메뉴 건너뛰기




Volumn 350, Issue 4, 2005, Pages 611-616

The 5 Å structure of heterologously expressed plant aquaporin SoPIP2;1

Author keywords

Aquaporin; Electron diffraction; Electron microscopy; Three dimensional structure; Two dimensional crystals

Indexed keywords

AQUAPORIN; AQUAPORIN SOPIP2.1; UNCLASSIFIED DRUG; VEGETABLE PROTEIN;

EID: 20544441912     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.jmb.2005.05.001     Document Type: Article
Times cited : (62)

References (35)
  • 2
    • 0034870819 scopus 로고    scopus 로고
    • The complete set of genes encoding major intrinsic proteins in Arabidopsis provides a framework for a new nomenclature for major intrinsic proteins in plants
    • U. Johanson, M. Karlsson, I. Johansson, S. Gustavsson, S. Sjövall, and L. Fraysse The complete set of genes encoding major intrinsic proteins in Arabidopsis provides a framework for a new nomenclature for major intrinsic proteins in plants Plant Physiol. 126 2001 1358 1369
    • (2001) Plant Physiol. , vol.126 , pp. 1358-1369
    • Johanson, U.1    Karlsson, M.2    Johansson, I.3    Gustavsson, S.4    Sjövall, S.5    Fraysse, L.6
  • 3
    • 0033996879 scopus 로고    scopus 로고
    • Plasma membrane intrinsic proteins from maize cluster in two sequence subgroups with differential aquaporin activity
    • F. Chaumont, F. Barrieu, E. Wojcik, M. Chrispeels, and R. Jung Plasma membrane intrinsic proteins from maize cluster in two sequence subgroups with differential aquaporin activity Plant Physiol. 122 2000 1025 1034
    • (2000) Plant Physiol. , vol.122 , pp. 1025-1034
    • Chaumont, F.1    Barrieu, F.2    Wojcik, E.3    Chrispeels, M.4    Jung, R.5
  • 5
    • 0032029335 scopus 로고    scopus 로고
    • Water transport activity of the plasma membrane aquaporin SoPIP2;1 is regulated by phosphorylation
    • I. Johansson, M. Karlsson, V.K. Shukla, M.J. Chrispeels, C. Larsson, and P. Kjellbom Water transport activity of the plasma membrane aquaporin SoPIP2;1 is regulated by phosphorylation Plant Cell 10 1998 451 459
    • (1998) Plant Cell , vol.10 , pp. 451-459
    • Johansson, I.1    Karlsson, M.2    Shukla, V.K.3    Chrispeels, M.J.4    Larsson, C.5    Kjellbom, P.6
  • 7
    • 0034609808 scopus 로고    scopus 로고
    • Structural determinants of water permeation through aquaporin-1
    • K. Murata, K. Mitsuoka, T. Hirai, T. Walz, P. Agre, and B. Heyman Structural determinants of water permeation through aquaporin-1 Nature 407 2000 605 612
    • (2000) Nature , vol.407 , pp. 605-612
    • Murata, K.1    Mitsuoka, K.2    Hirai, T.3    Walz, T.4    Agre, P.5    Heyman, B.6
  • 8
    • 0035924329 scopus 로고    scopus 로고
    • Structural basis of water-specific transport through AQP1 water channel
    • H. Sui, B.G. Han, J.K. Lee, P. Walian, and B.K. Jap Structural basis of water-specific transport through AQP1 water channel Nature 414 2001 872 878
    • (2001) Nature , vol.414 , pp. 872-878
    • Sui, H.1    Han, B.G.2    Lee, J.K.3    Walian, P.4    Jap, B.K.5
  • 9
    • 2442659197 scopus 로고    scopus 로고
    • Aquaporin-0 membrane junctions reveal the structure of a closed water pore
    • T. Gonen, P. Sliz, J. Kistler, Y. Cheng, and T. Walz Aquaporin-0 membrane junctions reveal the structure of a closed water pore Nature 429 2004 193 197
    • (2004) Nature , vol.429 , pp. 193-197
    • Gonen, T.1    Sliz, P.2    Kistler, J.3    Cheng, Y.4    Walz, T.5
  • 13
    • 0035861454 scopus 로고    scopus 로고
    • Water permeation across biological membranes: Mechanism and dynamics of aquaporin-1 and GlpF
    • B.L. De Groot, and H. Grubmüller Water permeation across biological membranes: mechanism and dynamics of aquaporin-1 and GlpF Science 294 2001 2352 2356
    • (2001) Science , vol.294 , pp. 2352-2356
    • De Groot, B.L.1    Grubmüller, H.2
  • 15
    • 0141534474 scopus 로고    scopus 로고
    • The mechanism of proton exclusion in the aquaporin-1 water channel
    • B.L. De Groot, T. Frigato, V. Helms, and H. Grubmüller The mechanism of proton exclusion in the aquaporin-1 water channel J. Mol. Biol. 333 2003 279 293
    • (2003) J. Mol. Biol. , vol.333 , pp. 279-293
    • De Groot, B.L.1    Frigato, T.2    Helms, V.3    Grubmüller, H.4
  • 17
    • 4644308725 scopus 로고    scopus 로고
    • Structural determinants of proton blockage in aquaporins
    • N. Chakrabarti, B. Roux, and R. Pomes Structural determinants of proton blockage in aquaporins J. Mol. Biol. 343 2004 493 510
    • (2004) J. Mol. Biol. , vol.343 , pp. 493-510
    • Chakrabarti, N.1    Roux, B.2    Pomes, R.3
  • 18
    • 0033579547 scopus 로고    scopus 로고
    • Projection structure of a plant vacuole membrane aquaporin by electron cryo-crystallography
    • M.J. Daniels, M.J. Chrispeels, and M. Yeager Projection structure of a plant vacuole membrane aquaporin by electron cryo-crystallography J. Mol. Biol. 294 1999 1337 1349
    • (1999) J. Mol. Biol. , vol.294 , pp. 1337-1349
    • Daniels, M.J.1    Chrispeels, M.J.2    Yeager, M.3
  • 19
    • 0037468462 scopus 로고    scopus 로고
    • Reconstitution of water channel function of an aquaporin overexpressed and purified from Pichia pastoris
    • M. Karlsson, D. Fotiadis, S. Sjövall, I. Johansson, K. Hedfalk, A. Engel, and P. Kjellbom Reconstitution of water channel function of an aquaporin overexpressed and purified from Pichia pastoris FEBS Letters 537 2003 68 72
    • (2003) FEBS Letters , vol.537 , pp. 68-72
    • Karlsson, M.1    Fotiadis, D.2    Sjövall, S.3    Johansson, I.4    Hedfalk, K.5    Engel, A.6    Kjellbom, P.7
  • 21
  • 23
    • 0034518307 scopus 로고    scopus 로고
    • Cellular volume control in stomatal movements in plants
    • M.R. Blatt Cellular volume control in stomatal movements in plants Annu. Rev. Cell Dev. Biol. 16 2000 221 241
    • (2000) Annu. Rev. Cell Dev. Biol. , vol.16 , pp. 221-241
    • Blatt, M.R.1
  • 24
    • 0036009778 scopus 로고    scopus 로고
    • The abscisic acid-related SNARE homolog NtSyr1 contributes to secretion and growth: Evidence from competition with its cytosolic domain
    • D. Geelen, B. Leyman, H. Batoko, G.P. Di Sansebastiano, I. Moore, and M.R. Blatt The abscisic acid-related SNARE homolog NtSyr1 contributes to secretion and growth: evidence from competition with its cytosolic domain Plant Cell 14 2002 387 406
    • (2002) Plant Cell , vol.14 , pp. 387-406
    • Geelen, D.1    Leyman, B.2    Batoko, H.3    Di Sansebastiano, G.P.4    Moore, I.5    Blatt, M.R.6
  • 26
    • 0032792265 scopus 로고    scopus 로고
    • Osmotic water permeability of isolated protoplasts. Modification during development
    • T. Ramahaleo, R. Morillon, J. Alexandre, and J.P. Lassalles Osmotic water permeability of isolated protoplasts. Modification during development Plant Physiol. 119 1999 885 896
    • (1999) Plant Physiol. , vol.119 , pp. 885-896
    • Ramahaleo, T.1    Morillon, R.2    Alexandre, J.3    Lassalles, J.P.4
  • 27
    • 0035193614 scopus 로고    scopus 로고
    • Rapid movements of plants organs require solute-water cotransporters or contractile proteins
    • R. Morillon, D. Lienard, M.J. Chrispeels, and J.P. Lassalles Rapid movements of plants organs require solute-water cotransporters or contractile proteins Plant Physiol. 127 2001 720 723
    • (2001) Plant Physiol. , vol.127 , pp. 720-723
    • Morillon, R.1    Lienard, D.2    Chrispeels, M.J.3    Lassalles, J.P.4
  • 28
    • 4444271852 scopus 로고    scopus 로고
    • Dynamic changes in the osmotic water permeability of protoplast plasma membrane
    • M. Moshelion, M. Moran, and F. Chaumont Dynamic changes in the osmotic water permeability of protoplast plasma membrane Plant Physiol. 135 2004 2301 2317
    • (2004) Plant Physiol. , vol.135 , pp. 2301-2317
    • Moshelion, M.1    Moran, M.2    Chaumont, F.3
  • 29
    • 0000179989 scopus 로고    scopus 로고
    • PIP1 aquaporins are concentrated in plasmalemmasomes of Arabidopsis thaliana mesophyll
    • D.G. Robinson, H. Sieber, W. Kammerloher, and A.R. Schaffner PIP1 aquaporins are concentrated in plasmalemmasomes of Arabidopsis thaliana mesophyll Plant Physiol. 111 1996 645 649
    • (1996) Plant Physiol. , vol.111 , pp. 645-649
    • Robinson, D.G.1    Sieber, H.2    Kammerloher, W.3    Schaffner, A.R.4
  • 30
    • 0034723156 scopus 로고    scopus 로고
    • Structural clues in the sequence of the aquaporins
    • J.B. Heymann, and A. Engel Structural clues in the sequence of the aquaporins J. Mol. Biol. 295 2000 1039 1053
    • (2000) J. Mol. Biol. , vol.295 , pp. 1039-1053
    • Heymann, J.B.1    Engel, A.2
  • 33
    • 0035106823 scopus 로고    scopus 로고
    • Aquaporins constitute a large and highly divergent protein family in maize
    • F. Chaumont, F. Barrieu, E. Wojcik, M.J. Chrispeels, and R. Jung Aquaporins constitute a large and highly divergent protein family in maize Plant Physiol. 125 2001 1206 1215
    • (2001) Plant Physiol. , vol.125 , pp. 1206-1215
    • Chaumont, F.1    Barrieu, F.2    Wojcik, E.3    Chrispeels, M.J.4    Jung, R.5
  • 35
    • 0025008168 scopus 로고
    • Sequence logos: A new way to display consensus sequences
    • T.D. Schneider, and R.M. Stephens Sequence logos: a new way to display consensus sequences Nucl. Acids Res. 18 1990 6097 6100
    • (1990) Nucl. Acids Res. , vol.18 , pp. 6097-6100
    • Schneider, T.D.1    Stephens, R.M.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.