메뉴 건너뛰기




Volumn 178, Issue 2, 1999, Pages 154-163

Metabolic regulation of protein-bound glutamyl phosphates: Insights into the function of prothymosin α

Author keywords

[No Author keywords available]

Indexed keywords

GLUTAMIC ACID; PROTHYMOSIN ALPHA;

EID: 0032946615     PISSN: 00219541     EISSN: None     Source Type: Journal    
DOI: 10.1002/(SICI)1097-4652(199902)178:2<154::AID-JCP4>3.0.CO;2-V     Document Type: Article
Times cited : (13)

References (40)
  • 4
    • 0023526027 scopus 로고
    • 32P-labeled and unlabeled nucleic acid
    • 32P-labeled and unlabeled nucleic acid. Methods Enzymol 152:49-54.
    • (1987) Methods Enzymol , vol.152 , pp. 49-54
    • Berger, S.L.1
  • 5
    • 0025967111 scopus 로고
    • Expression of the rat prothymosin α gene during T-lymphocyte proliferation and liver regeneration
    • Bustelo XR, Otero A, Gómez-Márquez J, Freire M. 1991. Expression of the rat prothymosin α gene during T-lymphocyte proliferation and liver regeneration. J Biol Chem 266:1443-1447.
    • (1991) J Biol Chem , vol.266 , pp. 1443-1447
    • Bustelo, X.R.1    Otero, A.2    Gómez-Márquez, J.3    Freire, M.4
  • 6
    • 0023277545 scopus 로고
    • Single-step method of RNA isolation by acid-guanidinium thiocyanate-phenol-chloroform extraction
    • Chomczynski P, Sacchi N. 1987. Single-step method of RNA isolation by acid-guanidinium thiocyanate-phenol-chloroform extraction. Anal Biochem 162:156-159.
    • (1987) Anal Biochem , vol.162 , pp. 156-159
    • Chomczynski, P.1    Sacchi, N.2
  • 8
    • 0023084134 scopus 로고
    • Use of eukaryotic expression technology in the functional analysis of cloned genes
    • Cullen BR. 1987. Use of eukaryotic expression technology in the functional analysis of cloned genes. Methods Enzymol 152:684-704.
    • (1987) Methods Enzymol , vol.152 , pp. 684-704
    • Cullen, B.R.1
  • 9
    • 0030570995 scopus 로고    scopus 로고
    • Prothymosin α binds histones in vitro and shows activity in nucleosome assembly assay
    • Díaz-Jullien C, Pérez-Éstez A, Covelo G, Freire M. 1996. Prothymosin α binds histones in vitro and shows activity in nucleosome assembly assay. Biochim Biophys Acta 1296:219-227.
    • (1996) Biochim Biophys Acta , vol.1296 , pp. 219-227
    • Díaz-Jullien, C.1    Pérez-Éstez, A.2    Covelo, G.3    Freire, M.4
  • 10
    • 0023064835 scopus 로고
    • Nucleoplasmin cDNA sequence reveals polyglutamic acid tracts and a cluster of sequences homologous to putative nuclear localization signals
    • Dingwall C, Dilworth SM, Black SJ, Kearsey SE, Cox LS, Laskey RA. 1987. Nucleoplasmin cDNA sequence reveals polyglutamic acid tracts and a cluster of sequences homologous to putative nuclear localization signals. EMBO J 6:69-74.
    • (1987) EMBO J , vol.6 , pp. 69-74
    • Dingwall, C.1    Dilworth, S.M.2    Black, S.J.3    Kearsey, S.E.4    Cox, L.S.5    Laskey, R.A.6
  • 11
    • 0022997102 scopus 로고
    • The human prothymosin α gene is polymorphic and induced upon growth stimulation: Evidence using a cloned cDNA
    • Eschenfeldt WH, Berger SL. 1986. The human prothymosin α gene is polymorphic and induced upon growth stimulation: evidence using a cloned cDNA. Proc Natl Acad Sci USA 83:9403-9407.
    • (1986) Proc Natl Acad Sci USA , vol.83 , pp. 9403-9407
    • Eschenfeldt, W.H.1    Berger, S.L.2
  • 12
    • 0024598760 scopus 로고
    • Isolation and partial sequencing of the human prothymosin α gene family
    • Eschenfeldt WH, Manrow RE, Krug MS, Berger SL. 1989. Isolation and partial sequencing of the human prothymosin α gene family. J Biol Chem 264:7546-7555.
    • (1989) J Biol Chem , vol.264 , pp. 7546-7555
    • Eschenfeldt, W.H.1    Manrow, R.E.2    Krug, M.S.3    Berger, S.L.4
  • 14
    • 0024340627 scopus 로고
    • The expression of prothymosin α gene in T lymphocytes and leukemic lymphoid cells is tied to lymphocyte proliferation
    • Gómez-Márquez J, Segade F, Dosil M, Pichel JG, Bustelo XR, Freire M. 1989. The expression of prothymosin α gene in T lymphocytes and leukemic lymphoid cells is tied to lymphocyte proliferation. J Biol Chem 264:8451-8454.
    • (1989) J Biol Chem , vol.264 , pp. 8451-8454
    • Gómez-Márquez, J.1    Segade, F.2    Dosil, M.3    Pichel, J.G.4    Bustelo, X.R.5    Freire, M.6
  • 15
    • 0018295378 scopus 로고
    • Cell cycle analysis by flow cytometry
    • Gray JW, Coffino P. 1979. Cell cycle analysis by flow cytometry. Methods Enzymol 58:233-248.
    • (1979) Methods Enzymol , vol.58 , pp. 233-248
    • Gray, J.W.1    Coffino, P.2
  • 19
    • 0024281410 scopus 로고
    • Phosphorylation of the three proteins in the signaling pathway of bacterial chemotaxis
    • Hess JF, Oosawa K, Kaplan N, Simon MI. 1988. Phosphorylation of the three proteins in the signaling pathway of bacterial chemotaxis. Cell 53:79-87.
    • (1988) Cell , vol.53 , pp. 79-87
    • Hess, J.F.1    Oosawa, K.2    Kaplan, N.3    Simon, M.I.4
  • 20
    • 0028908039 scopus 로고
    • Head-on collision between a DNA replication apparatus and RNA polymerase transcription complex
    • Liu B, Alberts BM. 1995. Head-on collision between a DNA replication apparatus and RNA polymerase transcription complex. Science 267:1131-1137.
    • (1995) Science , vol.267 , pp. 1131-1137
    • Liu, B.1    Alberts, B.M.2
  • 21
    • 0024040412 scopus 로고
    • Protein kinase and phosphoprotein phosphatase activities of nitrogen regulatory proteins NTRB and NTRC of enteric bacteria: Roles of the conserved amino-terminal domain of NTRC
    • Keener J, Kustu S. 1988. Protein kinase and phosphoprotein phosphatase activities of nitrogen regulatory proteins NTRB and NTRC of enteric bacteria: roles of the conserved amino-terminal domain of NTRC. Proc Natl Acad Sci USA 85:4976-4980.
    • (1988) Proc Natl Acad Sci USA , vol.85 , pp. 4976-4980
    • Keener, J.1    Kustu, S.2
  • 22
    • 33947463386 scopus 로고
    • The effect of catalysts on the hydrolysis of acetyl phosphate. Nucleophilic displacement mechanisms in enzymatic reactions
    • Koshland DE Jr. 1952. The effect of catalysts on the hydrolysis of acetyl phosphate. Nucleophilic displacement mechanisms in enzymatic reactions. J Am Chem Soc 74:2286-2292.
    • (1952) J Am Chem Soc , vol.74 , pp. 2286-2292
    • Koshland D.E., Jr.1
  • 23
    • 0028862786 scopus 로고
    • Binding of human prothymosin α to the leucine-motif/activation domains of HTLV-I rex and HIV-1 rev
    • Kubota S, Adachi Y, Copeland TD, Oroszlan S. 1995. Binding of human prothymosin α to the leucine-motif/activation domains of HTLV-I rex and HIV-1 rev. Eur J Biochem 233:48-54.
    • (1995) Eur J Biochem , vol.233 , pp. 48-54
    • Kubota, S.1    Adachi, Y.2    Copeland, T.D.3    Oroszlan, S.4
  • 25
    • 0028791884 scopus 로고
    • Do products of the myc proto-oncogene play a role in transcriptional regulation of the prothymosin α gene?
    • Mol PC, Wang R-H, Batey DW, Lee LA, Dang CV, Berger SL. 1995. Do products of the myc proto-oncogene play a role in transcriptional regulation of the prothymosin α gene? Mol Cell Biol 15:6999-7009.
    • (1995) Mol Cell Biol , vol.15 , pp. 6999-7009
    • Mol, P.C.1    Wang, R.-H.2    Batey, D.W.3    Lee, L.A.4    Dang, C.V.5    Berger, S.L.6
  • 27
    • 0028276120 scopus 로고
    • Prothymosin α binds to Histone H1 in vitro
    • Papamarcaki T, Tsolas O. 1994. Prothymosin α binds to Histone H1 in vitro. FEBS Lett 345:71-75.
    • (1994) FEBS Lett , vol.345 , pp. 71-75
    • Papamarcaki, T.1    Tsolas, O.2
  • 28
    • 0025509078 scopus 로고
    • Human prothymosin α: Purification of a highly acidic nuclear protein by means of a phenol extraction
    • Sburlati AR, Manrow RE, Berger SL. 1990. Human prothymosin α: purification of a highly acidic nuclear protein by means of a phenol extraction. Protein Express Purif 1:184-190.
    • (1990) Protein Express Purif , vol.1 , pp. 184-190
    • Sburlati, A.R.1    Manrow, R.E.2    Berger, S.L.3
  • 29
    • 0026018529 scopus 로고
    • Prothymosin α antisense oligomers inhibit myeloma cell division
    • Sburlati AR, Manrow RE, Berger SL. 1991. Prothymosin α antisense oligomers inhibit myeloma cell division. Proc Natl Acad Sci USA 88:253-257.
    • (1991) Proc Natl Acad Sci USA , vol.88 , pp. 253-257
    • Sburlati, A.R.1    Manrow, R.E.2    Berger, S.L.3
  • 33
    • 0030704349 scopus 로고    scopus 로고
    • Prothymosin α in vivo contains phosphorylated glutamic acid residues
    • Trumbore MW, Wang R-H, Enkemann SA, Berger SL. 1997. Prothymosin α in vivo contains phosphorylated glutamic acid residues. J Biol Chem 272:26394-26404.
    • (1997) J Biol Chem , vol.272 , pp. 26394-26404
    • Trumbore, M.W.1    Wang, R.-H.2    Enkemann, S.A.3    Berger, S.L.4
  • 34
    • 0030056458 scopus 로고    scopus 로고
    • Regulation of prothymosin alpha during the cell cycle
    • Vareli K, Tsolas O, Frangou-Lazaridis M. 1996. Regulation of prothymosin alpha during the cell cycle. Eur J Biochem 238:799-806.
    • (1996) Eur J Biochem , vol.238 , pp. 799-806
    • Vareli, K.1    Tsolas, O.2    Frangou-Lazaridis, M.3
  • 36
    • 0030704350 scopus 로고    scopus 로고
    • Turnover of the acyl phosphates of human and murine prothymosin α in vivo
    • Wang R-H, Tao L, Trumbore MW, Berger SL. 1997. Turnover of the acyl phosphates of human and murine prothymosin α in vivo. J Biol Chem 272:26405-26412.
    • (1997) J Biol Chem , vol.272 , pp. 26405-26412
    • Wang, R.-H.1    Tao, L.2    Trumbore, M.W.3    Berger, S.L.4
  • 40
    • 0018966230 scopus 로고
    • Production of large numbers of mitotic mammalian cells by use of the reversible microtubule inhibitor nocodazole
    • Zieve GW, Turnbull D, Mullins JM, McIntosh JR. 1980. Production of large numbers of mitotic mammalian cells by use of the reversible microtubule inhibitor nocodazole. Exp Cell Res 126:397-405.
    • (1980) Exp Cell Res , vol.126 , pp. 397-405
    • Zieve, G.W.1    Turnbull, D.2    Mullins, J.M.3    McIntosh, J.R.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.