메뉴 건너뛰기




Volumn 6, Issue 6, 1997, Pages 1347-1351

Nuclear magnetic resonance assignment and secondary structure of an ankyrin-like repeat-bearing protein: Myotrophin

Author keywords

ANK repeats; Myotrophin; NMR; Secondary structure

Indexed keywords

RECOMBINANT SOMATOMEDIN C;

EID: 0343852713     PISSN: 09618368     EISSN: None     Source Type: Journal    
DOI: 10.1002/pro.5560060625     Document Type: Article
Times cited : (15)

References (33)
  • 3
    • 0000041361 scopus 로고
    • A common sense approach to peak picking in two- three- and four-dimensional spectra using automatic computer analysis of contour diagrams
    • Garrett DS, Powers R, Gronenbom AM, Clore GM. 1991. A common sense approach to peak picking in two- three- and four-dimensional spectra using automatic computer analysis of contour diagrams. J Magn Reson 95:214-220.
    • (1991) J Magn Reson , vol.95 , pp. 214-220
    • Garrett, D.S.1    Powers, R.2    Gronenbom, A.M.3    Clore, G.M.4
  • 4
    • 0027445190 scopus 로고
    • The Drosophila ankyrin repeat protein cactus has a predominantly α-helical secondary structure
    • Gay NJ, Ntwasa M. 1993. The Drosophila ankyrin repeat protein cactus has a predominantly α-helical secondary structure. FEBS Lett 335:155-160.
    • (1993) FEBS Lett , vol.335 , pp. 155-160
    • Gay, N.J.1    Ntwasa, M.2
  • 5
    • 0030575866 scopus 로고    scopus 로고
    • Structure of the p53 tumor suppressor bound to the ankyrin and SH3 domains of 53BP2
    • Gorina S, Pavletich NP. 1996. Structure of the p53 tumor suppressor bound to the ankyrin and SH3 domains of 53BP2. Science 274:1001-1005.
    • (1996) Science , vol.274 , pp. 1001-1005
    • Gorina, S.1    Pavletich, N.P.2
  • 7
    • 0027787894 scopus 로고
    • 2O in protein NMR application to sensitivity enhancement and NOE measurements
    • 2O in protein NMR application to sensitivity enhancement and NOE measurements. J Am Chem Soc 115:12593-12594.
    • (1993) J Am Chem Soc , vol.115 , pp. 12593-12594
    • Grzesiek, S.1    Bax, A.2
  • 8
    • 0027270867 scopus 로고
    • A dominant negative mutant of 2-5A dependent RNase suppresses antiproliferative and antiviral effects of interferon
    • Hassel BA, Zhou A, Sotomayor C, Maran A, Silverman RH. 1993. A dominant negative mutant of 2-5A dependent RNase suppresses antiproliferative and antiviral effects of interferon. EMBO J 12:3297-3304.
    • (1993) EMBO J , vol.12 , pp. 3297-3304
    • Hassel, B.A.1    Zhou, A.2    Sotomayor, C.3    Maran, A.4    Silverman, R.H.5
  • 9
    • 0028986046 scopus 로고
    • Domain organization of IκBα and sites of interaction with NF-κB p65
    • Jaffray E, Wood KM, Hay RT. 1995. Domain organization of IκBα and sites of interaction with NF-κB p65. Mol Cell Biol 15:2166-2172.
    • (1995) Mol Cell Biol , vol.15 , pp. 2166-2172
    • Jaffray, E.1    Wood, K.M.2    Hay, R.T.3
  • 10
    • 0006925492 scopus 로고
    • Pure absorption gradient enhanced heteronuclear single quantum correlation spectroscopy with improved sensitivity
    • Kay LE, Keifer P, Saarinen T. 1992. Pure absorption gradient enhanced heteronuclear single quantum correlation spectroscopy with improved sensitivity. J Am Chem Soc 114:10663-10665.
    • (1992) J Am Chem Soc , vol.114 , pp. 10663-10665
    • Kay, L.E.1    Keifer, P.2    Saarinen, T.3
  • 12
    • 0026619586 scopus 로고
    • Side chain and backbone assignments in isotopically enriched proteins from two heteronuclear triple resonance experiments
    • Logan TM, Olejniczak ET, Xu RX, Fesik SW. 1992. Side chain and backbone assignments in isotopically enriched proteins from two heteronuclear triple resonance experiments. FEBS Lett 314:413-418.
    • (1992) FEBS Lett , vol.314 , pp. 413-418
    • Logan, T.M.1    Olejniczak, E.T.2    Xu, R.X.3    Fesik, S.W.4
  • 13
    • 0025117790 scopus 로고
    • Analysis of cDNA for human erythrocyte ankyrin indicates a repeated structure with homology to tissue-differentiation and cell-cycle control proteins
    • Lux SE, John KM, Bennett V. 1990. Analysis of cDNA for human erythrocyte ankyrin indicates a repeated structure with homology to tissue-differentiation and cell-cycle control proteins. Nature 344:36-42.
    • (1990) Nature , vol.344 , pp. 36-42
    • Lux, S.E.1    John, K.M.2    Bennett, V.3
  • 14
    • 0026607234 scopus 로고
    • The ANK repeat: A ubiquitous motif involved in macromolecular recognition
    • Michaely P, Bennett V. 1992. The ANK repeat: A ubiquitous motif involved in macromolecular recognition. Trends Cell Biol 2:127-129.
    • (1992) Trends Cell Biol , vol.2 , pp. 127-129
    • Michaely, P.1    Bennett, V.2
  • 15
    • 0027374511 scopus 로고
    • The membrane-binding domain of ankyrin contains four independently folded subdomains, each comprised of six ankyrin repeats
    • Michaely P, Bennett V. 1993. The membrane-binding domain of ankyrin contains four independently folded subdomains, each comprised of six ankyrin repeats. J Biol Chem 265:22703-22709.
    • (1993) J Biol Chem , vol.265 , pp. 22703-22709
    • Michaely, P.1    Bennett, V.2
  • 16
    • 0001689741 scopus 로고
    • Gradient-enhanced triple-resonance three-dimensional NMR experiments with improved sensitivity
    • Muhandiran DR, Kay LE. 1994. Gradient-enhanced triple-resonance three-dimensional NMR experiments with improved sensitivity. J Magn Reson B 103:203-216.
    • (1994) J Magn Reson B , vol.103 , pp. 203-216
    • Muhandiran, D.R.1    Kay, L.E.2
  • 17
    • 0027507022 scopus 로고
    • Myotrophin induces early response gene and enhances cardiac gene expression
    • Mukherjee DP, McTiernan CF, Sen S. 1993. Myotrophin induces early response gene and enhances cardiac gene expression. Hypertension 21:142-148.
    • (1993) Hypertension , vol.21 , pp. 142-148
    • Mukherjee, D.P.1    McTiernan, C.F.2    Sen, S.3
  • 18
    • 0028052088 scopus 로고
    • Phosphate-regulated inactivation of the kinase PH080-PH085 by the CDK inhibitor PH081
    • Schneider KR, Smith RL, O'Shea EK. 1994. Phosphate-regulated inactivation of the kinase PH080-PH085 by the CDK inhibitor PH081. Science 266:122-126.
    • (1994) Science , vol.266 , pp. 122-126
    • Schneider, K.R.1    Smith, R.L.2    O'Shea, E.K.3
  • 19
    • 0025131865 scopus 로고
    • Myotrophin: Purification of a novel peptide from spontaneously hypertensive rat heart that influences myocardial growth
    • Sen S, Kundu G, Mekhail N, Castel J, Misono K, Healy B. 1990. Myotrophin: Purification of a novel peptide from spontaneously hypertensive rat heart that influences myocardial growth. J Biol Chem 265:16635-16643.
    • (1990) J Biol Chem , vol.265 , pp. 16635-16643
    • Sen, S.1    Kundu, G.2    Mekhail, N.3    Castel, J.4    Misono, K.5    Healy, B.6
  • 20
    • 0023110676 scopus 로고
    • A factor that initiates myocardial hypertrophy in hypertension
    • Sen S, Petscher C. 1987. A factor that initiates myocardial hypertrophy in hypertension. Hypertension 9:261-266.
    • (1987) Hypertension , vol.9 , pp. 261-266
    • Sen, S.1    Petscher, C.2
  • 21
    • 0027254445 scopus 로고
    • Myotrophin in human cardiomyopathic heart
    • Sil P, Misono K, Sen S. 1993. Myotrophin in human cardiomyopathic heart. Circ Res 73:98-108.
    • (1993) Circ Res , vol.73 , pp. 98-108
    • Sil, P.1    Misono, K.2    Sen, S.3
  • 22
    • 0029077050 scopus 로고
    • Quantification of myotrophin from spontaneously hypertensive and normal rat hearts
    • Sil P, Mukherjee DP, Sen S. 1995. Quantification of myotrophin from spontaneously hypertensive and normal rat hearts. Circ Res 76:1020-1027.
    • (1995) Circ Res , vol.76 , pp. 1020-1027
    • Sil, P.1    Mukherjee, D.P.2    Sen, S.3
  • 23
    • 0030028205 scopus 로고    scopus 로고
    • Cardiac myotrophin exhibits rel/NFκB interacting activity in vitro
    • Sivasubramanian N, Adhikary G, Sil PC, Sen S. 1996. Cardiac myotrophin exhibits rel/NFκB interacting activity in vitro. J Biol Chem 271:2812-2816.
    • (1996) J Biol Chem , vol.271 , pp. 2812-2816
    • Sivasubramanian, N.1    Adhikary, G.2    Sil, P.C.3    Sen, S.4
  • 24
    • 0347610773 scopus 로고
    • β chemical shifts to the protein secondary structure
    • β chemical shifts to the protein secondary structure. J Am Chem Soc 113:5490-5492.
    • (1991) J Am Chem Soc , vol.113 , pp. 5490-5492
    • Spera, S.1    Bax, A.2
  • 25
    • 0030026562 scopus 로고    scopus 로고
    • Both amino- and carboxyl-terminal sequences within IκBα regulate its inducible degradation
    • Sun SC, Elwood J, Greene WC. 1996. Both amino- and carboxyl-terminal sequences within IκBα regulate its inducible degradation. Mol Cell Biol 16:1058-1065.
    • (1996) Mol Cell Biol , vol.16 , pp. 1058-1065
    • Sun, S.C.1    Elwood, J.2    Greene, W.C.3
  • 27
    • 0029665942 scopus 로고    scopus 로고
    • Tumor suppressor p16INK4A: Structural characterization of wild-type and mutant proteins by NMR and circular dichroism
    • Tevelev A, Byeon IJL, Selby T, Ericson K, Kim HJ, Kraynov V, Tsai MD. 1996. Tumor suppressor p16INK4A: Structural characterization of wild-type and mutant proteins by NMR and circular dichroism. Biochemistry 35:9475-9487.
    • (1996) Biochemistry , vol.35 , pp. 9475-9487
    • Tevelev, A.1    Byeon, I.J.L.2    Selby, T.3    Ericson, K.4    Kim, H.J.5    Kraynov, V.6    Tsai, M.D.7
  • 28
    • 0025812701 scopus 로고
    • Convergence of Ets- and Notch-related structural motifs in a heteromeric DNa binding complex
    • Thompson CC, Brown TA, McKnight SL. 1991. Convergence of Ets- and Notch-related structural motifs in a heteromeric DNA binding complex. Science 253:762-768.
    • (1991) Science , vol.253 , pp. 762-768
    • Thompson, C.C.1    Brown, T.A.2    McKnight, S.L.3
  • 30
    • 0028078624 scopus 로고
    • NMR evidence for similarities between the DNA-binding regions of Drosophila melanogaster heat shock factor and the helix-turn-helix and HNF-3/forkhead families of transcription factors
    • Vuister GW, Kim SJ, Wu C, Bax A. 1994. NMR evidence for similarities between the DNA-binding regions of Drosophila melanogaster heat shock factor and the helix-turn-helix and HNF-3/forkhead families of transcription factors. J Am Chem Soc 33:10-16.
    • (1994) J Am Chem Soc , vol.33 , pp. 10-16
    • Vuister, G.W.1    Kim, S.J.2    Wu, C.3    Bax, A.4
  • 31
    • 0026410969 scopus 로고
    • Relationship between nuclear magnetic resonance chemical shift and protein secondary structure
    • Wishart DS, Sykes BD, Richard FM. 1991. Relationship between nuclear magnetic resonance chemical shift and protein secondary structure. J Mol Biol 222:311-333.
    • (1991) J Mol Biol , vol.222 , pp. 311-333
    • Wishart, D.S.1    Sykes, B.D.2    Richard, F.M.3
  • 32
    • 43949167657 scopus 로고
    • HNCACB, a high-sensitivity 3D NMR experiment to correlate amide-proton and nitrogen resonances with alpha- and beta-carbon resonances in proteins
    • Wittekind M, Muller L. 1993. HNCACB, a high-sensitivity 3D NMR experiment to correlate amide-proton and nitrogen resonances with alpha- and beta-carbon resonances in proteins. J Magn Reson B 101:201-205.
    • (1993) J Magn Reson B , vol.101 , pp. 201-205
    • Wittekind, M.1    Muller, L.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.