Big Chemical Encyclopedia

Chemical substances, components, reactions, process design ...

Articles Figures Tables About

Retargeting

Two implementation decisions could be made immediately. First, DPMTA is based on the PVM message-passing library [11] and therefore it was necessary to base NAMD on PVM as well. All communication done by NAMD, however, would use an intermediate interface to allow communications to be easily retargeted to MPI [12] or other standards, and to simplify later implementation of communication optimizations such as combining messages destined for the same processor. Second, after much debate C++ was selected... [Pg.473]

ZHU, Q ZENG, C HUHALOV, A., YAO, J., TURI, T.G., DANLEY, D., HYNES, T CONG, Y., DIMATTIA, D., KENNEDY, S., DAUMY, G., SCHAEFFER, E., MARASCO, W.A., HUSTON, J.S., Extended half-life and elevated steady-state level of a single-chain Fv intrabody are critical for specific intracellular retargeting of its antigen, caspase-7, J. Immunol. Methods, 1999, 231, 207-222. [Pg.109]

Chaddock, J.A., Purkiss, J.R., Friis, L.M., Broadbridge, J.D., Duggan, M.J. Fooks, S.J., Shone, C.C., Quinn, C.P. and Foster, K.A., Inhibition of vesicular secretion in both neuronal and nonneuronal cells by a retargeted endopeptidase derivate of Clostridium botulinum neurotoxin type A, Infect. Immun., 68, 2587-2593, 2000. [Pg.212]

Ried, M.U., A. Girod, K. Leike, H. Buning, and M. Hallek, Adeno-associated virus capsids displaying immunoglobulin-binding domains permit antibody-mediated vector retargeting to specific cell surface receptors. J Virol, 2002. 76(9) 4559-66. [Pg.424]

Fisher, K.D. (2001). Polymer-coated adenovirus permits efficient retargeting and evades neutralising antibodies. Gene Ther., 8, 341-348. [Pg.367]

Dash, P.R., Read, M.L., Fisher, K.D., et al. (2000). Decreased binding to proteins and cells of polymeric gene delivery vectors surface modified with a multivalent hydrophilic polymer and retargeting through attachment of transferrin. J. Biol. Chem., 275, 3793-3802. [Pg.375]

J. Doukas, D. K. Hoganson, M. Ong, W. Ying, D. L. Lacey, A. Baird, G. F. Pierce, and B. A. Sosnowski, Retargeted delivery of adenoviral vectors through fibroblast growth factor receptors involves unique cellular pathways, FASEB J. 13 1459 (1999). [Pg.279]

S. L. Aukerman, Fibroblast growth factor 2-retargeted adenoviral vectors exhibit a modified biolocalization pattern and display reduced toxicity relative to native adenoviral vectors, Hum. Gene Ther. 11 191 (2000). [Pg.279]

D. M. Shayakhmetov, T. Papayannopoulou, G. Stamatoyannopoulos, and A. Lieber, Efficient gene transfer into human CD34(+) cells by a retargeted adenovirus vector, J. Virol. 74 2567 (2000). [Pg.280]

R. Y. Chung, Y. Saeki, and E. A. Chiocca, B-myb promoter retargeting of herpes simplex virus gamma34.5 gene-mediated virulence toward tumor and cycling cells, J. Virol. 73 7556 (1999). [Pg.286]

Fig. 7.2. The vast majority of mitochondrial proteins did not originate from the ancestral a-proteobacterial endosymbiont but from a variety of eukaryotic, eubacterial, and archaeal sources (Gabaldon and Huynen 2004 Esser et al. 2004 Timmis et al. 2004). The evolution of mitochondria was not only accompanied by a substantial loss of superfluous genes, but also by the transfer of many a-proteobacterial genes into the nucleus. As a consequence, many a-proteobacterial proteins were retargeted to other cellular compartments. Consequently, mitochondria and peroxisomes possess a similar fraction of proteins of a-proteobacterial proteins (Gabaldon et al. 2006), whereas up to 80% of the mitochondrial proteome can be made up from proteins that have various non-a-proteobacterial origins. (Modified from Gabaldon and Huynen 2004)... Fig. 7.2. The vast majority of mitochondrial proteins did not originate from the ancestral a-proteobacterial endosymbiont but from a variety of eukaryotic, eubacterial, and archaeal sources (Gabaldon and Huynen 2004 Esser et al. 2004 Timmis et al. 2004). The evolution of mitochondria was not only accompanied by a substantial loss of superfluous genes, but also by the transfer of many a-proteobacterial genes into the nucleus. As a consequence, many a-proteobacterial proteins were retargeted to other cellular compartments. Consequently, mitochondria and peroxisomes possess a similar fraction of proteins of a-proteobacterial proteins (Gabaldon et al. 2006), whereas up to 80% of the mitochondrial proteome can be made up from proteins that have various non-a-proteobacterial origins. (Modified from Gabaldon and Huynen 2004)...
In contrast, N- and P/Q-type Ca2+ currents are suppressed by stimulation of D1 receptors (Surmeier et al., 1995 Zhang et al., 2002). Surprisingly, inhibition of both PKA and PP-1 impairs the development of this effect. This suggests that the D1 receptor-dependent activation of PKA stimulates a PP-1-dependent dephosphorylation of Ca2+ channels, presumably by retargeting PP-1 in close vicinity of Ca2+ channels (Surmeier et al., 1995). In adrenal cells, dopamine inhibits T-type Ca2+ channel by stimulating... [Pg.118]

Introduction of a peptide into the AAV2 capsid is a viable strategy for retargeting AAV2 to additional cell types however, modifications in the AAV2 capsid often result in a reduction in vector yields, especially if the insertion is large. The unique N-terminal region of VP2 allows for peptide insertions without a loss of titer, when... [Pg.60]


See other pages where Retargeting is mentioned: [Pg.285]    [Pg.619]    [Pg.366]    [Pg.156]    [Pg.156]    [Pg.148]    [Pg.124]    [Pg.274]    [Pg.266]    [Pg.267]    [Pg.267]    [Pg.268]    [Pg.270]    [Pg.147]    [Pg.148]    [Pg.173]    [Pg.178]    [Pg.181]    [Pg.182]    [Pg.183]    [Pg.184]    [Pg.184]    [Pg.185]    [Pg.267]    [Pg.716]    [Pg.203]    [Pg.716]    [Pg.426]    [Pg.60]    [Pg.60]    [Pg.61]   
See also in sourсe #XX -- [ Pg.138 , Pg.173 , Pg.178 , Pg.184 ]




SEARCH



Adenoviral vectors retargeting

© 2024 chempedia.info