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Volumn 109, Issue 44, 2012, Pages 17814-17819

Calcium-dependent folding of single calmodulin molecules

Author keywords

EF hand; Ligand; Protein folding

Indexed keywords

CALCIUM; CALMODULIN;

EID: 84868095059     PISSN: 00278424     EISSN: 10916490     Source Type: Journal    
DOI: 10.1073/pnas.1201801109     Document Type: Article
Times cited : (68)

References (28)
  • 2
    • 1942496481 scopus 로고    scopus 로고
    • Calmodulin's flexibility allows for promiscuity in its interactions with target proteins and peptides
    • Yamniuk AP, Vogel HJ (2004) Calmodulin's flexibility allows for promiscuity in its interactions with target proteins and peptides. Mol Biotechnol 27:33-57.
    • (2004) Mol Biotechnol , vol.27 , pp. 33-57
    • Yamniuk, A.P.1    Vogel, H.J.2
  • 3
    • 0025823438 scopus 로고
    • Calcium binding to calmodulin and its globular domains
    • Linse S, Helmersson A, Forsén S (1991) Calcium binding to calmodulin and its globular domains. J Biol Chem 266:8050-8054.
    • (1991) J Biol Chem , vol.266 , pp. 8050-8054
    • Linse, S.1    Helmersson, A.2    Forsén, S.3
  • 4
    • 0037058908 scopus 로고    scopus 로고
    • Temperature jump kinetic study of the stability of apo-calmodulin
    • Rabl C-R, Martin SR, Neumann E, Bayley PM (2002) Temperature jump kinetic study of the stability of apo-calmodulin. Biophys Chem 101-102:553-564.
    • (2002) Biophys Chem , vol.101-102 , pp. 553-564
    • Rabl, C.-R.1    Martin, S.R.2    Neumann, E.3    Bayley, P.M.4
  • 5
    • 0033837859 scopus 로고    scopus 로고
    • Ligand binding and thermodynamic stability of a multidomain protein, calmodulin
    • Masino L, Martin SR, Bayley PM (2000) Ligand binding and thermodynamic stability of a multidomain protein, calmodulin. Protein Sci 9:1519-1529.
    • (2000) Protein Sci , vol.9 , pp. 1519-1529
    • Masino, L.1    Martin, S.R.2    Bayley, P.M.3
  • 6
    • 0022411702 scopus 로고
    • Kinetics of calcium dissociation from calmodulin and its tryptic fragments. A stopped-flow fluorescence study using Quin 2 reveals a two-domain structure
    • Martin SR, Andersson Teleman A, Bayley PM, Drakenberg T, Forsén S (1985) Kinetics of calcium dissociation from calmodulin and its tryptic fragments. A stopped-flow fluorescence study using Quin 2 reveals a two-domain structure. Eur J Biochem 151:543-550.
    • (1985) Eur J Biochem , vol.151 , pp. 543-550
    • Martin, S.R.1    Andersson Teleman, A.2    Bayley, P.M.3    Drakenberg, T.4    Forsén, S.5
  • 7
    • 0021326939 scopus 로고
    • The kinetics of calcium binding to calmodulin: Quin 2 and ANS stopped-flow flurescence studies
    • Bayley P, Ahlström P, Martin SR, Forsen S (1984) The kinetics of calcium binding to calmodulin: Quin 2 and ANS stopped-flow flurescence studies. Biochem Biophys Res Commun 120:185-191.
    • (1984) Biochem Biophys Res Commun , vol.120 , pp. 185-191
    • Bayley, P.1    Ahlström, P.2    Martin, S.R.3    Forsen, S.4
  • 9
    • 59149096062 scopus 로고    scopus 로고
    • Ligand-dependent equilibrium fluctuations of single calmodulin molecules
    • Junker JP, Ziegler F, RiefM(2009) Ligand-dependent equilibrium fluctuations of single calmodulin molecules. Science 323:633-637.
    • (2009) Science , vol.323 , pp. 633-637
    • Junker, J.P.1    Ziegler, F.2    Rief, M.3
  • 10
    • 25444512161 scopus 로고    scopus 로고
    • Direct observation of the three-state folding of a single protein molecule
    • Cecconi C, Shank EA, Bustamante C, Marqusee S (2005) Direct observation of the three-state folding of a single protein molecule. Science 309:2057-2060.
    • (2005) Science , vol.309 , pp. 2057-2060
    • Cecconi, C.1    Shank, E.A.2    Bustamante, C.3    Marqusee, S.4
  • 11
    • 33646587736 scopus 로고    scopus 로고
    • Nanomechanical measurements of the sequence-dependent folding landscapes of single nucleic acid hairpins
    • Woodside MT, et al. (2006) Nanomechanical measurements of the sequence-dependent folding landscapes of single nucleic acid hairpins. Proc Natl Acad Sci USA 103:6190-6195.
    • (2006) Proc Natl Acad Sci USA , vol.103 , pp. 6190-6195
    • Woodside, M.T.1
  • 12
    • 76649093956 scopus 로고    scopus 로고
    • Full distance-resolved folding energy landscape of one single protein molecule
    • Gebhardt JCM, Bornschlögl T, RiefM(2010) Full distance-resolved folding energy landscape of one single protein molecule. Proc Natl Acad Sci USA 107:2013-2018.
    • (2010) Proc Natl Acad Sci USA , vol.107 , pp. 2013-2018
    • Gebhardt, J.C.M.1    Bornschlögl, T.2    Rief, M.3
  • 13
    • 0030008340 scopus 로고    scopus 로고
    • Target recognition by calmodulin: Dissecting the kinetics and affinity of interaction using short peptide sequences
    • Bayley PM, Findlay WA, Martin SR (1996) Target recognition by calmodulin: Dissecting the kinetics and affinity of interaction using short peptide sequences. Protein Sci 5:1215-1228.
    • (1996) Protein Sci , vol.5 , pp. 1215-1228
    • Bayley, P.M.1    Findlay, W.A.2    Martin, S.R.3
  • 14
    • 36849080807 scopus 로고    scopus 로고
    • Direct observation of active protein folding using lock-in force spectroscopy
    • Schlierf M, Berkemeier F, Rief M (2007) Direct observation of active protein folding using lock-in force spectroscopy. Biophys J 93:3989-3998.
    • (2007) Biophys J , vol.93 , pp. 3989-3998
    • Schlierf, M.1    Berkemeier, F.2    Rief, M.3
  • 15
    • 10644295536 scopus 로고    scopus 로고
    • Phi value versus psi analysis
    • Fersht AR (2004) Phi value versus psi analysis. Proc Natl Acad Sci USA 101:17327-17328.
    • (2004) Proc Natl Acad Sci USA , vol.101 , pp. 17327-17328
    • Fersht, A.R.1
  • 16
    • 22444441276 scopus 로고    scopus 로고
    • Interpretation of protein folding psi values
    • Bodenreider C, Kiefhaber T (2005) Interpretation of protein folding psi values. J Mol Biol 351:393-401.
    • (2005) J Mol Biol , vol.351 , pp. 393-401
    • Bodenreider, C.1    Kiefhaber, T.2
  • 17
    • 37149029370 scopus 로고    scopus 로고
    • Calcium signaling
    • Clapham DE (2007) Calcium signaling. Cell 131:1047-1058.
    • (2007) Cell , vol.131 , pp. 1047-1058
    • Clapham, D.E.1
  • 18
    • 34249793711 scopus 로고    scopus 로고
    • Calcium-induced folding of a fragment of calmodulin composed of EF-hands 2 and 3
    • Lakowski T, Lee G, Okon M, Reid R, McIntosh L (2007) Calcium-induced folding of a fragment of calmodulin composed of EF-hands 2 and 3. Protein Sci 16:1119-1132.
    • (2007) Protein Sci , vol.16 , pp. 1119-1132
    • Lakowski, T.1    Lee, G.2    Okon, M.3    Reid, R.4    McIntosh, L.5
  • 19
    • 0026089108 scopus 로고
    • Electrostatic contributions to the binding of Ca2+ in calbindin D9k
    • Linse S, et al. (1991) Electrostatic contributions to the binding of Ca2+ in calbindin D9k. Biochemistry 30:154-162.
    • (1991) Biochemistry , vol.30 , pp. 154-162
    • Linse, S.1
  • 20
    • 0033527588 scopus 로고    scopus 로고
    • Structural dynamics in the C-terminal domain of calmodulin at low calcium levels
    • Malmendal A, Evenäs J, Forsén S, Akke M (1999) Structural dynamics in the C-terminal domain of calmodulin at low calcium levels. J Mol Biol 293:883-899.
    • (1999) J Mol Biol , vol.293 , pp. 883-899
    • Malmendal, A.1    Evenäs, J.2    Forsén, S.3    Akke, M.4
  • 21
    • 33847617864 scopus 로고    scopus 로고
    • Slow conformational dynamics and unfolding of the calmodulin C-terminal domain
    • Chen Y-G, Hummer G (2007) Slow conformational dynamics and unfolding of the calmodulin C-terminal domain. J Am Chem Soc 129:2414-2415.
    • (2007) J Am Chem Soc , vol.129 , pp. 2414-2415
    • Chen, Y.-G.1    Hummer, G.2
  • 22
    • 38649118463 scopus 로고    scopus 로고
    • Conformational changes of calmodulin upon Ca2+ binding studied with a microfluidic mixer
    • Park HY, et al. (2008) Conformational changes of calmodulin upon Ca2+ binding studied with a microfluidic mixer. Proc Natl Acad Sci USA 105:542-547.
    • (2008) Proc Natl Acad Sci USA , vol.105 , pp. 542-547
    • Park, H.Y.1
  • 23
    • 13844272482 scopus 로고    scopus 로고
    • Structure of a trapped intermediate of calmodulin: Calcium regulation of EF-hand proteins from a new perspective
    • Grabarek Z (2005) Structure of a trapped intermediate of calmodulin: Calcium regulation of EF-hand proteins from a new perspective. J Mol Biol 346:1351-1366.
    • (2005) J Mol Biol , vol.346 , pp. 1351-1366
    • Grabarek, Z.1
  • 24
    • 67650069571 scopus 로고    scopus 로고
    • A force-spectroscopy-based single-molecule metalbinding assay
    • Cao Y, Er KS, Parhar R, Li H (2009) A force-spectroscopy-based single-molecule metalbinding assay. Chemphyschem 10:1450-1454.
    • (2009) Chemphyschem , vol.10 , pp. 1450-1454
    • Cao, Y.1    Er, K.S.2    Parhar, R.3    Li, H.4
  • 25
    • 80054679425 scopus 로고    scopus 로고
    • Dynamics of protein folding and cofactor binding monitored by single-molecule force spectroscopy
    • Cao Y, Li H (2011) Dynamics of protein folding and cofactor binding monitored by single-molecule force spectroscopy. Biophys J 101:2009-2017.
    • (2011) Biophys J , vol.101 , pp. 2009-2017
    • Cao, Y.1    Li, H.2
  • 26
    • 76249114882 scopus 로고    scopus 로고
    • Exploring the conformation-regulated function of titin kinase by mechanical pump and probe experiments with single molecules
    • Puchner EM, Gaub HE (2010) Exploring the conformation-regulated function of titin kinase by mechanical pump and probe experiments with single molecules. Angew Chem Int Ed Engl 49:1147-1150.
    • (2010) Angew Chem Int Ed Engl , vol.49 , pp. 1147-1150
    • Puchner, E.M.1    Gaub, H.E.2
  • 27
    • 0024610919 scopus 로고
    • A tutorial on Hidden Markov models and selected applications in speech recognition
    • Rabiner LR (1989) A tutorial on Hidden Markov models and selected applications in speech recognition. Proc IEEE 77:257-286.
    • (1989) Proc IEEE , vol.77 , pp. 257-286
    • Rabiner, L.R.1
  • 28
    • 84859014128 scopus 로고    scopus 로고
    • Hidden Markov analysis of trajectories in single-molecule experiments and the effects of missed events
    • Stigler J, Rief M (2012) Hidden Markov analysis of trajectories in single-molecule experiments and the effects of missed events. Chemphyschem 13:1079-1086.
    • (2012) Chemphyschem , vol.13 , pp. 1079-1086
    • Stigler, J.1    Rief, M.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.