메뉴 건너뛰기




Volumn 47, Issue 42, 2008, Pages 11055-11061

Integrin binding immunoglobulin type filamin domains have variable stability

Author keywords

[No Author keywords available]

Indexed keywords

BINDING ENERGY; NUCLEAR MAGNETIC RESONANCE;

EID: 54349094265     PISSN: 00062960     EISSN: None     Source Type: Journal    
DOI: 10.1021/bi8011466     Document Type: Article
Times cited : (9)

References (33)
  • 1
    • 0016787774 scopus 로고
    • Isolation and properties of actin, myosin, and a new actin binding protein in rabbit alveolar macrophages
    • Hartwig, J. H., and Stossel, T. P. (1975) Isolation and properties of actin, myosin, and a new actin binding protein in rabbit alveolar macrophages. J. Biol. Chem. 250, 5696-5705.
    • (1975) J. Biol. Chem , vol.250 , pp. 5696-5705
    • Hartwig, J.H.1    Stossel, T.P.2
  • 2
    • 0016767817 scopus 로고
    • 2+-adenosine triphosphatase requires a cofactor for activation by actin
    • 2+-adenosine triphosphatase requires a cofactor for activation by actin. J. Biol. Chem. 250, 5706-5712.
    • (1975) J. Biol. Chem , vol.250 , pp. 5706-5712
    • Stossel, T.P.1    Hartwig, J.H.2
  • 4
    • 14844344918 scopus 로고    scopus 로고
    • Molecular pathology of filamin A: Diverse phenotypes, many functions
    • Robertson, S. P. (2004) Molecular pathology of filamin A: Diverse phenotypes, many functions. Clin. Dysmorphol. 13, 123-131.
    • (2004) Clin. Dysmorphol , vol.13 , pp. 123-131
    • Robertson, S.P.1
  • 5
    • 19444368524 scopus 로고    scopus 로고
    • Filamin A: Phenotypic diversity
    • Robertson, S. P. (2005) Filamin A: Phenotypic diversity. Curr. Opin. Genet. Dev. 15, 301-307.
    • (2005) Curr. Opin. Genet. Dev , vol.15 , pp. 301-307
    • Robertson, S.P.1
  • 6
    • 33746617484 scopus 로고    scopus 로고
    • Robertson, S. P., Jenkins, Z. A., Morgan, T., Ades, L., Aftimos, S., Boute, O., Fiskerstrand, T., Garcia-Minaur, S., Grix, A., Green, A., Der Kaloustian, V., Lewkonia, R., McInnes, B., van Haelst, M. M., Mancini, G., Illes, T., Mortier, G., Newbury-Ecob, R., Nicholson, L., Scott, C. I., Ochman, K., Brozek, I., Shears, D. J., Superti-Furga, A., Suri, M., Whiteford, M., Wilkie, A. O., and Krakow, D. (2006) Frontometaphyseal dysplasia: Mutations in FLNA and phenotypic diversity. Am. J. Med. Genet. 140, 1726-1736.
    • Robertson, S. P., Jenkins, Z. A., Morgan, T., Ades, L., Aftimos, S., Boute, O., Fiskerstrand, T., Garcia-Minaur, S., Grix, A., Green, A., Der Kaloustian, V., Lewkonia, R., McInnes, B., van Haelst, M. M., Mancini, G., Illes, T., Mortier, G., Newbury-Ecob, R., Nicholson, L., Scott, C. I., Ochman, K., Brozek, I., Shears, D. J., Superti-Furga, A., Suri, M., Whiteford, M., Wilkie, A. O., and Krakow, D. (2006) Frontometaphyseal dysplasia: Mutations in FLNA and phenotypic diversity. Am. J. Med. Genet. 140, 1726-1736.
  • 10
    • 33750533178 scopus 로고    scopus 로고
    • CD28 interaction with filamin-A controls lipid raft accumulation at the T-cell immunological synapse
    • Tavano, R., Contento, R. L., Baranda, S. J., Soligo, M., Tuosto, L., Manes, S., and Viola, A. (2006) CD28 interaction with filamin-A controls lipid raft accumulation at the T-cell immunological synapse. Nat. Cell Biol. 8, 1270-1276.
    • (2006) Nat. Cell Biol , vol.8 , pp. 1270-1276
    • Tavano, R.1    Contento, R.L.2    Baranda, S.J.3    Soligo, M.4    Tuosto, L.5    Manes, S.6    Viola, A.7
  • 13
    • 33646198383 scopus 로고    scopus 로고
    • Cell Mechanics: Filamin A Leads the Way
    • McGrath, J. L. (2006) Cell Mechanics: Filamin A Leads the Way. Curr. Biol. 16, R326-R327.
    • (2006) Curr. Biol , vol.16
    • McGrath, J.L.1
  • 16
    • 32544454854 scopus 로고
    • Calibration of Methanol and Glycol Nuclear Magnetic Resonance Thermometers with a Static Thermistor Probe
    • Vangeet, A. L. (1968) Calibration of Methanol and Glycol Nuclear Magnetic Resonance Thermometers with a Static Thermistor Probe. Anal. Chem. 40, 2227-2229.
    • (1968) Anal. Chem , vol.40 , pp. 2227-2229
    • Vangeet, A.L.1
  • 20
    • 0029400480 scopus 로고
    • NMRPipe: A multidimensional spectral processing system based on UNIX pipes
    • Delaglio, F., Grzesiek, S., Vuister, G. W., Zhu, G., Pfeifer, J., and Bax, A. (1995) NMRPipe: A multidimensional spectral processing system based on UNIX pipes. J. Biomol. NMR 6, 277-293.
    • (1995) J. Biomol. NMR , vol.6 , pp. 277-293
    • Delaglio, F.1    Grzesiek, S.2    Vuister, G.W.3    Zhu, G.4    Pfeifer, J.5    Bax, A.6
  • 21
    • 54349122930 scopus 로고
    • version 2.3 () Biosym Technologies, San Diego
    • Felix, user guide, version 2.3 (1994) Biosym Technologies, San Diego.
    • (1994) Felix, user guide
  • 25
    • 34247863735 scopus 로고    scopus 로고
    • Unbiased cold denaturation: Low-and high-temperature unfolding of yeast frataxin under physiological conditions
    • Pastore, A., Martin, S. R., Politou, A., Kondapalli, K. C., Stemmler, T., and Temussi, P. A. (2007) Unbiased cold denaturation: Low-and high-temperature unfolding of yeast frataxin under physiological conditions. J. Am. Chem. Soc. 129, 5374-5375.
    • (2007) J. Am. Chem. Soc , vol.129 , pp. 5374-5375
    • Pastore, A.1    Martin, S.R.2    Politou, A.3    Kondapalli, K.C.4    Stemmler, T.5    Temussi, P.A.6
  • 26
    • 0028834886 scopus 로고
    • The folding and stability of titin immunoglobulin-like modules, with implications for the mechanism of elasticity
    • Politou, A. S., Thomas, D. J., and Pastore, A. (1995) The folding and stability of titin immunoglobulin-like modules, with implications for the mechanism of elasticity. Biophys. J. 69, 2601-2610.
    • (1995) Biophys. J , vol.69 , pp. 2601-2610
    • Politou, A.S.1    Thomas, D.J.2    Pastore, A.3
  • 28
    • 27644473726 scopus 로고    scopus 로고
    • Temperature Softening of a Protein in Single-molecule Experiments
    • Schlierf, M., and Rief, M. (2005) Temperature Softening of a Protein in Single-molecule Experiments. J. Mol. Biol. 354, 497-503.
    • (2005) J. Mol. Biol , vol.354 , pp. 497-503
    • Schlierf, M.1    Rief, M.2
  • 29
    • 0035370113 scopus 로고    scopus 로고
    • Mechanical unfolding of single filamin A (ABP-280) molecules detected by atomic force microscopy
    • Furuike, S., Ito, T., and Yamazaki, M. (2001) Mechanical unfolding of single filamin A (ABP-280) molecules detected by atomic force microscopy. FEBS Lett. 498, 72-75.
    • (2001) FEBS Lett , vol.498 , pp. 72-75
    • Furuike, S.1    Ito, T.2    Yamazaki, M.3
  • 30
    • 0038583855 scopus 로고    scopus 로고
    • Mechanical response of single filamin A (ABP-280) molecules and its role in the actin cytoskeleton
    • Yamazaki, M., Furuike, S., and Ito, T. (2002) Mechanical response of single filamin A (ABP-280) molecules and its role in the actin cytoskeleton. J. Muscle Res. Cell Motil. 23, 525-534.
    • (2002) J. Muscle Res. Cell Motil , vol.23 , pp. 525-534
    • Yamazaki, M.1    Furuike, S.2    Ito, T.3
  • 31
    • 33747044675 scopus 로고    scopus 로고
    • Filamin cross-linked semiflexible networks: Fragility under strain
    • DiDonna, B. A., and Levine, A. J. (2006) Filamin cross-linked semiflexible networks: Fragility under strain. Phys. Rev. Lett. 97, 068104.
    • (2006) Phys. Rev. Lett , vol.97 , pp. 068104
    • DiDonna, B.A.1    Levine, A.J.2
  • 32
    • 34247123153 scopus 로고    scopus 로고
    • Unfolding cross-linkers as rheology regulators in F-actin networks
    • DiDonna, B. A., and Levine, A. J. (2007) Unfolding cross-linkers as rheology regulators in F-actin networks. Phys. Rev. E 75, 041909.
    • (2007) Phys. Rev. E , vol.75 , pp. 041909
    • DiDonna, B.A.1    Levine, A.J.2
  • 33
    • 0034612284 scopus 로고    scopus 로고
    • Unfolding proteins by external forces and temperature: The importance of topology and energetics
    • Paci, E., and Karplus, M. (2000) Unfolding proteins by external forces and temperature: The importance of topology and energetics. Proc. Natl. Acad. Sci. U.S.A. 97, 6521-6526.
    • (2000) Proc. Natl. Acad. Sci. U.S.A , vol.97 , pp. 6521-6526
    • Paci, E.1    Karplus, M.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.