메뉴 건너뛰기




Volumn 6, Issue 1, 2011, Pages 96-100

Electrospray ionization-mass spectrometry conformational analysis of isolated domains of an intrinsically disordered protein

Author keywords

Charge state distributions; Cyclin dependent protein kinase inhibitors; Nano electrospray; Partially folded states; Sic1

Indexed keywords

CHARGE STATE DISTRIBUTION; CYCLIN-DEPENDENT PROTEIN KINASE INHIBITORS; ELECTROSPRAYS; FOLDED STATE; SIC1;

EID: 78651327259     PISSN: 18606768     EISSN: 18607314     Source Type: Journal    
DOI: 10.1002/biot.201000253     Document Type: Article
Times cited : (22)

References (20)
  • 1
    • 13844255387 scopus 로고    scopus 로고
    • Natively unfolded proteins.
    • Fink, A. L., Natively unfolded proteins. Curr. Opin. Struct. Biol. 2005, 15, 35-41.
    • (2005) Curr. Opin. Struct. Biol. , vol.15 , pp. 35-41
    • Fink, A.L.1
  • 2
    • 25144472591 scopus 로고    scopus 로고
    • Showing your ID: Intrinsic disorder as an ID for recognition, regulation and cell signaling.
    • Uversky, V. N., Oldfield, C. J., Dunker, A. K., Showing your ID: Intrinsic disorder as an ID for recognition, regulation and cell signaling. J. Mol. Recognit. 2005, 18, 343-384.
    • (2005) J. Mol. Recognit. , vol.18 , pp. 343-384
    • Uversky, V.N.1    Oldfield, C.J.2    Dunker, A.K.3
  • 3
    • 60349087841 scopus 로고    scopus 로고
    • Biophysical characterization of intrinsically disordered proteins.
    • Eliezer, D., Biophysical characterization of intrinsically disordered proteins. Curr. Opin. Struct. Biol. 2009, 19, 23-30.
    • (2009) Curr. Opin. Struct. Biol. , vol.19 , pp. 23-30
    • Eliezer, D.1
  • 4
    • 0030919476 scopus 로고    scopus 로고
    • Acid-induced denaturation of myoglobin studied by time-resolved electrospray ionization mass spectrometry.
    • Konermann, L., Rosell, F. I., Mauk, A. G., Douglas, D. J., Acid-induced denaturation of myoglobin studied by time-resolved electrospray ionization mass spectrometry. Biochemistry 1997, 36, 6448-6454.
    • (1997) Biochemistry , vol.36 , pp. 6448-6454
    • Konermann, L.1    Rosell, F.I.2    Mauk, A.G.3    Douglas, D.J.4
  • 5
    • 50849098485 scopus 로고    scopus 로고
    • Do ionic charges in ESI MS provide useful information on macromolecular structure?
    • Kaltashov, I. A., Abzalimov, R. R., Do ionic charges in ESI MS provide useful information on macromolecular structure? J. Am. Soc. Mass Spectrom. 2008, 19, 1239-1246.
    • (2008) J. Am. Soc. Mass Spectrom. , vol.19 , pp. 1239-1246
    • Kaltashov, I.A.1    Abzalimov, R.R.2
  • 6
    • 0028114987 scopus 로고
    • The B-type cyclin kinase inhibitor p40SIC1 controls the G1 to S transition in S. cerevisiae.
    • Schwob, E., Bohm, T., Mendenhall, M. D., Nasmyth, K., The B-type cyclin kinase inhibitor p40SIC1 controls the G1 to S transition in S. cerevisiae. Cell 1994, 79, 233-244.
    • (1994) Cell , vol.79 , pp. 233-244
    • Schwob, E.1    Bohm, T.2    Mendenhall, M.D.3    Nasmyth, K.4
  • 7
    • 68049128317 scopus 로고    scopus 로고
    • Order propensity of an intrinsically disordered protein, the cyclin-dependent-kinase inhibitor Sic1.
    • Brocca, S., Samalikova, M., Uversky, V. N., Lotti, M. et al., Order propensity of an intrinsically disordered protein, the cyclin-dependent-kinase inhibitor Sic1. Proteins 2009, 76, 731-746.
    • (2009) Proteins , vol.76 , pp. 731-746
    • Brocca, S.1    Samalikova, M.2    Uversky, V.N.3    Lotti, M.4
  • 8
    • 79551520602 scopus 로고    scopus 로고
    • Defining structural domains of an intrinsically disordered protein: Sic1, the cyclin-dependent kinase inhibitor of Saccharomyces cerevisiae.
    • DOI:10.1007/s12033-010-9309-y.
    • Brocca, S., Testa, L., Samalikova, M., Grandori, R. et al., Defining structural domains of an intrinsically disordered protein: Sic1, the cyclin-dependent kinase inhibitor of Saccharomyces cerevisiae. Mol. Biotechnol. 2010, DOI:10.1007/s12033-010-9309-y.
    • (2010) Mol. Biotechnol.
    • Brocca, S.1    Testa, L.2    Samalikova, M.3    Grandori, R.4
  • 9
    • 0037014618 scopus 로고    scopus 로고
    • Amino acid determinants of alpha-synuclein aggregation: Putting together pieces of the puzzle.
    • Uversky, V. N., Fink, A. L., Amino acid determinants of alpha-synuclein aggregation: Putting together pieces of the puzzle. FEBS Lett. 2002, 522, 9-13.
    • (2002) FEBS Lett. , vol.522 , pp. 9-13
    • Uversky, V.N.1    Fink, A.L.2
  • 10
    • 0032878307 scopus 로고    scopus 로고
    • The cyclin-dependent kinase inhibitory domain of the yeast Sic1 protein is contained within the C-terminal 70 amino acids.
    • Hodge, A., Mendenhall, M., The cyclin-dependent kinase inhibitory domain of the yeast Sic1 protein is contained within the C-terminal 70 amino acids. Mol. Gen. Genet. 1999, 262, 55-64.
    • (1999) Mol. Gen. Genet. , vol.262 , pp. 55-64
    • Hodge, A.1    Mendenhall, M.2
  • 11
    • 18844415826 scopus 로고    scopus 로고
    • The yeast cyclin-dependent kinase inhibitor Sic1 and mammalian p27Kip1 are functional homologues with a structurally conserved inhibitory domain.
    • Barberis, M., De Gioia, L., Ruzzene, M., Sarno, S. et al., The yeast cyclin-dependent kinase inhibitor Sic1 and mammalian p27Kip1 are functional homologues with a structurally conserved inhibitory domain. Biochem. J. 2005, 387, 639-647.
    • (2005) Biochem. J. , vol.387 , pp. 639-647
    • Barberis, M.1    De Gioia, L.2    Ruzzene, M.3    Sarno, S.4
  • 12
    • 47649102449 scopus 로고    scopus 로고
    • Regulation of cell division by intrinsically unstructured proteins: Intrinsic flexibility, modularity, and signaling conduits.
    • Galea, C. A., Wang, Y., Sivakolundu, S. G., Kriwacki, R. W., Regulation of cell division by intrinsically unstructured proteins: Intrinsic flexibility, modularity, and signaling conduits. Biochemistry 2008, 47, 7598-7609.
    • (2008) Biochemistry , vol.47 , pp. 7598-7609
    • Galea, C.A.1    Wang, Y.2    Sivakolundu, S.G.3    Kriwacki, R.W.4
  • 13
    • 3042648557 scopus 로고    scopus 로고
    • Co-populated conformational ensembles of beta2-microglobulin uncovered quantitatively by electrospray ionization mass spectrometry.
    • Borysik, A. J., Radford, S. E., Ashcroft, A. E., Co-populated conformational ensembles of beta2-microglobulin uncovered quantitatively by electrospray ionization mass spectrometry. J. Biol. Chem. 2004, 279, 27069-27077.
    • (2004) J. Biol. Chem. , vol.279 , pp. 27069-27077
    • Borysik, A.J.1    Radford, S.E.2    Ashcroft, A.E.3
  • 14
    • 14544299774 scopus 로고    scopus 로고
    • Optimizing long intrinsic disorder predictors with protein evolutionary information.
    • Peng, K., Vucetic, S., Radivojac, P., Brown, C. J. et al., Optimizing long intrinsic disorder predictors with protein evolutionary information. J. Bioinform. Comput. Biol. 2005, 3, 35-60.
    • (2005) J. Bioinform. Comput. Biol. , vol.3 , pp. 35-60
    • Peng, K.1    Vucetic, S.2    Radivojac, P.3    Brown, C.J.4
  • 15
    • 77951645923 scopus 로고    scopus 로고
    • Sequence determinants of compaction in intrinsically disordered proteins.
    • Marsh, J. A., Forman-Kay, J. D., Sequence determinants of compaction in intrinsically disordered proteins. Biophys. J. 2010, 98, 2383-2390.
    • (2010) Biophys. J. , vol.98 , pp. 2383-2390
    • Marsh, J.A.1    Forman-Kay, J.D.2
  • 16
    • 0035886952 scopus 로고    scopus 로고
    • Detection of multiple protein conformational ensembles in solution via deconvolution of charge-state distributions in ESI MS.
    • Dobo, A., Kaltashov, I. A., Detection of multiple protein conformational ensembles in solution via deconvolution of charge-state distributions in ESI MS. Anal. Chem. 2001, 73, 4763-4773.
    • (2001) Anal. Chem. , vol.73 , pp. 4763-4773
    • Dobo, A.1    Kaltashov, I.A.2
  • 17
    • 33947377924 scopus 로고    scopus 로고
    • Signal response of coexisting protein conformers in electrospray mass spectrometry.
    • Kuprowski, M. C., Konermann, L., Signal response of coexisting protein conformers in electrospray mass spectrometry. Anal. Chem. 2007, 79, 2499-2506.
    • (2007) Anal. Chem. , vol.79 , pp. 2499-2506
    • Kuprowski, M.C.1    Konermann, L.2
  • 18
    • 4444243006 scopus 로고    scopus 로고
    • Investigation of intact protein complexes by mass spectrometry.
    • Heck, A. J., Van Den Heuvel, R. H., Investigation of intact protein complexes by mass spectrometry. Mass Spectrom. Rev. 2004, 23, 368-389.
    • (2004) Mass Spectrom. Rev. , vol.23 , pp. 368-389
    • Heck, A.J.1    Van Den Heuvel, R.H.2
  • 19
    • 58949101630 scopus 로고    scopus 로고
    • Leucine-rich hydrophobic clusters promote folding of the N-terminus of the intrinsically disordered transactivation domain of p53.
    • Espinoza-Fonseca, L. M., Leucine-rich hydrophobic clusters promote folding of the N-terminus of the intrinsically disordered transactivation domain of p53. FEBS Lett. 2009, 583, 556-560.
    • (2009) FEBS Lett. , vol.583 , pp. 556-560
    • Espinoza-Fonseca, L.M.1
  • 20
    • 77951631601 scopus 로고    scopus 로고
    • Structure/function implications in a dynamic complex of the intrinsically disordered Sic1 with the Cdc4 subunit of an SCF ubiquitin ligase.
    • Mittag, T., Marsh, J., Grishaev, A., Orlicky, S. et al., Structure/function implications in a dynamic complex of the intrinsically disordered Sic1 with the Cdc4 subunit of an SCF ubiquitin ligase. Structure 2010, 18, 494-506.
    • (2010) Structure , vol.18 , pp. 494-506
    • Mittag, T.1    Marsh, J.2    Grishaev, A.3    Orlicky, S.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.