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Volumn 34, Issue 11, 2004, Pages 1187-1193

Molecular crowding as a mechanism for tick secretory granule biogenesis

Author keywords

Lipocalins; Ornithoros savignyi; Salivary glands; Ticks

Indexed keywords

PROTEIN;

EID: 7444259144     PISSN: 09651748     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.ibmb.2004.07.007     Document Type: Article
Times cited : (10)

References (35)
  • 1
    • 0032526224 scopus 로고    scopus 로고
    • Sorting and storage during secretory granule biogenesis: Looking backward and looking forward
    • P. Arvan, and D. Castle Sorting and storage during secretory granule biogenesis looking backward and looking forward Biochemical Journal 15 1998 593 610
    • (1998) Biochemical Journal , vol.15 , pp. 593-610
    • Arvan, P.1    Castle, D.2
  • 3
    • 0033851201 scopus 로고    scopus 로고
    • Basic mechanisms of secretion: Sorting into the regulated secretory pathway
    • M. Blazquez, and K.I. Shennan Basic mechanisms of secretion sorting into the regulated secretory pathway Biochemistry and Cell Biology 78 2000 181 191
    • (2000) Biochemistry and Cell Biology , vol.78 , pp. 181-191
    • Blazquez, M.1    Shennan, K.I.2
  • 5
    • 0017184389 scopus 로고
    • A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein dye-binding
    • M. Bradford A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein dye-binding Analytical Biochemistry 72 1976 248 254
    • (1976) Analytical Biochemistry , vol.72 , pp. 248-254
    • Bradford, M.1
  • 6
    • 0027605112 scopus 로고
    • Protein targeting to dense-core secretory granules
    • M.A.J. Chidgey Protein targeting to dense-core secretory granules BioEssays 15 1993 317 321
    • (1993) BioEssays , vol.15 , pp. 317-321
    • Chidgey, M.A.J.1
  • 7
    • 0016241224 scopus 로고
    • Importance of controls for the demonstration of carbohydrates in electron microscopy with the silver methanamine or the thiocarbohydrazide-silver proteinate methods
    • R. Courtoy, and L.J. Simar Importance of controls for the demonstration of carbohydrates in electron microscopy with the silver methanamine or the thiocarbohydrazide-silver proteinate methods Journal of Microscopy 100 1974 199 211
    • (1974) Journal of Microscopy , vol.100 , pp. 199-211
    • Courtoy, R.1    Simar, L.J.2
  • 8
    • 0035253217 scopus 로고    scopus 로고
    • Macromolecular crowding: An important but neglected aspect of the intracellular environment
    • R.J. Ellis Macromolecular crowding an important but neglected aspect of the intracellular environment Current Opinion in Structural Biology 11 2001 114 119
    • (2001) Current Opinion in Structural Biology , vol.11 , pp. 114-119
    • Ellis, R.J.1
  • 9
    • 0035478585 scopus 로고    scopus 로고
    • Macromolecular crowding: Obvious but underappreciated
    • R.J. Ellis Macromolecular crowding obvious but underappreciated Trends in Biochemical Sciences 26 2001 597 604
    • (2001) Trends in Biochemical Sciences , vol.26 , pp. 597-604
    • Ellis, R.J.1
  • 10
    • 0034043450 scopus 로고    scopus 로고
    • Signal-mediated sorting of neuropeptides and prohormones: Secretory granule biogenesis revisited
    • M.M. Glombik, and H.H. Gerdes Signal-mediated sorting of neuropeptides and prohormones secretory granule biogenesis revisited Biochimie 82 2000 315 326
    • (2000) Biochimie , vol.82 , pp. 315-326
    • Glombik, M.M.1    Gerdes, H.H.2
  • 11
    • 0014493079 scopus 로고
    • Isolation and properties of secretory granules from rat islets of Langerhans II. Ultrastructure of the beta granule.
    • M.H. Greider, S.L. Howell, and P.E. Lacy Isolation and properties of secretory granules from rat islets of Langerhans II. Ultrastructure of the beta granule. Journal of Cell Biology 41 1969 162 166
    • (1969) Journal of Cell Biology , vol.41 , pp. 162-166
    • Greider, M.H.1    Howell, S.L.2    Lacy, P.E.3
  • 13
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • U.K. Laemmli Cleavage of structural proteins during the assembly of the head of bacteriophage T4 Nature 227 1970 680 685
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 15
  • 16
    • 57649133146 scopus 로고    scopus 로고
    • Identification of putative proteins involved in granule biogenesis of tick salivary glands
    • B.J. Mans, J.D. Venter, P.J. Vrey, A.I. Louw, and A.W.H. Neitz Identification of putative proteins involved in granule biogenesis of tick salivary glands Electrophoresis 22 2001 1739 1746
    • (2001) Electrophoresis , vol.22 , pp. 1739-1746
    • Mans, B.J.1    Venter, J.D.2    Vrey, P.J.3    Louw, A.I.4    Neitz, A.W.H.5
  • 17
    • 0037743752 scopus 로고    scopus 로고
    • The major tick salivary gland proteins and toxins from the soft tick, Ornithodoros savignyi, are part of the tick lipocalin family: Implications for the origins of tick toxicoses
    • B.J. Mans, A.I. Louw, and A.W.H. Neitz The major tick salivary gland proteins and toxins from the soft tick, Ornithodoros savignyi, are part of the tick lipocalin family implications for the origins of tick toxicoses Molecular Biology and Evolution 20 2003 1158 1167
    • (2003) Molecular Biology and Evolution , vol.20 , pp. 1158-1167
    • Mans, B.J.1    Louw, A.I.2    Neitz, A.W.H.3
  • 18
    • 0742305631 scopus 로고    scopus 로고
    • Adaptation of ticks to a blood-feeding environment: Evolution from a functional perspective
    • B.J. Mans, and A.W.H. Neitz Adaptation of ticks to a blood-feeding environment evolution from a functional perspective Insect Biochemistry and Molecular Biology 34 2004 1 17
    • (2004) Insect Biochemistry and Molecular Biology , vol.34 , pp. 1-17
    • Mans, B.J.1    Neitz, A.W.H.2
  • 19
    • 2442560330 scopus 로고    scopus 로고
    • Exon-intron structure of outlier tick lipocalins indicate a monophyletic origin within the larger lipocalin family
    • in press.
    • Mans, B.J., Neitz, A.W.H., 2004b. Exon-intron structure of outlier tick lipocalins indicate a monophyletic origin within the larger lipocalin family. Insect Biochemistry and Molecular Biology, in press.
    • (2004) Insect Biochemistry and Molecular Biology
    • Mans, B.J.1    Neitz, A.W.H.2
  • 22
    • 0031022118 scopus 로고    scopus 로고
    • Influence of excluded volume upon macromolecular structure and associations in 'crowded' media
    • A.P. Minton Influence of excluded volume upon macromolecular structure and associations in 'crowded' media Current Opinion in Biotechnology 8 1997 65 69
    • (1997) Current Opinion in Biotechnology , vol.8 , pp. 65-69
    • Minton, A.P.1
  • 23
    • 0033969150 scopus 로고    scopus 로고
    • Implications of macromolecular crowding for protein assembly
    • A.P. Minton Implications of macromolecular crowding for protein assembly Current Opinion in Structural Biology 10 2000 34 39
    • (2000) Current Opinion in Structural Biology , vol.10 , pp. 34-39
    • Minton, A.P.1
  • 24
    • 0035815743 scopus 로고    scopus 로고
    • The influence of macromolecular crowding and macromolecular confinement on biochemical reactions in physiological media
    • A.P. Minton The influence of macromolecular crowding and macromolecular confinement on biochemical reactions in physiological media Journal of Biological Chemistry 276 2001 10577 10580
    • (2001) Journal of Biological Chemistry , vol.276 , pp. 10577-10580
    • Minton, A.P.1
  • 25
    • 0030614959 scopus 로고    scopus 로고
    • Identification of prokaryotic and eukaryotic signal peptides and prediction of their cleavage sites
    • H. Nielsen, J. Engelbrecht, S. Brunak, and G. von Heijne Identification of prokaryotic and eukaryotic signal peptides and prediction of their cleavage sites Protein Science 10 1997 1 6
    • (1997) Protein Science , vol.10 , pp. 1-6
    • Nielsen, H.1    Engelbrecht, J.2    Brunak, S.3    Von Heijne, G.4
  • 26
    • 0033040796 scopus 로고    scopus 로고
    • Tick histamine-binding proteins: Isolation, cloning, and three-dimensional structure
    • G.C. Paesen, P.L. Adams, K. Harlos, P.A. Nuttall, and D.I. Stuart Tick histamine-binding proteins isolation, cloning, and three-dimensional structure Molecular Cell 3 1999 661 671
    • (1999) Molecular Cell , vol.3 , pp. 661-671
    • Paesen, G.C.1    Adams, P.L.2    Harlos, K.3    Nuttall, P.A.4    Stuart, D.I.5
  • 27
    • 0001123138 scopus 로고
    • Effects of "crowding" in protein solutions
    • G.B. Ralston Effects of "crowding" in protein solutions Journal of Chemical Education 67 1990 857 860
    • (1990) Journal of Chemical Education , vol.67 , pp. 857-860
    • Ralston, G.B.1
  • 28
    • 0023174943 scopus 로고
    • Role of saliva in blood-feeding by arthropods
    • J.M.C. Ribeiro Role of saliva in blood-feeding by arthropods Annual Reviews in Entomology 32 1987 463 478
    • (1987) Annual Reviews in Entomology , vol.32 , pp. 463-478
    • Ribeiro, J.M.C.1
  • 31
    • 0032516858 scopus 로고    scopus 로고
    • Biogenesis of secretory granules in the trans-Golgi network of neuroendocrine and endocrine cells
    • S. Tooze Biogenesis of secretory granules in the trans-Golgi network of neuroendocrine and endocrine cells Biochimica et Biophysica Acta 1404 1998 231 244
    • (1998) Biochimica et Biophysica Acta , vol.1404 , pp. 231-244
    • Tooze, S.1
  • 33
    • 1042268889 scopus 로고    scopus 로고
    • Out with a bang! tetrahymena as a model system to study secretory granule biogenesis
    • A.P. Turkewitz Out with a bang! tetrahymena as a model system to study secretory granule biogenesis Traffic 5 2004 63 68
    • (2004) Traffic , vol.5 , pp. 63-68
    • Turkewitz, A.P.1
  • 34
    • 0030759249 scopus 로고    scopus 로고
    • Formation of secretory vesicles in the biosynthetic pathway
    • S. Urbé, S.A. Tooze, and F.A. Barr Formation of secretory vesicles in the biosynthetic pathway Biochimica et Biophysica Acta 1358 1997 6 22
    • (1997) Biochimica et Biophysica Acta , vol.1358 , pp. 6-22
    • Urbé, S.1    Tooze, S.A.2    Barr, F.A.3
  • 35
    • 0027496418 scopus 로고
    • Macromolecular crowding effects on macromolecular interactions: Some implications for genome structure and function
    • S.B. Zimmerman Macromolecular crowding effects on macromolecular interactions some implications for genome structure and function Biochimica et Biophysica Acta 1216 1993 175 185
    • (1993) Biochimica et Biophysica Acta , vol.1216 , pp. 175-185
    • Zimmerman, S.B.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.