메뉴 건너뛰기




Volumn 22, Issue 10, 2014, Pages 1520-1527

The structure of a conserved piezo channel domain reveals a topologically distinct β sandwich fold

Author keywords

[No Author keywords available]

Indexed keywords

CAENORHABDITIS ELEGANS PROTEIN; DROSOPHILA PROTEIN; ION CHANNEL; PIEZO PROTEIN, DROSOPHILA; PIEZO1 PROTEIN, HUMAN; PIEZO1 PROTEIN, MOUSE; PIEZO2 PROTEIN, MOUSE;

EID: 84908208511     PISSN: 09692126     EISSN: 18784186     Source Type: Journal    
DOI: 10.1016/j.str.2014.08.009     Document Type: Article
Times cited : (43)

References (40)
  • 3
    • 77954257799 scopus 로고    scopus 로고
    • ConSurf 2010: Calculating evolutionary conservation in sequence and structure of proteins and nucleic acids
    • H. Ashkenazy, E. Erez, E. Martz, T. Pupko, and N. Ben-Tal ConSurf 2010: calculating evolutionary conservation in sequence and structure of proteins and nucleic acids Nucleic Acids Res. 38 2010 W529 W533
    • (2010) Nucleic Acids Res. , vol.38 , pp. 529-W533
    • Ashkenazy, H.1    Erez, E.2    Martz, E.3    Pupko, T.4    Ben-Tal, N.5
  • 4
    • 79960498823 scopus 로고    scopus 로고
    • The mechanosensitive ion channel Piezo1 is inhibited by the peptide GsMTx4
    • C. Bae, F. Sachs, and P.A. Gottlieb The mechanosensitive ion channel Piezo1 is inhibited by the peptide GsMTx4 Biochemistry 50 2011 6295 6300
    • (2011) Biochemistry , vol.50 , pp. 6295-6300
    • Bae, C.1    Sachs, F.2    Gottlieb, P.A.3
  • 5
    • 84875274978 scopus 로고    scopus 로고
    • Xerocytosis is caused by mutations that alter the kinetics of the mechanosensitive channel PIEZO1
    • C. Bae, R. Gnanasambandam, C. Nicolai, F. Sachs, and P.A. Gottlieb Xerocytosis is caused by mutations that alter the kinetics of the mechanosensitive channel PIEZO1 Proc. Natl. Acad. Sci. USA 110 2013 E1162 E1168
    • (2013) Proc. Natl. Acad. Sci. USA , vol.110 , pp. 1162-E1168
    • Bae, C.1    Gnanasambandam, R.2    Nicolai, C.3    Sachs, F.4    Gottlieb, P.A.5
  • 6
    • 84883041172 scopus 로고    scopus 로고
    • Human PIEZO1: Removing inactivation
    • C. Bae, P.A. Gottlieb, and F. Sachs Human PIEZO1: removing inactivation Biophys. J. 105 2013 880 886
    • (2013) Biophys. J. , vol.105 , pp. 880-886
    • Bae, C.1    Gottlieb, P.A.2    Sachs, F.3
  • 9
    • 58049196875 scopus 로고    scopus 로고
    • Neurosensory mechanotransduction
    • M. Chalfie Neurosensory mechanotransduction Nat. Rev. Mol. Cell Biol. 10 2009 44 52
    • (2009) Nat. Rev. Mol. Cell Biol. , vol.10 , pp. 44-52
    • Chalfie, M.1
  • 16
    • 0000207681 scopus 로고
    • TMBASE - A database of membrane spanning protein segments
    • K. Hofmann, and W. Stoffel TMBASE - A database of membrane spanning protein segments Biol. Chem. Hoppe-Seyler 374 1993 166
    • (1993) Biol. Chem. Hoppe-Seyler , vol.374 , pp. 166
    • Hofmann, K.1    Stoffel, W.2
  • 17
    • 77954288774 scopus 로고    scopus 로고
    • Dali server: Conservation mapping in 3D
    • L. Holm, and P. Rosenström Dali server: conservation mapping in 3D Nucleic Acids Res. 38 2010 W545 W549
    • (2010) Nucleic Acids Res. , vol.38 , pp. 545-W549
    • Holm, L.1    Rosenström, P.2
  • 18
    • 34548813656 scopus 로고    scopus 로고
    • Structure of acid-sensing ion channel 1 at 1.9 A resolution and low pH
    • J. Jasti, H. Furukawa, E.B. Gonzales, and E. Gouaux Structure of acid-sensing ion channel 1 at 1.9 A resolution and low pH Nature 449 2007 316 323
    • (2007) Nature , vol.449 , pp. 316-323
    • Jasti, J.1    Furukawa, H.2    Gonzales, E.B.3    Gouaux, E.4
  • 19
    • 76449106188 scopus 로고    scopus 로고
    • Integration, scaling, space-group assignment and post-refinement
    • W. Kabsch Integration, scaling, space-group assignment and post-refinement Acta Crystallogr. D Biol. Crystallogr. 66 2010 133 144
    • (2010) Acta Crystallogr. D Biol. Crystallogr. , vol.66 , pp. 133-144
    • Kabsch, W.1
  • 20
    • 34547584314 scopus 로고    scopus 로고
    • Advantages of combined transmembrane topology and signal peptide prediction - The Phobius web server
    • L. Käll, A. Krogh, and E.L. Sonnhammer Advantages of combined transmembrane topology and signal peptide prediction - the Phobius web server Nucleic Acids Res. 35 2007 W429 W432
    • (2007) Nucleic Acids Res. , vol.35 , pp. 429-W432
    • Käll, L.1    Krogh, A.2    Sonnhammer, E.L.3
  • 21
    • 0037100671 scopus 로고    scopus 로고
    • MAFFT: A novel method for rapid multiple sequence alignment based on fast Fourier transform
    • K. Katoh, K. Misawa, K. Kuma, and T. Miyata MAFFT: a novel method for rapid multiple sequence alignment based on fast Fourier transform Nucleic Acids Res. 30 2002 3059 3066
    • (2002) Nucleic Acids Res. , vol.30 , pp. 3059-3066
    • Katoh, K.1    Misawa, K.2    Kuma, K.3    Miyata, T.4
  • 22
    • 67949117176 scopus 로고    scopus 로고
    • Crystal structure of the ATP-gated P2X(4) ion channel in the closed state
    • T. Kawate, J.C. Michel, W.T. Birdsong, and E. Gouaux Crystal structure of the ATP-gated P2X(4) ion channel in the closed state Nature 460 2009 592 598
    • (2009) Nature , vol.460 , pp. 592-598
    • Kawate, T.1    Michel, J.C.2    Birdsong, W.T.3    Gouaux, E.4
  • 23
    • 63849246525 scopus 로고    scopus 로고
    • Protein structure prediction on the Web: A case study using the Phyre server
    • L.A. Kelley, and M.J. Sternberg Protein structure prediction on the Web: a case study using the Phyre server Nat. Protoc. 4 2009 363 371
    • (2009) Nat. Protoc. , vol.4 , pp. 363-371
    • Kelley, L.A.1    Sternberg, M.J.2
  • 24
    • 84862776759 scopus 로고    scopus 로고
    • The role of Drosophila Piezo in mechanical nociception
    • S.E. Kim, B. Coste, A. Chadha, B. Cook, and A. Patapoutian The role of Drosophila Piezo in mechanical nociception Nature 483 2012 209 212
    • (2012) Nature , vol.483 , pp. 209-212
    • Kim, S.E.1    Coste, B.2    Chadha, A.3    Cook, B.4    Patapoutian, A.5
  • 25
    • 13444307044 scopus 로고    scopus 로고
    • Secondary-structure matching (SSM), a new tool for fast protein structure alignment in three dimensions
    • E. Krissinel, and K. Henrick Secondary-structure matching (SSM), a new tool for fast protein structure alignment in three dimensions Acta Crystallogr. D Biol. Crystallogr. 60 2004 2256 2268
    • (2004) Acta Crystallogr. D Biol. Crystallogr. , vol.60 , pp. 2256-2268
    • Krissinel, E.1    Henrick, K.2
  • 26
    • 23644451510 scopus 로고    scopus 로고
    • A possible unifying principle for mechanosensation
    • C. Kung A possible unifying principle for mechanosensation Nature 436 2005 647 654
    • (2005) Nature , vol.436 , pp. 647-654
    • Kung, C.1
  • 27
    • 22544441094 scopus 로고    scopus 로고
    • ProFunc: A server for predicting protein function from 3D structure
    • R.A. Laskowski, J.D. Watson, and J.M. Thornton ProFunc: a server for predicting protein function from 3D structure Nucleic Acids Res. 33 2005 W89 W93
    • (2005) Nucleic Acids Res. , vol.33 , pp. 89-W93
    • Laskowski, R.A.1    Watson, J.D.2    Thornton, J.M.3
  • 28
    • 22544486576 scopus 로고    scopus 로고
    • Protein function prediction using local 3D templates
    • R.A. Laskowski, J.D. Watson, and J.M. Thornton Protein function prediction using local 3D templates J. Mol. Biol. 351 2005 614 626
    • (2005) J. Mol. Biol. , vol.351 , pp. 614-626
    • Laskowski, R.A.1    Watson, J.D.2    Thornton, J.M.3
  • 29
    • 0345196593 scopus 로고    scopus 로고
    • Protection of Escherichia coli cells against extreme turgor by activation of MscS and MscL mechanosensitive channels: Identification of genes required for MscS activity
    • N. Levina, S. Tötemeyer, N.R. Stokes, P. Louis, M.A. Jones, and I.R. Booth Protection of Escherichia coli cells against extreme turgor by activation of MscS and MscL mechanosensitive channels: identification of genes required for MscS activity EMBO J. 18 1999 1730 1737
    • (1999) EMBO J. , vol.18 , pp. 1730-1737
    • Levina, N.1    Tötemeyer, S.2    Stokes, N.R.3    Louis, P.4    Jones, M.A.5    Booth, I.R.6
  • 30
    • 33846426122 scopus 로고    scopus 로고
    • Solving structures of protein complexes by molecular replacement with Phaser
    • A.J. McCoy Solving structures of protein complexes by molecular replacement with Phaser Acta Crystallogr. D Biol. Crystallogr. 63 2007 32 41
    • (2007) Acta Crystallogr. D Biol. Crystallogr. , vol.63 , pp. 32-41
    • McCoy, A.J.1
  • 31
    • 84863630891 scopus 로고    scopus 로고
    • Loss of the integrin-activating transmembrane protein Fam38A (Piezo1) promotes a switch to a reduced integrin-dependent mode of cell migration
    • B.J. McHugh, A. Murdoch, C. Haslett, and T. Sethi Loss of the integrin-activating transmembrane protein Fam38A (Piezo1) promotes a switch to a reduced integrin-dependent mode of cell migration PLoS ONE 7 2012 e40346
    • (2012) PLoS ONE , vol.7 , pp. 40346
    • McHugh, B.J.1    Murdoch, A.2    Haslett, C.3    Sethi, T.4
  • 34
    • 84878998633 scopus 로고    scopus 로고
    • Identification and analysis of putative homologues of mechanosensitive channels in pathogenic protozoa
    • D.L. Prole, and C.W. Taylor Identification and analysis of putative homologues of mechanosensitive channels in pathogenic protozoa PLoS ONE 8 2013 e66068
    • (2013) PLoS ONE , vol.8 , pp. 66068
    • Prole, D.L.1    Taylor, C.W.2
  • 35
    • 0032568655 scopus 로고    scopus 로고
    • SMART, a simple modular architecture research tool: Identification of signaling domains
    • J. Schultz, F. Milpetz, P. Bork, and C.P. Ponting SMART, a simple modular architecture research tool: identification of signaling domains Proc. Natl. Acad. Sci. USA 95 1998 5857 5864
    • (1998) Proc. Natl. Acad. Sci. USA , vol.95 , pp. 5857-5864
    • Schultz, J.1    Milpetz, F.2    Bork, P.3    Ponting, C.P.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.