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Volumn 29, Issue 47, 2009, Pages 14869-14880

Peptidyl-prolyl isomerase 1 regulates protein phosphatase 2A-mediated topographic phosphorylation of neurofilament proteins

Author keywords

[No Author keywords available]

Indexed keywords

CYCLIN DEPENDENT KINASE 5; FOSTRIECIN; MICROCYSTIN LR; MITOGEN ACTIVATED PROTEIN KINASE; NEUROFILAMENT PROTEIN; OKADAIC ACID; PEPTIDYLPROLYL ISOMERASE; PEPTIDYLPROLYL ISOMERASE PIN1; PHOSPHOPROTEIN PHOSPHATASE 2A; SERINE; STRESS ACTIVATED PROTEIN KINASE; THREONINE;

EID: 72449200109     PISSN: 02706474     EISSN: 15292401     Source Type: Journal    
DOI: 10.1523/JNEUROSCI.4469-09.2009     Document Type: Article
Times cited : (29)

References (59)
  • 2
    • 0035253619 scopus 로고    scopus 로고
    • Juglone, an inhibitor of the peptidyl-prolyl isomerase Pin1, also directly blocks transcription
    • Chao SH, Greenleaf AL, Price DH (2001) Juglone, an inhibitor of the peptidyl-prolyl isomerase Pin1, also directly blocks transcription. Nucleic Acids Res 29:767-773.
    • (2001) Nucleic Acids Res , vol.29 , pp. 767-773
    • Chao, S.H.1    Greenleaf, A.L.2    Price, D.H.3
  • 3
    • 0025514319 scopus 로고
    • Transfected rat high-molecular-weight neurofilament (NF-H) coassembles with vimentin in a predominantly nonphosphorylated form
    • Chin SS, Liem RK (1990) Transfected rat high-molecular-weight neurofilament (NF-H) coassembles with vimentin in a predominantly nonphosphorylated form. J Neurosci 10:3714-3726.
    • (1990) J Neurosci , vol.10 , pp. 3714-3726
    • Chin, S.S.1    Liem, R.K.2
  • 4
    • 0036316279 scopus 로고    scopus 로고
    • Myelin-associated glycoprotein modulates expression and phosphorylation of neuronal cytoskeletal elements and their associated kinases
    • Dashiell SM, Tanner SL, Pant HC, Quarles RH (2002) Myelin-associated glycoprotein modulates expression and phosphorylation of neuronal cytoskeletal elements and their associated kinases. J Neurochem 81:1263-1272.
    • (2002) J Neurochem , vol.81 , pp. 1263-1272
    • Dashiell, S.M.1    Tanner, S.L.2    Pant, H.C.3    Quarles, R.H.4
  • 5
    • 0026580004 scopus 로고
    • Local modulation of neurofilament phosphorylation, axonal caliber and slow axonal transport by mylenating Schwann cells
    • de Waegh SM, Lee VM, Brady ST (1992) Local modulation of neurofilament phosphorylation, axonal caliber and slow axonal transport by mylenating Schwann cells. Cell 68:451 463.
    • (1992) Cell , vol.68 , pp. 451-463
    • De Waegh, S.M.1    Lee, V.M.2    Brady, S.T.3
  • 8
    • 52049111869 scopus 로고    scopus 로고
    • Juglone inactivates cysteine-rich proteins required for progression through mitosis
    • Fila C, Metz C, van der Sluijs P (2008) Juglone inactivates cysteine-rich proteins required for progression through mitosis. J Biol Chem 283:21714-21724.
    • (2008) J Biol Chem , vol.283 , pp. 21714-21724
    • Fila, C.1    Metz, C.2    Van Der Sluijs, P.3
  • 9
    • 0022616904 scopus 로고
    • Cytoskeletal protein abnormalities in neurodegenerative diseases
    • Goldman JE, Yen SH (1986) Cytoskeletal protein abnormalities in neurodegenerative diseases. Ann Neurol 19:209-223.
    • (1986) Ann Neurol , vol.19 , pp. 209-223
    • Goldman, J.E.1    Yen, S.H.2
  • 10
    • 0034433275 scopus 로고    scopus 로고
    • Neurofilament protein synthesis and phosphorylation
    • Grant P, Pant HC (2000) Neurofilament protein synthesis and phosphorylation. J Neurocytol 29:843-872.
    • (2000) J Neurocytol , vol.29 , pp. 843-872
    • Grant, P.1    Pant, H.C.2
  • 12
    • 34250635347 scopus 로고    scopus 로고
    • Protein kinase C-mediated down-regulation of cyclin D1 involves activation of the translational repressor 4E-BP1 via a phosphoinositide 3-kinase/Akt-independent, protein phosphatase 2A-dependent mechanism in intestinal epithelial cells
    • DOI 10.1074/jbc.M610513200
    • Guan L, Song K, Pysz MA, Curry KJ, Hizli AA, Danielpour D, Black AR, Black JD (2007) Protein kinase C-mediated down-regulation of cyclin D1 involves activation of the translational repressor 4E-BP1 via a phosphoinositide 3-kinase/Akt-independent, protein phosphatase 2A-dependent mechanism in intestinal epithelial cells. J Biol Chem 282:14213-14225. (Pubitemid 47100475)
    • (2007) Journal of Biological Chemistry , vol.282 , Issue.19 , pp. 14213-14225
    • Guan, L.1    Song, K.2    Pysz, M.A.3    Curry, K.J.4    Hizli, A.A.5    Danielpour, D.6    Black, A.R.7    Black, J.D.8
  • 13
    • 0026056514 scopus 로고
    • Effect of chronic ethanol ingestion on phosphate content of NF proteins and NF associated protein phosphatase in rat spinal cord
    • Guru SC, Shetty KT, Shankar SK (1991) Effect of chronic ethanol ingestion on phosphate content of NF proteins and NF associated protein phosphatase in rat spinal cord. Neurochem Res 16:1193-1197.
    • (1991) Neurochem Res , vol.16 , pp. 1193-1197
    • Guru, S.C.1    Shetty, K.T.2    Shankar, S.K.3
  • 14
    • 0026042995 scopus 로고
    • Cytopathology of amyotrophic lateral sclerosis
    • Hirano A (1991) Cytopathology of amyotrophic lateral sclerosis. Adv Neurol 56:91-101.
    • (1991) Adv Neurol , vol.56 , pp. 91-101
    • Hirano, A.1
  • 16
    • 0016541063 scopus 로고
    • The slow component of axonal transport. Identification of major structural polypeptides of the axon and their generality among mammalian neurons
    • Hoffman PN, Lasek RJ (1975) The slow component of axonal transport. Identification of major structural polypeptides of the axon and their generality among mammalian neurons. J Cell Biol 66:351-366.
    • (1975) J Cell Biol , vol.66 , pp. 351-366
    • Hoffman, P.N.1    Lasek, R.J.2
  • 17
    • 0032542058 scopus 로고    scopus 로고
    • Characterization of serine and threonine phosphorylation sites in beta- elimination/ethanethiol addition-modified proteins by electrospray tandem mass spectrometry and database searching
    • DOI 10.1021/bi981264p
    • Jaffe H, Veeranna, Pant HC (1998) Characterization of serine and threonine phosphorylation sites in beta-elimination/ethanethiol addition-modified proteins by electrospray tandem mass spectrometry and database searching. Biochemistry 37:16211-16224. (Pubitemid 28536257)
    • (1998) Biochemistry , vol.37 , Issue.46 , pp. 16211-16224
    • Jaffe, H.1    Veeranna2    Pant, H.C.3
  • 18
    • 0029366767 scopus 로고
    • A role of neurofilaments in the pathogenesis of amyotrophic lateral sclerosis
    • Julien JP (1995) A role of neurofilaments in the pathogenesis of amyotrophic lateral sclerosis. Biochem Cell Biol 73:593-597.
    • (1995) Biochem Cell Biol , vol.73 , pp. 593-597
    • Julien, J.P.1
  • 19
    • 19544366223 scopus 로고    scopus 로고
    • Neurofilament subunits undergo more rapid translocation within retinas than in optic axons
    • DOI 10.1016/j.molbrainres.2003.10.008, PII S0169328X03004686
    • Jung C, Shea TB (2004) Neurofilament subunits undergo more rapid translocation within retinas than in optic axons. Brain Res Mol Brain Res 122:188-192. (Pubitemid 38317077)
    • (2004) Molecular Brain Research , vol.122 , Issue.2 , pp. 188-192
    • Jung, C.1    Shea, T.B.2
  • 21
    • 0042679510 scopus 로고    scopus 로고
    • Activation of the ERK and JNK signaling pathways caused by neuron-specific inhibition of PP2A in transgenic mice
    • Kins S, Kurosinski P, Nitsch RM, Götz J (2003) Activation of the ERK and JNK signaling pathways caused by neuron-specific inhibition of PP2A in transgenic mice. Am J Pathol 163:833-843. (Pubitemid 37040120)
    • (2003) American Journal of Pathology , vol.163 , Issue.3 , pp. 833-843
    • Kins, S.1    Kurosinski, P.2    Nitsch, R.M.3    Gotz, J.4
  • 22
    • 0023931776 scopus 로고
    • Identification and quantification of calcium-binding proteins in squid axoplasm
    • Krinks MH, Klee CB, Pant HC, Gainer H (1988) Identification and quantification of calcium-binding proteins in squid axoplasm. J Neurosci 8:2172-2182. (Pubitemid 18162724)
    • (1988) Journal of Neuroscience , vol.8 , Issue.6 , pp. 2172-2182
    • Krinks, M.H.1    Klee, C.B.2    Pant, H.C.3    Gainer, H.4
  • 23
    • 61349151785 scopus 로고    scopus 로고
    • Prolyl isomerase Pin1 is highly expressed in Her2-positive breast cancer and regulates erbB2 protein stability
    • Lam PB, Burga LN, Wu BP, Hofstatter EW, Lu KP, Wulf GM (2008) Prolyl isomerase Pin1 is highly expressed in Her2-positive breast cancer and regulates erbB2 protein stability. Mol Cancer 7:91.
    • (2008) Mol Cancer , vol.7 , pp. 91
    • Lam, P.B.1    Burga, L.N.2    Wu, B.P.3    Hofstatter, E.W.4    Lu, K.P.5    Wulf, G.M.6
  • 25
    • 27644478606 scopus 로고    scopus 로고
    • Contributions of protein phosphatases PP1, PP2A, PP2B and PP5 to the regulation of tau phosphorylation
    • DOI 10.1111/j.1460-9568.2005.04391.x
    • Liu F, Grundke-Iqbal I, Iqbal K, Gong CX (2005) Contributions of protein phosphatases PP1, PP2A, PP2B and PP5 to the regulation of tau phosphorylation. Eur J Neurosci 22:1942-1950. (Pubitemid 41579384)
    • (2005) European Journal of Neuroscience , vol.22 , Issue.8 , pp. 1942-1950
    • Liu, F.1    Grundke-Iqbal, I.2    Iqbal, K.3    Gong, C.-X.4
  • 26
    • 35448945269 scopus 로고    scopus 로고
    • The prolyl isomerase PIN1: A pivotal new twist in phosphorylation signaling and disease
    • Lu KP, Zhou XZ (2007) The prolyl isomerase PIN1: a pivotal new twist in phosphorylation signaling and disease. Nat Rev Mol Cell Biol 8:904-916.
    • (2007) Nat Rev Mol Cell Biol , vol.8 , pp. 904-916
    • Lu, K.P.1    Zhou, X.Z.2
  • 27
    • 0033600242 scopus 로고    scopus 로고
    • The prolyl isomerase Pin1 restores the function of Alzheimer-associated phosphorylated tau protein
    • DOI 10.1038/21650
    • Lu PJ, Wulf G, Zhou XZ, Davies P, Lu KP (1999) The prolyl isomerase Pin1 restores the function of Alzheimer-associated phosphorylated tau protein. Nature 399:784-788. (Pubitemid 29293174)
    • (1999) Nature , vol.399 , Issue.6738 , pp. 784-788
    • Lu, P.-J.1    Wulf, G.2    Zhou, X.Z.3    Davies, P.4    Lu, K.P.5
  • 29
    • 0026529403 scopus 로고
    • Phosphorylation dependent neurofilament epitopes are reduced at the node of Ranvier
    • Mata M, Kupina N, Fink DJ (1992) Phosphorylation dependent neurofilament epitopes are reduced at the node of Ranvier. J Neurocytol 21:199-210.
    • (1992) J Neurocytol , vol.21 , pp. 199-210
    • Mata, M.1    Kupina, N.2    Fink, D.J.3
  • 30
    • 0023148301 scopus 로고
    • Posttranslational modification of neurofilament proteins by phosphate during axoplasmic transport in retinal ganglion cell neurons
    • Nixon RA, Lewis SE, Marotta CA (1987) Posttranslational modification of neurofilament proteins by phosphate during axoplasmic transport in retinal ganglion cell neurons. J Neurosci 7:1145-1158.
    • (1987) J Neurosci , vol.7 , pp. 1145-1158
    • Nixon, R.A.1    Lewis, S.E.2    Marotta, C.A.3
  • 31
  • 32
    • 0038632271 scopus 로고    scopus 로고
    • Defective neurofilament transport in mouse models of amyotrophic lateral sclerosis: A review
    • Rao MV, Nixon RA (2003) Defective neurofilament transport in mouse models of amyotrophic lateral sclerosis: a review. Neurochem Res 28:1041-1047.
    • (2003) Neurochem Res , vol.28 , pp. 1041-1047
    • Rao, M.V.1    Nixon, R.A.2
  • 33
    • 72449212469 scopus 로고    scopus 로고
    • Phosphorylation-specific peptidyl-prolyl isomerization of neuronal cytoskeletal proteins by Pin1: Implications for therapeutics in neurodegeneration
    • Advance online publication. Retrieved November 12, 2009. doi:10.3233/JAD-2009-1243
    • Rudrabhatla P, Pant HC (2009) Phosphorylation-specific peptidyl-prolyl isomerization of neuronal cytoskeletal proteins by Pin1: implications for therapeutics in neurodegeneration. J Alzheimers Dis. Advance online publication. Retrieved November 12, 2009. doi:10.3233/JAD-2009-1243.
    • (2009) J Alzheimers Dis.
    • Rudrabhatla, P.1    Pant, H.C.2
  • 34
    • 55549124552 scopus 로고    scopus 로고
    • Pin1-dependent prolyl isomerization modulates the stress-induced phosphorylation of high molecular weight neurofilament protein
    • Rudrabhatla P, Zheng YL, Amin ND, Kesavapany S, Albers W, Pant HC (2008) Pin1-dependent prolyl isomerization modulates the stress-induced phosphorylation of high molecular weight neurofilament protein. J Biol Chem 283:26737-26747.
    • (2008) J Biol Chem , vol.283 , pp. 26737-26747
    • Rudrabhatla, P.1    Zheng, Y.L.2    Amin, N.D.3    Kesavapany, S.4    Albers, W.5    Pant, H.C.6
  • 35
    • 0036315162 scopus 로고    scopus 로고
    • PIN1 is an E2F target gene essential for Neu/Ras-induced transformation of mammary epithelial cells
    • DOI 10.1128/MCB.22.15.5281-5295.2002
    • Ryo A, Liou YC, Wulf G, Nakamura M, Lee SW, Lu KP (2002) PIN1 is an E2F target gene essential for Neu/Ras-induced transformation of mammary epithelial cells. Mol Cell Biol 22:5281-5295. (Pubitemid 34755742)
    • (2002) Molecular and Cellular Biology , vol.22 , Issue.15 , pp. 5281-5295
    • Ryo, A.1    Liou, Y.-C.2    Wulf, G.3    Nakamura, M.4    Lee, S.W.5    Lu, K.P.6
  • 36
    • 0026779629 scopus 로고
    • Okadaic acid induces the rapid and reversible disruption of the neurofilament network in rat dorsal root ganglion neurons
    • Sacher MG, Athlan ES, Mushynski WE (1992) Okadaic acid induces the rapid and reversible disruption of the neurofilament network in rat dorsal root ganglion neurons. Biochem Biophys Res Commun 186:524-530.
    • (1992) Biochem Biophys Res Commun , vol.186 , pp. 524-530
    • Sacher, M.G.1    Athlan, E.S.2    Mushynski, W.E.3
  • 37
    • 0028227860 scopus 로고
    • Increased phosphorylation of the amino-terminal domain of the low molecular weight neurofilament subunit in okadaic acid-treated neurons
    • Sacher MG, Athlan ES, Mushynski WE (1994) Increased phosphorylation of the amino-terminal domain of the low molecular weight neurofilament subunit in okadaic acid-treated neurons. J Biol Chem 269:18480-18484.
    • (1994) J Biol Chem , vol.269 , pp. 18480-18484
    • Sacher, M.G.1    Athlan, E.S.2    Mushynski, W.E.3
  • 38
    • 0024570237 scopus 로고
    • Detection and partial characterization of a developmentally regulated nuclear antigen in neural cells in vitro and in vivo
    • Schilling K, Duvernoy C, Keck S, Pilgrim C (1989) Detection and partial characterization of a developmentally regulated nuclear antigen in neural cells in vitro and in vivo. J Histochem Cytochem 37:241-247.
    • (1989) J Histochem Cytochem , vol.37 , pp. 241-247
    • Schilling, K.1    Duvernoy, C.2    Keck, S.3    Pilgrim, C.4
  • 39
    • 0027164845 scopus 로고
    • The protein phosphatase inhibitor okadaic acid increases axonal neurofilaments and neurite caliber, and decreases axonal microtubules in NB2a/d1 cells
    • Shea TB, Paskevich PA, Beermann ML (1993) The protein phosphatase inhibitor okadaic acid increases axonal neurofilaments and neurite caliber, and decreases axonal microtubules in NB2a/d1 cells. J Neurosci Res 35:507-521.
    • (1993) J Neurosci Res , vol.35 , pp. 507-521
    • Shea, T.B.1    Paskevich, P.A.2    Beermann, M.L.3
  • 40
    • 2642524580 scopus 로고    scopus 로고
    • Cyclin-dependent kinase 5 increases perikaryal neurofilament phosphorylation and inhibits neurofilament axonal transport
    • Shea TB, Zheng YL, Ortiz D, Pant HC (2004) Cyclin-dependent kinase 5 increases perikaryal neurofilament phosphorylation and inhibits neurofilament axonal transport. J Neurosci Res 76:795-800.
    • (2004) J Neurosci Res , vol.76 , pp. 795-800
    • Shea, T.B.1    Zheng, Y.L.2    Ortiz, D.3    Pant, H.C.4
  • 41
    • 0026529602 scopus 로고
    • Effect of chronic ethanol ingestion on phosphate content of neurofilament proteins and neurofilament associated protein phosphatase in rat spinal cord
    • Shetty KT, Veeranna, Guru SC (1992) Effect of chronic ethanol ingestion on phosphate content of neurofilament proteins and neurofilament associated protein phosphatase in rat spinal cord. Neurosci Lett 137:83-86.
    • (1992) Neurosci Lett , vol.137 , pp. 83-86
    • Shetty, K.T.1    Veeranna2    Guru, S.C.3
  • 42
    • 0026276683 scopus 로고
    • The regulation and function of protein phosphatases in the brain
    • Sim ATR (1991) The regulation and function of protein phosphatases in the brain. Mol Neurobiol 5:229-246.
    • (1991) Mol Neurobiol , vol.5 , pp. 229-246
    • Sim, A.T.R.1
  • 43
  • 45
    • 0030684714 scopus 로고    scopus 로고
    • Protein serine/threonine phosphatase 1 and 2A associate with and dephosphorylate neurofilaments
    • DOI 10.1016/S0169-328X(97)00117-4, PII S0169328X97001174
    • Strack S, Westphal RS, Colbran RJ, Ebner FF, Wadzinski BE (1997) Protein serine/threonine phosphatase 1 and 2A associate with and dephosphorylate neurofilaments. Brain Res Mol Brain Res 49:15-28. (Pubitemid 27453110)
    • (1997) Molecular Brain Research , vol.49 , Issue.1-2 , pp. 15-28
    • Strack, S.1    Westphal, R.S.2    Colbran, R.J.3    Ebner, F.F.4    Wadzinski, B.E.5
  • 46
    • 23844538993 scopus 로고    scopus 로고
    • The pathobiology of amyotrophic lateral sclerosis: A proteinopathy?
    • Strong MJ, Kesavapany S, Pant HC (2005) The pathobiology of amyotrophic lateral sclerosis: a proteinopathy? J Neuropathol Exp Neurol 64:649-664.
    • (2005) J Neuropathol Exp Neurol , vol.64 , pp. 649-664
    • Strong, M.J.1    Kesavapany, S.2    Pant, H.C.3
  • 48
    • 0029022205 scopus 로고
    • Neuronal cyclin-dependent kinase-5 phosphorylation sites in neurofilament protein (NF-H) are dephosphorylated by protein phosphatase 2A
    • Veeranna, Shetty KT, Link WT, Jaffe H, Wang J, Pant HC (1995) Neuronal cyclin-dependent kinase-5 phosphorylation sites in neurofilament protein (NF-H) are dephosphorylated by protein phosphatase 2A. J Neurochem 64:2681-2690.
    • (1995) J Neurochem , vol.64 , pp. 2681-2690
    • Veeranna Shetty, K.T.1    Link, W.T.2    Jaffe, H.3    Wang, J.4    Pant, H.C.5
  • 49
    • 0032100631 scopus 로고    scopus 로고
    • Mitogen-activated protein kinases (Erk1,2) phosphorylate lys-ser-pro (KSP) repeats in neurofilament proteins NF-H and NF-M
    • Veeranna, Amin ND, Ahn NG, Jaffe H, Winters CA, Grant P, Pant HC (1998) Mitogen-activated protein kinases (Erk1,2) phosphorylate Lys- Ser-Pro (KSP) repeats in neurofilament proteins NF-H and NF-M. J Neurosci 18:4008-4021. (Pubitemid 28243798)
    • (1998) Journal of Neuroscience , vol.18 , Issue.11 , pp. 4008-4021
    • Veeranna1    Amin, N.D.2    Ahn, N.G.3    Jaffe, H.4    Winters, C.A.5    Grant, P.6    Pant, H.C.7
  • 50
    • 0035075793 scopus 로고    scopus 로고
    • PP2A mRNA expression is quantitatively decreased in Alzheimer's disease hippocampus
    • DOI 10.1006/exnr.2001.7630
    • Vogelsberg-Ragaglia V, Schuck T, Trojanowski JQ, Lee VM (2001) PP2A mRNA expression is quantitatively decreased in Alzheimer's disease hippocampus. Exp Neurol 168:402-412. (Pubitemid 32289776)
    • (2001) Experimental Neurology , vol.168 , Issue.2 , pp. 402-412
    • Vogelsberg-Ragaglia, V.1    Schuck, T.2    Trojanowski, J.Q.3    Lee, V.M.-Y.4
  • 51
    • 0033776708 scopus 로고    scopus 로고
    • Rapid movement of axonal neurofilaments interrupted by prolonged pauses
    • DOI 10.1038/35004008
    • Wang L, Ho CL, Sun D, Liem RKH, Brown A (2000) Rapid movement of axonal neurofilaments interrupted by prolonged pauses. Nat Cell Biol 2:137-141. (Pubitemid 30781127)
    • (2000) Nature Cell Biology , vol.2 , Issue.3 , pp. 137-141
    • Wang, L.1    Ho, C.-L.2    Sun, D.3    Liem, R.K.H.4    Brown, A.5
  • 52
    • 0037781642 scopus 로고    scopus 로고
    • Discrete nuclear structures in actively growing neuroblastoma cells are revealed by antibodies raised against phosphorylated neurofilament proteins
    • DOI 10.1186/1471-2202-4-6
    • Weigum SE, García DM, Raabe TD, Christodoulides N, Koke JR (2003) Discrete nuclear structures in actively growing neuroblastoma cells are revealed by antibodies raised against phosphorylated neurofilament proteins. BMC Neurosci 4:6. (Pubitemid 38729173)
    • (2003) BMC Neuroscience , vol.4 , pp. 6
    • Weigum, S.E.1    Garcia, D.M.2    Raabe, T.D.3    Christodoulides, N.4    Koke, J.R.5
  • 53
    • 77957157543 scopus 로고    scopus 로고
    • Pathology of motor neuron disorders
    • (Shaw PJ, Strong MJ, eds), Philadelphia: Butterworth Heinemann
    • Wharton S, Ince PG (2003) Pathology of motor neuron disorders. In: Motor neuron disorders blue books of practical neurology (Shaw PJ, Strong MJ, eds), pp 17-49. Philadelphia: Butterworth Heinemann.
    • (2003) Motor Neuron Disorders Blue Books of Practical Neurology , pp. 17-49
    • Wharton, S.1    Ince, P.G.2
  • 54
  • 55
    • 0344011538 scopus 로고    scopus 로고
    • Pin1 modulates the structure and function of human RNA polymerase II
    • DOI 10.1101/gad.1135503
    • Xu YX, Hirose Y, Zhou XZ, Lu KP, Manley JL (2003) Pin1 modulates the structure and function of human RNA polymerase II. Genes Dev 17:2765-2776. (Pubitemid 37463286)
    • (2003) Genes and Development , vol.17 , Issue.22 , pp. 2765-2776
    • Xu, Y.-X.1    Hirose, Y.2    Zhou, X.Z.3    Lu, K.P.4    Manley, J.L.5
  • 56
    • 0032694199 scopus 로고    scopus 로고
    • Kinesin-mediated transport of neurofilament protein oligomers in growing axons
    • Yabe JT, Pimenta A, Shea TB (1999) Kinesin-mediated transport of neurofilament protein oligomers in growing axons. J Cell Sci 112:3799-3814.
    • (1999) J Cell Sci , vol.112 , pp. 3799-3814
    • Yabe, J.T.1    Pimenta, A.2    Shea, T.B.3


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