168
    • Vincent, S.R.1    Leung, E.2    Watanabe, K.3
  • 53
    • 0242720407 scopus 로고    scopus 로고
    • PAD, a growing family of citrullinating enzymes: Genes, features, and involvement in disease
    • PMID:14579251, doi:10.1002/bies.10357
    • Vossenaar, E.R., Zendman, A.J., van Venrooij, W.J., and Pruijn, G.J. 2003. PAD, a growing family of citrullinating enzymes: genes, features, and involvement in disease. Bioessays, 25: 1106-1118. doi:10.1002/bies.10357. PMID:14579251.
    • (2003) Bioessays , vol.25 , pp. 1106-1118
    • Vossenaar, E.R.1    Zendman, A.J.2    van Venrooij, W.J.3    Pruijn, G.J.4
  • 54
    • 0024281847 scopus 로고
    • Combined biochemical and immunochemical comparison of peptidylarginine deiminases present in various tissues
    • PMID: 3416014
    • Watanabe, K., Akiyama, K., Hikichi, K., Ohtsuka, R., Okuyama, A., and Senshu, T. 1988. Combined biochemical and immunochemical comparison of peptidylarginine deiminases present in various tissues. Biochim. Biophys. Acta, 966: 375-383. PMID: 3416014.
    • (1988) Biochim. Biophys. Acta , vol.966 , pp. 375-383
    • Watanabe, K.1    Akiyama, K.2    Hikichi, K.3    Ohtsuka, R.4    Okuyama, A.5    Senshu, T.6
  • 55
    • 41149143688 scopus 로고    scopus 로고
    • Myelin localization of peptidylarginine deiminases 2 and 4: Comparison of PAD2 and PAD4 activities
    • PMID:18227806, doi:10.1038/labinvest.3700748
    • Wood, D.D., Ackerley, C.A., Brand, B., Zhang, L., Raijmakers, R., Mastronardi, F.G., and Moscarello, M.A. 2008. Myelin localization of peptidylarginine deiminases 2 and 4: comparison of PAD2 and PAD4 activities. Lab. Invest. 88: 354-364. doi:10.1038/labinvest.3700748. PMID:18227806.
    • (2008) Lab. Invest , vol.88 , pp. 354-364
    • Wood, D.D.1    Ackerley, C.A.2    Brand, B.3    Zhang, L.4    Raijmakers, R.5    Mastronardi, F.G.6    Moscarello, M.A.7
  • 56
    • 34548415797 scopus 로고    scopus 로고
    • ABAP: Antibody-based assay for peptidylarginine deiminase activity
    • PMID:17716614, doi:10.1016/j.ab.2007. 07.009
    • Zendman, A.J., Raijmakers, R., Nijenhuis, S., Vossenaar, E.R., Tillaart, M., Chirivi, R.G., et al. 2007. ABAP: antibody-based assay for peptidylarginine deiminase activity. Anal. Biochem. 369: 232-240. doi:10.1016/j.ab.2007. 07.009. PMID:17716614.
    • (2007) Anal. Biochem , vol.369 , pp. 232-240
    • Zendman, A.J.1    Raijmakers, R.2    Nijenhuis, S.3    Vossenaar, E.R.4    Tillaart, M.5    Chirivi, R.G.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.