메뉴 건너뛰기




Volumn 429, Issue 2, 2010, Pages 261-271

An extracellular transglutaminase is required for apple pollen tube growth

Author keywords

Extracellular localization; Malus domestica; Pollen tube growth; Polyamine; Protein cross link; Transglutaminase

Indexed keywords

EXTRACELLULAR; MALUS DOMESTICA; POLLEN TUBE GROWTH; POLYAMINES; PROTEIN CROSS-LINK; TRANSGLUTAMINASES;

EID: 77954754937     PISSN: 02646021     EISSN: 14708728     Source Type: Journal    
DOI: 10.1042/BJ20100291     Document Type: Article
Times cited : (41)

References (50)
  • 1
    • 0041966088 scopus 로고    scopus 로고
    • Control of pollen tube growth: Role of ion gradients and fluxes
    • Holdaway-Clarke, T. L. and Hepler, P. K. (2003) Control of pollen tube growth: role of ion gradients and fluxes. New Phytol. 159, 539-563
    • (2003) New Phytol. , vol.159 , pp. 539-563
    • Holdaway-Clarke, T.L.1    Hepler, P.K.2
  • 2
    • 0008904539 scopus 로고
    • Pollen-stigma interaction in grasses: A brief review
    • Heslop-Harrison, J. (1979) Pollen-stigma interaction in grasses: a brief review. New Zealand J. Bot. 17, 537-546
    • (1979) New Zealand J. Bot. , vol.17 , pp. 537-546
    • Heslop-Harrison, J.1
  • 3
    • 0037215676 scopus 로고    scopus 로고
    • Characterization and localization of the transmitting tissue-specific PELPIII proteins of Nicotiana tabacum
    • de Graaf, B. H. J., Knuiman, B. A., Derksen, J. and Mariani, C. (2003) Characterization and localization of the transmitting tissue-specific PELPIII proteins of Nicotiana tabacum. J. Exp. Bot. 54, 55-63
    • (2003) J. Exp. Bot. , vol.54 , pp. 55-63
    • De Graaf, B.H.J.1    Knuiman, B.A.2    Derksen, J.3    Mariani, C.4
  • 4
    • 0029081037 scopus 로고
    • A floral transmitting tissue-specific glycoprotein attracts pollen tubes and stimulates their growth
    • Cheung, A. Y., Wang, H. and Wu, H. (1995) A floral transmitting tissue-specific glycoprotein attracts pollen tubes and stimulates their growth. Cell 82, 383-393
    • (1995) Cell , vol.82 , pp. 383-393
    • Cheung, A.Y.1    Wang, H.2    Wu, H.3
  • 5
    • 0036437302 scopus 로고    scopus 로고
    • The mechanisms of pollination and fertilization in plants
    • Lord, E. M. and Russell, S. D. (2002) The mechanisms of pollination and fertilization in plants. Ann. Rev. Cell Develop. Biol. 18, 81-105
    • (2002) Ann. Rev. Cell Develop. Biol. , vol.18 , pp. 81-105
    • Lord, E.M.1    Russell, S.D.2
  • 6
    • 0005747424 scopus 로고
    • Compounds released from incompatible apple pollen during in vitro germination
    • Speranza, A. and Calzoni, G. L. (1980) Compounds released from incompatible apple pollen during in vitro germination. Z. Pflanzenphysiol. 97, 95-102
    • (1980) Z. Pflanzenphysiol. , vol.97 , pp. 95-102
    • Speranza, A.1    Calzoni, G.L.2
  • 7
    • 0000364270 scopus 로고
    • RNA, proteins and polyamines during tube growth in germinating apple pollen
    • Bagni, N., Adamo, P. and Serafini-Fracassini, D. (1981) RNA, proteins and polyamines during tube growth in germinating apple pollen. Plant Physiol. 68, 727-730
    • (1981) Plant Physiol. , vol.68 , pp. 727-730
    • Bagni, N.1    Adamo, P.2    Serafini-Fracassini, D.3
  • 8
    • 77954914015 scopus 로고    scopus 로고
    • Identification of markers for sexual determination in Actinidia deliciosa
    • Biasi, R., Altamura, M. M. and Bagni, N. (1999) Identification of markers for sexual determination in Actinidia deliciosa. Acta Hortic. 498, 93-97
    • (1999) Acta Hortic. , vol.498 , pp. 93-97
    • Biasi, R.1    Altamura, M.M.2    Bagni, N.3
  • 9
    • 79952200367 scopus 로고    scopus 로고
    • Polyamine biosynthesis and control of the development of functional pollen in kiwifruit
    • doi:10.1016/j.plaphy.2010.02.013
    • Falasca, G., Franceschetti, M., Bagni, N., Altamura, M. M. and Biasi, R. (2010) Polyamine biosynthesis and control of the development of functional pollen in kiwifruit. Plant Physiol. Biochem., doi:10.1016/j.plaphy.2010.02.013
    • (2010) Plant Physiol. Biochem.
    • Falasca, G.1    Franceschetti, M.2    Bagni, N.3    Altamura, M.M.4    Biasi, R.5
  • 10
    • 0028039340 scopus 로고
    • Changes in polyamine synthesis during anther development and pollen germination in tobacco (Nicotiana tabacum)
    • DOI 10.1034/j.1399-3054.1994.920109.x
    • Chibi, F., Matilla, A. J., Angosto, T. and Garrido, D. (1994) Changes in polyamine synthesis during anther development and pollen germination in tobacco ( Nicotiana tabacum). Physiol. Plant. 92, 61-68 (Pubitemid 2137676)
    • (1994) Physiologia Plantarum , vol.92 , Issue.1 , pp. 61-68
    • Chibi, F.1    Matilla, A.J.2    Angosto, T.3    Garrido, D.4
  • 11
    • 42449156764 scopus 로고    scopus 로고
    • Bis(guanylhydrazones) negatively affected in vitro germination of kiwi fruit pollen and alter the endogenous polyamine pool
    • Antognoni, F. and Bagni, N. (2008) Bis(guanylhydrazones) negatively affected in vitro germination of kiwi fruit pollen and alter the endogenous polyamine pool. Plant Biol. 10, 334-341
    • (2008) Plant Biol. , vol.10 , pp. 334-341
    • Antognoni, F.1    Bagni, N.2
  • 13
    • 27644503707 scopus 로고    scopus 로고
    • Do polyamines contribute to plant cell wall assembly by forming amide bonds with pectins?
    • Lenucci, M., Piro, G., Miller, J. G., Dalessandro, G. and Fry, S. C. (2005) Do polyamines contribute to plant cell wall assembly by forming amide bonds with pectins? Phytochemistry 66, 2581-2594
    • (2005) Phytochemistry , vol.66 , pp. 2581-2594
    • Lenucci, M.1    Piro, G.2    Miller, J.G.3    Dalessandro, G.4    Fry, S.C.5
  • 14
    • 64249148286 scopus 로고    scopus 로고
    • A BAHD acyltransferase is expressed in the tapetum of Arabidopsis anthers and is involved in the synthesis of hydroxycinnamoyl spermidines
    • Grienenberger, E., Besseau, S., GeoVroy, P., Debayle, D., Heintz, D., Lapierre, C., Pollet, B., Heitz, T. and Legrand, M. (2009) A BAHD acyltransferase is expressed in the tapetum of Arabidopsis anthers and is involved in the synthesis of hydroxycinnamoyl spermidines. Plant J. 58, 246-259
    • (2009) Plant J. , vol.58 , pp. 246-259
    • Grienenberger, E.1    Besseau, S.2    Geovroy, P.3    Debayle, D.4    Heintz, D.5    Lapierre, C.6    Pollet, B.7    Heitz, T.8    Legrand, M.9
  • 15
    • 0028873507 scopus 로고
    • Trisubstituted hydroxycinnamic acid spermidines from Quercus dentata pollen
    • Bokern, M., Witte, L., Wray, V., Nimtz, M. and Meurer-Grimes, B. (1995) Trisubstituted hydroxycinnamic acid spermidines from Quercus dentata pollen. Phytochemistry 39, 1371-1375
    • (1995) Phytochemistry , vol.39 , pp. 1371-1375
    • Bokern, M.1    Witte, L.2    Wray, V.3    Nimtz, M.4    Meurer-Grimes, B.5
  • 16
    • 0037317032 scopus 로고    scopus 로고
    • Transglutaminases: Crosslinking enzymes with pleiotropic functions
    • Lorand, L. and Graham, R. M. (2003) Transglutaminases: crosslinking enzymes with pleiotropic functions. Nat. Rev. Mol. Cell Biol. 4, 140-156
    • (2003) Nat. Rev. Mol. Cell Biol. , vol.4 , pp. 140-156
    • Lorand, L.1    Graham, R.M.2
  • 17
    • 0036901574 scopus 로고    scopus 로고
    • Transglutaminases: Nature's biological glues
    • Griffin, M., Casadio, R. and Bergamini, C. (2002) Transglutaminases: nature's biological glues. Biochem. J. 368, 377-396
    • (2002) Biochem. J. , vol.368 , pp. 377-396
    • Griffin, M.1    Casadio, R.2    Bergamini, C.3
  • 19
    • 0010115712 scopus 로고    scopus 로고
    • Reduced expression of tissue transglutaminase in a human endothelial cell line leads to changes in cell spreading, cell adhesion and reduced polymerisation of fibronectin
    • Jones, R. A., Nicholas, B., Mian, S., Davies, P. J. and Griffin, M. (1997) Reduced expression of tissue transglutaminase in a human endothelial cell line leads to changes in cell spreading, cell adhesion and reduced polymerisation of fibronectin. J. Cell Sci. 110, 2461-2472 (Pubitemid 127699160)
    • (1997) Journal of Cell Science , vol.110 , Issue.19 , pp. 2461-2472
    • Jones, R.A.1    Nicholas, B.2    Mian, S.3    Davies, P.J.A.4    Griffin, M.5
  • 20
    • 0142242157 scopus 로고    scopus 로고
    • A novel RGD independent cell adhesion pathway mediated by fibronectin-bound tissue transglutaminase rescues cells from anoikis
    • Verderio, E., Telci, D., Okoye, A., Melino, G. and Griffin, M. (2003) A novel RGD independent cell adhesion pathway mediated by fibronectin-bound tissue transglutaminase rescues cells from anoikis. J. Biol. Chem. 278, 42604-42614
    • (2003) J. Biol. Chem. , vol.278 , pp. 42604-42614
    • Verderio, E.1    Telci, D.2    Okoye, A.3    Melino, G.4    Griffin, M.5
  • 21
    • 18244399091 scopus 로고    scopus 로고
    • Transglutaminase-mediated oligomerization of the fibrin(ogen) αC-domains promotes integrin-dependent cell adhesion and signaling
    • Belkin, A. M., Tsurupa, G., Zemskov, E., Veklich, Y., Weisel, J. W. and Medved, L. (2005) Transglutaminase-mediated oligomerization of the fibrin(ogen) αC-domains promotes integrin-dependent cell adhesion and signaling. Blood 105, 3561-3568
    • (2005) Blood , vol.105 , pp. 3561-3568
    • Belkin, A.M.1    Tsurupa, G.2    Zemskov, E.3    Veklich, Y.4    Weisel, J.W.5    Medved, L.6
  • 22
    • 0037053359 scopus 로고    scopus 로고
    • Analysis of tissue transglutaminase function in the migration of Swiss 3T3 fibroblasts: The active-state conformation of the enzyme does not affect cell motility but is important for its secretion
    • Balklava, Z., Verderio, E., Collighan, R., Gross, S., Adams, J. and Griffin, M. (2002) Analysis of tissue transglutaminase function in the migration of Swiss 3T3 fibroblasts: the active-state conformation of the enzyme does not affect cell motility but is important for its secretion. J. Biol. Chem. 277, 16567-16575
    • (2002) J. Biol. Chem. , vol.277 , pp. 16567-16575
    • Balklava, Z.1    Verderio, E.2    Collighan, R.3    Gross, S.4    Adams, J.5    Griffin, M.6
  • 23
    • 67650513329 scopus 로고    scopus 로고
    • Heparan sulfate proteoglycans are receptors for the cell-surface trafficking and biological activity of transglutaminase-2
    • Scarpellini, A., Germack, R., Lortat-Jacob, H., Muramatsu, T., Billett, E., Johnson, T. and Verderio, E. (2009) Heparan sulfate proteoglycans are receptors for the cell-surface trafficking and biological activity of transglutaminase-2. J. Biol. Chem. 284, 18411-18423
    • (2009) J. Biol. Chem. , vol.284 , pp. 18411-18423
    • Scarpellini, A.1    Germack, R.2    Lortat-Jacob, H.3    Muramatsu, T.4    Billett, E.5    Johnson, T.6    Verderio, E.7
  • 24
    • 47649091159 scopus 로고    scopus 로고
    • Tranglutaminases: Widespread cross-linking enzymes in plants
    • Serafini-Fracassini, D. and Del Duca, S. (2008) Tranglutaminases: widespread cross-linking enzymes in plants. Ann. Bot. 102, 145-152
    • (2008) Ann. Bot. , vol.102 , pp. 145-152
    • Serafini-Fracassini, D.1    Del Duca, S.2
  • 25
    • 0030905623 scopus 로고    scopus 로고
    • Transglutaminase-catalized modification of cytoskeletal proteins by polyamines during the germination of Malus domestica pollen
    • Del Duca, S., Bregoli, A. M., Bergamini, C. and Serafini-Fracassini, D. (1997) Transglutaminase-catalized modification of cytoskeletal proteins by polyamines during the germination of Malus domestica pollen. Sex. Plant Reprod. 10, 89-95
    • (1997) Sex. Plant Reprod. , vol.10 , pp. 89-95
    • Del Duca, S.1    Bregoli, A.M.2    Bergamini, C.3    Serafini-Fracassini, D.4
  • 26
    • 62149146855 scopus 로고    scopus 로고
    • Effects of post-translational modifications catalyzed by pollen transglutaminase on the functional properties of microtubules and actin filaments
    • Del Duca, S., Serafini-Fracassini, D., Bonner, P., Cresti, M. and Cai, G. (2009) Effects of post-translational modifications catalyzed by pollen transglutaminase on the functional properties of microtubules and actin filaments. Biochem. J. 418, 651-664
    • (2009) Biochem. J. , vol.418 , pp. 651-664
    • Del Duca, S.1    Serafini-Fracassini, D.2    Bonner, P.3    Cresti, M.4    Cai, G.5
  • 27
    • 47649092897 scopus 로고    scopus 로고
    • Visualisation of transglutaminase-mediated cross-linking activity in germinating pollen by laser confocal microscopy
    • Iorio, R. A., Di Sandro, A., Scarpellini, A., Del Duca, S., Serafini-Fracassini, D. and Verderio, E. (2008) Visualisation of transglutaminase-mediated cross-linking activity in germinating pollen by laser confocal microscopy. Plant Biosystems 142, 360-365
    • (2008) Plant Biosystems , vol.142 , pp. 360-365
    • Iorio, R.A.1    Di Sandro, A.2    Scarpellini, A.3    Del Duca, S.4    Serafini-Fracassini, D.5    Verderio, E.6
  • 28
    • 0033230231 scopus 로고    scopus 로고
    • A transglutaminase immunologically related to tissue transglutaminase catalyzes cross-linking of cell wall proteins in Chlamydomonas reinhardtii
    • Waffenschmidt, S., Kusch, T. and Woessner, J. P. (1999) A transglutaminase immunologically related to tissue transglutaminase catalyzes cross-linking of cell wall proteins in Chlamydomonas reinhardtii. Plant Physiol. 121, 1003-1015
    • (1999) Plant Physiol. , vol.121 , pp. 1003-1015
    • Waffenschmidt, S.1    Kusch, T.2    Woessner, J.P.3
  • 29
    • 34250683461 scopus 로고    scopus 로고
    • The acropetal wave of developmental cell death (DCD) of Nicotiana tabacum corolla is preceded by activation of transglutaminase in different cell compartments
    • Della Mea, M., De Filippis, F., Genovesi, V., Serafini-Fracassini, D. and Del Duca, S. (2007) The acropetal wave of developmental cell death (DCD) of Nicotiana tabacum corolla is preceded by activation of transglutaminase in different cell compartments. Plant Physiol. 144, 1211-1222
    • (2007) Plant Physiol. , vol.144 , pp. 1211-1222
    • Della Mea, M.1    De Filippis, F.2    Genovesi, V.3    Serafini-Fracassini, D.4    Del Duca, S.5
  • 30
    • 0027935343 scopus 로고
    • Transglutaminase inhibition by 2-[(2-Oxopropyl)thio] imidazolium derivatives: Mechanism of Factor XIIIa inactivation
    • Freund, K. F., Doshi, K. P., Gaul, S., Claremon, D. A., Remy, D. C., Baldwin, J. J., Pitzenberger, S. M. and Stern, A. M. (1994) Transglutaminase inhibition by 2-[(2-Oxopropyl)thio] imidazolium derivatives: mechanism of Factor XIIIa inactivation. Biochemistry 33, 10109-10119
    • (1994) Biochemistry , vol.33 , pp. 10109-10119
    • Freund, K.F.1    Doshi, K.P.2    Gaul, S.3    Claremon, D.A.4    Remy, D.C.5    Baldwin, J.J.6    Pitzenberger, S.M.7    Stern, A.M.8
  • 34
    • 33746472503 scopus 로고    scopus 로고
    • The role of tissue transglutaminase in 1-methyl-4-phenylpyridinium(MPP+)- induced toxicity in different human SH-SY5Y neuroblastoma cells
    • Beck, K. E., De Girolamo, L. A., Griffin, M. and Billet, E. E. (2006) The role of tissue transglutaminase in 1-methyl-4-phenylpyridinium(MPP+)-induced toxicity in different human SH-SY5Y neuroblastoma cells. Neurosci. Lett. 405, 46-51
    • (2006) Neurosci. Lett. , vol.405 , pp. 46-51
    • Beck, K.E.1    De Girolamo, L.A.2    Griffin, M.3    Billet, E.E.4
  • 36
    • 0035150905 scopus 로고    scopus 로고
    • A simple assay and histochemical localization of transglutaminase activity using a derivative of green fluorescent protein as a substrate
    • Furutani, Y., Kato, A., Notoya, M., Ghoneim, M. A. and Hirose, S. (2001) A simple assay and histochemical localization of transglutaminase activity using a derivative of green fluorescent protein as a substrate. J. Histochem. Cytochem. 9, 247-258
    • (2001) J. Histochem. Cytochem. , vol.9 , pp. 247-258
    • Furutani, Y.1    Kato, A.2    Notoya, M.3    Ghoneim, M.A.4    Hirose, S.5
  • 38
    • 0033791741 scopus 로고    scopus 로고
    • Identification and characterization of a novel microtubule-based motor associated with membranous organelles in tobacco pollen tubes
    • Cai, G., Romagnoli, S., Moscatelli, A., Ovidi, E., Gambellini, G., Tiezzi, A. and Cresti, M. (2000) Identification and characterization of a novel microtubule-based motor associated with membranous organelles in tobacco pollen tubes. Plant Cell 12, 1719-1736
    • (2000) Plant Cell , vol.12 , pp. 1719-1736
    • Cai, G.1    Romagnoli, S.2    Moscatelli, A.3    Ovidi, E.4    Gambellini, G.5    Tiezzi, A.6    Cresti, M.7
  • 39
    • 4444310397 scopus 로고
    • Cell-wall proteins in pollen and roots of Lilium longiflorum: Extraction and partial characterization
    • Yi-Qin, L., Croes, A. F. and Linskens, H. F. (1983) Cell-wall proteins in pollen and roots of Lilium longiflorum: extraction and partial characterization. Planta 158, 422-427
    • (1983) Planta , vol.158 , pp. 422-427
    • Yi-Qin, L.1    Croes, A.F.2    Linskens, H.F.3
  • 40
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • Laemmli, U. K. (1970) Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature 227, 680-685
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 41
    • 0001653786 scopus 로고    scopus 로고
    • 2+-dependent transglutaminase activity in root and leaf tissue of monocotyledonous and dicotyledonous plants
    • 2+-dependent transglutaminase activity in root and leaf tissue of monocotyledonous and dicotyledonous plants. Plant Physiol. 117, 1115-1123
    • (1998) Plant Physiol. , vol.117 , pp. 1115-1123
    • Lilley, G.R.1    Skill, J.2    Griffin, M.3    Bonner, P.L.4
  • 42
    • 0028831597 scopus 로고
    • Polyamines in chloroplasts: Identification of their glutamyl- And acetyl-derivatives
    • Del Duca, S., Beninati, S. and Serafini-Fracassini, D. (1995) Polyamines in chloroplasts: identification of their glutamyl- and acetyl-derivatives. Biochem. J. 305, 233-237
    • (1995) Biochem. J. , vol.305 , pp. 233-237
    • Del Duca, S.1    Beninati, S.2    Serafini-Fracassini, D.3
  • 43
    • 0029166933 scopus 로고
    • Identification and localization of three classes of myosins in pollen tubes of Lilium longiflorumand Nicotiana alata
    • Miller, D. D., Scordilis, S. P. and Hepler, P. K. (1995) Identification and localization of three classes of myosins in pollen tubes of Lilium longiflorumand Nicotiana alata. J. Cell Sci. 108, 2549-2653
    • (1995) J. Cell Sci. , vol.108 , pp. 2549-2653
    • Miller, D.D.1    Scordilis, S.P.2    Hepler, P.K.3
  • 45
    • 0027745789 scopus 로고
    • Distribution of microtubules during the growth of tobacco pollen tubes
    • Del Casino, C., Li, Y., Moscatelli, A., Scali, M., Tiezzi, A. and Cresti, M. (1993) Distribution of microtubules during the growth of tobacco pollen tubes. Biol. Cell 79, 125-132
    • (1993) Biol. Cell , vol.79 , pp. 125-132
    • Del Casino, C.1    Li, Y.2    Moscatelli, A.3    Scali, M.4    Tiezzi, A.5    Cresti, M.6
  • 46
    • 0345169048 scopus 로고    scopus 로고
    • Post-translational modifications regulate microtubule function
    • DOI 10.1038/nrm1260
    • Westermann, S. and Weber, K. (2003) Post-translational modifications regulate microtubule function. Nature 4, 938-947 (Pubitemid 37493642)
    • (2003) Nature Reviews Molecular Cell Biology , vol.4 , Issue.12 , pp. 938-947
    • Westermann, S.1    Weber, K.2
  • 47
    • 4444225815 scopus 로고    scopus 로고
    • Definition of the fine specificity of the monoclonal antibody 81D4: Its reactivity with lysine and polyamine isopeptide cross-links
    • Thomas, V., Fournet, G., Simonet, F., Roch, A. M., Ceylan, I., El Alaouia, S. and Quash, G. (2004) Definition of the fine specificity of the monoclonal antibody 81D4: its reactivity with lysine and polyamine isopeptide cross-links. J. Immunol. Met. 292, 83-95
    • (2004) J. Immunol. Met. , vol.292 , pp. 83-95
    • Thomas, V.1    Fournet, G.2    Simonet, F.3    Roch, A.M.4    Ceylan, I.5    El Alaouia, S.6    Quash, G.7
  • 48
    • 0010257285 scopus 로고
    • Presumed phylogenetic basis of the correlation of pectin deposition pattern in pollen tube walls and the stylar structure of angiosperms
    • Li, Y. Q., Fang, C., Faleri, C., Ciampolini, F., Linskens, H. F. and Cresti, M. (1995) Presumed phylogenetic basis of the correlation of pectin deposition pattern in pollen tube walls and the stylar structure of angiosperms. Proc. Kon. Ned. Akad. v. Wetensch. 98, 39-44
    • (1995) Proc. Kon. Ned. Akad. V. Wetensch. , vol.98 , pp. 39-44
    • Li, Y.Q.1    Fang, C.2    Faleri, C.3    Ciampolini, F.4    Linskens, H.F.5    Cresti, M.6
  • 49
    • 0034695929 scopus 로고    scopus 로고
    • Tissue transglutaminase is an integrin-binding adhesion coreceptor for fibronectin
    • Akimov, S. S., Krylov, D., Fleischman, L. F. and Belkin, A. M. (2000) Tissue transglutaminase is an integrin-binding adhesion coreceptor for fibronectin. J. Cell Biol. 148, 825-838
    • (2000) J. Cell Biol. , vol.148 , pp. 825-838
    • Akimov, S.S.1    Krylov, D.2    Fleischman, L.F.3    Belkin, A.M.4
  • 50
    • 0032747129 scopus 로고    scopus 로고
    • Cell surface localisation of tissue transglutaminase is dependent on a fibronectin-binding site in its N-terminal β-sandwich domain
    • Gaudry, C. A., Verderio, E., Aeschlimann, D., Cox, A., Smith, C. and Griffin, M. (1999) Cell surface localisation of tissue transglutaminase is dependent on a fibronectin-binding site in its N-terminal β-sandwich domain. J. Biol. Chem. 274, 30707-30714
    • (1999) J. Biol. Chem. , vol.274 , pp. 30707-30714
    • Gaudry, C.A.1    Verderio, E.2    Aeschlimann, D.3    Cox, A.4    Smith, C.5    Griffin, M.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.