메뉴 건너뛰기




Volumn 11, Issue 1, 2006, Pages 40-46

Protein crystallization in vivo

Author keywords

Aggregation; Protein crystallization

Indexed keywords

AGGLOMERATION; COLLOIDS; CRYSTALLINE MATERIALS; CRYSTALLIZATION; PHYSICAL PROPERTIES; SELF ASSEMBLY;

EID: 33646118750     PISSN: 13590294     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.cocis.2005.10.002     Document Type: Review
Times cited : (96)

References (57)
  • 1
    • 0003468009 scopus 로고    scopus 로고
    • Cold Spring Harbor Laboratory Press, Cold Spring Harbor. Chapter 10 contains the first survey of in vivo protein crystallization.
    • McPherson A. Crystallization of biological macromolecules (1999), Cold Spring Harbor Laboratory Press, Cold Spring Harbor. Chapter 10 contains the first survey of in vivo protein crystallization.
    • (1999) Crystallization of biological macromolecules
    • McPherson, A.1
  • 2
    • 33745321115 scopus 로고    scopus 로고
    • The physics of protein crystallization
    • An excellent review of the physical principles underlying protein crystallization in vitro.
    • Vekilov P.G., and Chernov A.A. The physics of protein crystallization. Solid State Phys 57 (2002) 1-147. An excellent review of the physical principles underlying protein crystallization in vitro.
    • (2002) Solid State Phys , vol.57 , pp. 1-147
    • Vekilov, P.G.1    Chernov, A.A.2
  • 3
    • 0000874294 scopus 로고    scopus 로고
    • Crystallization of globular proteins
    • Poon W.C.K. Crystallization of globular proteins. Phys Rev E 55 (1997) 3762-3764
    • (1997) Phys Rev E , vol.55 , pp. 3762-3764
    • Poon, W.C.K.1
  • 4
    • 0000854412 scopus 로고    scopus 로고
    • Phase behaviour of a simple model of globular proteins
    • Sear R.P. Phase behaviour of a simple model of globular proteins. J Chem Phys 111 (1999) 4800-4806
    • (1999) J Chem Phys , vol.111 , pp. 4800-4806
    • Sear, R.P.1
  • 5
    • 33645064077 scopus 로고    scopus 로고
    • The role of anisotropic interactions in protein phase behavior
    • Asherie N., Lomakin A., and Benedek G.B. The role of anisotropic interactions in protein phase behavior. Biophys J 82 (2002) 317
    • (2002) Biophys J , vol.82 , pp. 317
    • Asherie, N.1    Lomakin, A.2    Benedek, G.B.3
  • 9
    • 33748580982 scopus 로고    scopus 로고
    • Inhibition of protein crystallization by evolutionary negative design
    • This paper advances the hypothesis that the difficulty of crystallizing proteins in vitro reflects the evolutionary selection pressure against native state aggregation and crystallization occurring in vivo.
    • Doye J.P.K., Louis A.A., and Vendruscolo M. Inhibition of protein crystallization by evolutionary negative design. Phys Biol 1 (2004) 9-13. This paper advances the hypothesis that the difficulty of crystallizing proteins in vitro reflects the evolutionary selection pressure against native state aggregation and crystallization occurring in vivo.
    • (2004) Phys Biol , vol.1 , pp. 9-13
    • Doye, J.P.K.1    Louis, A.A.2    Vendruscolo, M.3
  • 10
    • 0018977198 scopus 로고
    • The structure of cucurbitin: subunit symmetry and organization in situ
    • Colman P.M., Suzuki E., and van Donkelaar A. The structure of cucurbitin: subunit symmetry and organization in situ. Eur J Biochem 103 (1980) 585-588
    • (1980) Eur J Biochem , vol.103 , pp. 585-588
    • Colman, P.M.1    Suzuki, E.2    van Donkelaar, A.3
  • 12
    • 0032168206 scopus 로고    scopus 로고
    • Deposition of storage proteins
    • Müntz K. Deposition of storage proteins. Plant Mol Biol 38 (1998) 77-99
    • (1998) Plant Mol Biol , vol.38 , pp. 77-99
    • Müntz, K.1
  • 13
    • 0034698757 scopus 로고    scopus 로고
    • Biogenesis of the protein storage vacuole crystalloid
    • Jiang L., Phillips T.E., Rogers S.W., and Rogers J.C. Biogenesis of the protein storage vacuole crystalloid. J Cell Biol 150 (2000) 755-770
    • (2000) J Cell Biol , vol.150 , pp. 755-770
    • Jiang, L.1    Phillips, T.E.2    Rogers, S.W.3    Rogers, J.C.4
  • 14
    • 0035033768 scopus 로고    scopus 로고
    • Pea legumin overexpressed in wheat endosperm assembles into an ordered paracrystalline matrix
    • A unique transgenic example of crystallization in vivo.
    • Stoöger E., Parker M., Christou P., and Casey R. Pea legumin overexpressed in wheat endosperm assembles into an ordered paracrystalline matrix. Plant Physiol 125 (2001) 1732-1742. A unique transgenic example of crystallization in vivo.
    • (2001) Plant Physiol , vol.125 , pp. 1732-1742
    • Stoöger, E.1    Parker, M.2    Christou, P.3    Casey, R.4
  • 15
    • 0001909782 scopus 로고    scopus 로고
    • The structure and biosynthesis of legume seed storage proteins: a biological solution to the storage of nitrogen in seeds
    • Boulter D., and Croy R.R.D. The structure and biosynthesis of legume seed storage proteins: a biological solution to the storage of nitrogen in seeds. Adv Bot Res 27 (1997) 1-84
    • (1997) Adv Bot Res , vol.27 , pp. 1-84
    • Boulter, D.1    Croy, R.R.D.2
  • 16
    • 0034826426 scopus 로고    scopus 로고
    • Crystal structures of recombinant and native soybean beta-conglycinin beta homotrimers
    • Maruyama N., Adachi M., Takahashi K., Yagasaki K., Kohno M., Takenaka Y., et al. Crystal structures of recombinant and native soybean beta-conglycinin beta homotrimers. Eur J Biochem 268 (1998) 3595-3604
    • (1998) Eur J Biochem , vol.268 , pp. 3595-3604
    • Maruyama, N.1    Adachi, M.2    Takahashi, K.3    Yagasaki, K.4    Kohno, M.5    Takenaka, Y.6
  • 18
    • 0032526224 scopus 로고    scopus 로고
    • Sorting and storage during secretory granule biogenesis: looking backward and looking forward
    • This paper argues for the potential role of aggregation in the sorting of secretory proteins.
    • Arvan P., and Castle P. Sorting and storage during secretory granule biogenesis: looking backward and looking forward. Biochem J 332 (1998) 593-610. This paper argues for the potential role of aggregation in the sorting of secretory proteins.
    • (1998) Biochem J , vol.332 , pp. 593-610
    • Arvan, P.1    Castle, P.2
  • 19
    • 0027753944 scopus 로고
    • Intracisternal crystals in pancreatic acinar cells: failure in the distinct aggregation of secretory proteins
    • Arias A.E., and Bendayan M. Intracisternal crystals in pancreatic acinar cells: failure in the distinct aggregation of secretory proteins. Eur J Cell Biol 62 (1993) 282-293
    • (1993) Eur J Cell Biol , vol.62 , pp. 282-293
    • Arias, A.E.1    Bendayan, M.2
  • 20
    • 0033062601 scopus 로고    scopus 로고
    • Protein hormone storage in secretory granules: mechanisms for concentration and sorting
    • Dannies P.S. Protein hormone storage in secretory granules: mechanisms for concentration and sorting. Endocr Rev 20 (1999) 3-21
    • (1999) Endocr Rev , vol.20 , pp. 3-21
    • Dannies, P.S.1
  • 21
    • 0032054714 scopus 로고    scopus 로고
    • The role of assembly in insulin's biosynthesis
    • A review of the interprotein interactions underlying the assembly of insulin granules.
    • Dodson G., and Steiner D. The role of assembly in insulin's biosynthesis. Curr Opin Struct Biol 8 (1998) 189-194. A review of the interprotein interactions underlying the assembly of insulin granules.
    • (1998) Curr Opin Struct Biol , vol.8 , pp. 189-194
    • Dodson, G.1    Steiner, D.2
  • 22
    • 0033006040 scopus 로고    scopus 로고
    • Pharmacology of the eosinophil
    • Giembycz M.A., and Lindsay M.A. Pharmacology of the eosinophil. Pharmacol Rev 51 (1999) 213-340
    • (1999) Pharmacol Rev , vol.51 , pp. 213-340
    • Giembycz, M.A.1    Lindsay, M.A.2
  • 23
    • 0035854756 scopus 로고    scopus 로고
    • Crystal structure of the eosinophil major basic protein at 1.8 Å: an atypical lectin with a paradigm shift in specificity
    • Swaminathan G.J., Weaver A.J., Loegering D.A., Checkel J.L., Leonidas D.D., Gleich G.J., et al. Crystal structure of the eosinophil major basic protein at 1.8 Å: an atypical lectin with a paradigm shift in specificity. J Biol Chem 276 (2001) 26197-26203
    • (2001) J Biol Chem , vol.276 , pp. 26197-26203
    • Swaminathan, G.J.1    Weaver, A.J.2    Loegering, D.A.3    Checkel, J.L.4    Leonidas, D.D.5    Gleich, G.J.6
  • 24
    • 0029646108 scopus 로고
    • Crystal structure of human Charcot-Leyden crystal protein, and eosinophil lysophospholipase, identifies it as a new member of the carbohydrate-binding family of galectins
    • Leonidas D.D., Elbert B.L., Zhou Z., Leffler H., Ackerman S.J., and Acharya K.R. Crystal structure of human Charcot-Leyden crystal protein, and eosinophil lysophospholipase, identifies it as a new member of the carbohydrate-binding family of galectins. Structure 3 (1995) 1379-1393
    • (1995) Structure , vol.3 , pp. 1379-1393
    • Leonidas, D.D.1    Elbert, B.L.2    Zhou, Z.3    Leffler, H.4    Ackerman, S.J.5    Acharya, K.R.6
  • 26
    • 0018195610 scopus 로고
    • Extrusive organelles in protists
    • Hausmann K. Extrusive organelles in protists. Int Rev Cytol 52 (1978) 197-276
    • (1978) Int Rev Cytol , vol.52 , pp. 197-276
    • Hausmann, K.1
  • 27
    • 33646094654 scopus 로고    scopus 로고
    • Out with a bang! Tetrahymena as a model system to study secretory granule biogenesis
    • Turkewitz A.P. Out with a bang! Tetrahymena as a model system to study secretory granule biogenesis. J Chem Phys 112 (2000) 4773
    • (2000) J Chem Phys , vol.112 , pp. 4773
    • Turkewitz, A.P.1
  • 28
    • 0034122147 scopus 로고    scopus 로고
    • Molecular genetics of regulated secretion in Paramecium
    • Vayssié L., Skouri F., Sperling L., and Cohen J. Molecular genetics of regulated secretion in Paramecium. Biochimie 82 (2000) 269-288
    • (2000) Biochimie , vol.82 , pp. 269-288
    • Vayssié, L.1    Skouri, F.2    Sperling, L.3    Cohen, J.4
  • 29
    • 0035065377 scopus 로고    scopus 로고
    • Growth and form of secretory granules involves stepwise assembly but not differential sorting of a family of secretory proteins in Paramecium
    • Vayssié L., Garreau de Loubresse N., and Sperling L. Growth and form of secretory granules involves stepwise assembly but not differential sorting of a family of secretory proteins in Paramecium. J Cell Sci 114 (2001) 875-886
    • (2001) J Cell Sci , vol.114 , pp. 875-886
    • Vayssié, L.1    Garreau de Loubresse, N.2    Sperling, L.3
  • 30
    • 0001509897 scopus 로고
    • Local trichocyst exocytosis provides an efficient escape mechanism for Paramecium cells
    • Knoll G., Haackebell B., and Plattner H. Local trichocyst exocytosis provides an efficient escape mechanism for Paramecium cells. Eur J Protistol 27 (1991) 381-385
    • (1991) Eur J Protistol , vol.27 , pp. 381-385
    • Knoll, G.1    Haackebell, B.2    Plattner, H.3
  • 31
    • 0027516245 scopus 로고
    • The secretory granule matrix: a fast-acting smart polymer
    • Nanavati C., and Fernandez J.M. The secretory granule matrix: a fast-acting smart polymer. Science 259 (1993) 963-965
    • (1993) Science , vol.259 , pp. 963-965
    • Nanavati, C.1    Fernandez, J.M.2
  • 33
    • 0348047325 scopus 로고    scopus 로고
    • Structure, diversity and evolution of protein toxins from spore-forming entomopathogenic bacteria
    • de Maagd R.A., Bravo A., Berry C., Crickmore N., and Schnepf H.E. Structure, diversity and evolution of protein toxins from spore-forming entomopathogenic bacteria. Annu Rev Genet 37 (2003) 409-433
    • (2003) Annu Rev Genet , vol.37 , pp. 409-433
    • de Maagd, R.A.1    Bravo, A.2    Berry, C.3    Crickmore, N.4    Schnepf, H.E.5
  • 34
    • 0035162968 scopus 로고    scopus 로고
    • Overexpression of the Bt cry2Aa2 operon in chloroplasts leads to the formation of insecticidal crystals
    • De Cosa B., Moar W., Lee S.-B., Miller M., and Daniell H. Overexpression of the Bt cry2Aa2 operon in chloroplasts leads to the formation of insecticidal crystals. Nat Biotechnol 19 (2001) 71-74
    • (2001) Nat Biotechnol , vol.19 , pp. 71-74
    • De Cosa, B.1    Moar, W.2    Lee, S.-B.3    Miller, M.4    Daniell, H.5
  • 35
    • 0004231081 scopus 로고
    • Longman, London. A review of insect viruses with an emphasis on the ultrastructural features associated with infection. A significant portion of the book is given over to those viruses which induce the formation of crystalline protein inclusion bodies.
    • Smith K.M. Virus-insect relationships (1976), Longman, London. A review of insect viruses with an emphasis on the ultrastructural features associated with infection. A significant portion of the book is given over to those viruses which induce the formation of crystalline protein inclusion bodies.
    • (1976) Virus-insect relationships
    • Smith, K.M.1
  • 36
    • 0030617463 scopus 로고    scopus 로고
    • Wipfelkrankheit: modification of host behaviour during baculoviral infection
    • Goulson D. Wipfelkrankheit: modification of host behaviour during baculoviral infection. Oecologica 109 (1997) 219-228
    • (1997) Oecologica , vol.109 , pp. 219-228
    • Goulson, D.1
  • 37
    • 1842577741 scopus 로고    scopus 로고
    • Onset of heterogeneous crystal nucleation in colloidal suspensions
    • Cacciuto A., Auer S., and Frenkel D. Onset of heterogeneous crystal nucleation in colloidal suspensions. Nature 428 (2004) 404-406
    • (2004) Nature , vol.428 , pp. 404-406
    • Cacciuto, A.1    Auer, S.2    Frenkel, D.3
  • 38
    • 0014201224 scopus 로고
    • An ultrastructural study of the development of a granulosis virus in the cells of the moth Plodia interpunctella (Hbn.)
    • Arnott H.J., and Smith K.M. An ultrastructural study of the development of a granulosis virus in the cells of the moth Plodia interpunctella (Hbn.). J Ultrastruct Res 21 (1968) 251-268
    • (1968) J Ultrastruct Res , vol.21 , pp. 251-268
    • Arnott, H.J.1    Smith, K.M.2
  • 39
    • 33646113084 scopus 로고    scopus 로고
    • Y. Chiu, personal communication.
  • 42
    • 0026027138 scopus 로고    scopus 로고
    • Assembly of alcohol oxidase in the cytosol of a peroxisome-deficient mutant of Hansenula polymorpha-properties of the protein and architecture of the crystals
    • van der Klei I.J., Sulter G.J., Harder W., and Veenhuis M. Assembly of alcohol oxidase in the cytosol of a peroxisome-deficient mutant of Hansenula polymorpha-properties of the protein and architecture of the crystals. Yeast 7 (2004) 15-24
    • (2004) Yeast , vol.7 , pp. 15-24
    • van der Klei, I.J.1    Sulter, G.J.2    Harder, W.3    Veenhuis, M.4
  • 43
    • 0033782946 scopus 로고    scopus 로고
    • A new self-assembled peroxisomal vesicle required for efficient resealing
    • Jedd G., and Chua N.-H. A new self-assembled peroxisomal vesicle required for efficient resealing. Nat Cell Biol 2 (2000) 226-231
    • (2000) Nat Cell Biol , vol.2 , pp. 226-231
    • Jedd, G.1    Chua, N.-H.2
  • 44
    • 0037388850 scopus 로고    scopus 로고
    • A HEX-1 crystal lattice required for Woronin body function in Neurospora crassa
    • One of the most recent examples of protein crystallization in vivo in the biology literature; also a clear example of crystallization linked to function.
    • Yuan P., Jedd G., Kumaran D., Swaminathan S., Shio H., Hewitt D., et al. A HEX-1 crystal lattice required for Woronin body function in Neurospora crassa. Nat Struct Biol 10 (2003) 264-270. One of the most recent examples of protein crystallization in vivo in the biology literature; also a clear example of crystallization linked to function.
    • (2003) Nat Struct Biol , vol.10 , pp. 264-270
    • Yuan, P.1    Jedd, G.2    Kumaran, D.3    Swaminathan, S.4    Shio, H.5    Hewitt, D.6
  • 45
    • 0026323715 scopus 로고
    • Penetration of hard substrates by a fungus employing enormous turgor pressures
    • Howard R.J., Ferrari M.A., Roach D.H., and Money N.P. Penetration of hard substrates by a fungus employing enormous turgor pressures. Proc Natl Acad Sci U S A 88 (1991) 11281-11284
    • (1991) Proc Natl Acad Sci U S A , vol.88 , pp. 11281-11284
    • Howard, R.J.1    Ferrari, M.A.2    Roach, D.H.3    Money, N.P.4
  • 46
    • 0037237928 scopus 로고    scopus 로고
    • The phloem, a miracle of ingenuity
    • van Bel A.J.E. The phloem, a miracle of ingenuity. Plant Cell Environ 26 (2003) 125-24
    • (2003) Plant Cell Environ , vol.26 , pp. 125-24
    • van Bel, A.J.E.1
  • 47
    • 0035018617 scopus 로고    scopus 로고
    • Reversible calcium-regulated stopcocks in legume sieve tubes
    • Knoblauch M., Peters W.S., Ehlers K., and vanBel A.J.E. Reversible calcium-regulated stopcocks in legume sieve tubes. Plant Cell 13 (2001) 1221-1230
    • (2001) Plant Cell , vol.13 , pp. 1221-1230
    • Knoblauch, M.1    Peters, W.S.2    Ehlers, K.3    vanBel, A.J.E.4
  • 48
    • 0035997073 scopus 로고    scopus 로고
    • Intermolecular interactions, nucleation and thermodynamics of crystallization of hemoglobin C
    • Vekilov P.G., Feeling-Taylor A.R., Petsev D.N., Galkin O., Nagel R.L., and Hirsch R.E. Intermolecular interactions, nucleation and thermodynamics of crystallization of hemoglobin C. Biophys J 83 (2002) 1147-1156
    • (2002) Biophys J , vol.83 , pp. 1147-1156
    • Vekilov, P.G.1    Feeling-Taylor, A.R.2    Petsev, D.N.3    Galkin, O.4    Nagel, R.L.5    Hirsch, R.E.6
  • 49
    • 1542375225 scopus 로고    scopus 로고
    • Liquid-liquid phase separation in hemoglobins: distinct aggregation mechanisms of the β6 mutants
    • Chen Q., Vekilov P.G., Nagel R.L., and Hirsch R.E. Liquid-liquid phase separation in hemoglobins: distinct aggregation mechanisms of the β6 mutants. Biophys J 86 (2004) 1702-1712
    • (2004) Biophys J , vol.86 , pp. 1702-1712
    • Chen, Q.1    Vekilov, P.G.2    Nagel, R.L.3    Hirsch, R.E.4
  • 51
    • 0035933113 scopus 로고    scopus 로고
    • Crystal cataracts: human genetic cataract caused by protein crystallization
    • One of the clearest examples of in vivo crystallization causing disease.
    • Pande A., Pande J., Asherie N., Lomakin A., Ogun O., King J., et al. Crystal cataracts: human genetic cataract caused by protein crystallization. Proc Natl Acad Sci U S A 98 (2001) 6116-6120. One of the clearest examples of in vivo crystallization causing disease.
    • (2001) Proc Natl Acad Sci U S A , vol.98 , pp. 6116-6120
    • Pande, A.1    Pande, J.2    Asherie, N.3    Lomakin, A.4    Ogun, O.5    King, J.6
  • 52
    • 2342567457 scopus 로고    scopus 로고
    • Cellular inclusions: diagnostic clues in surgical pathology
    • Lee M.W., Qureshi H.S., Ho K.L., and Min K.W. Cellular inclusions: diagnostic clues in surgical pathology. Path Case Rev. 7 (2002) 186-192
    • (2002) Path Case Rev. , vol.7 , pp. 186-192
    • Lee, M.W.1    Qureshi, H.S.2    Ho, K.L.3    Min, K.W.4
  • 53
    • 0036720517 scopus 로고    scopus 로고
    • Generalized crystal-storing histiocytosis associated with monoclonal gammopathy: molecular analysis of a disorder with rapid clinical course and review of the literature
    • Lebeau A., Zeindl-Eberhart E., Müller E.-C., Müller-Höcker J., Jungblut P.R., Emmerich B., et al. Generalized crystal-storing histiocytosis associated with monoclonal gammopathy: molecular analysis of a disorder with rapid clinical course and review of the literature. Blood 100 (2002) 1817-1827
    • (2002) Blood , vol.100 , pp. 1817-1827
    • Lebeau, A.1    Zeindl-Eberhart, E.2    Müller, E.-C.3    Müller-Höcker, J.4    Jungblut, P.R.5    Emmerich, B.6
  • 54
    • 0017378921 scopus 로고
    • Arrangement of cytochrome-oxidase molecules in 2-dimensional vesicle crystals
    • Henderson R., Capaldi R.A., and Leigh J.S. Arrangement of cytochrome-oxidase molecules in 2-dimensional vesicle crystals. J Mol Biol 112 (1977) 631-648
    • (1977) J Mol Biol , vol.112 , pp. 631-648
    • Henderson, R.1    Capaldi, R.A.2    Leigh, J.S.3
  • 55
    • 0033984760 scopus 로고    scopus 로고
    • S-layer proteins
    • Sára M., and Sleytr U.B. S-layer proteins. J Bacteriol 182 (2000) 859-868
    • (2000) J Bacteriol , vol.182 , pp. 859-868
    • Sára, M.1    Sleytr, U.B.2
  • 56
  • 57
    • 0028820391 scopus 로고
    • How does Bacillus thuringiensis produce so much insecticidal crystal protein?
    • Agaisse H., and Lereclus D. How does Bacillus thuringiensis produce so much insecticidal crystal protein?. J Bacteriol 177 (1995) 6027-6032
    • (1995) J Bacteriol , vol.177 , pp. 6027-6032
    • Agaisse, H.1    Lereclus, D.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.