Cell-free analysis of tail-anchor protein targeting to membranes
Henderson, M.P.A., Billen, L.P., Kim, P.K., Andrews, D.W., Cell-free analysis of tail-anchor protein targeting to membranes. (2007) Methods, 41:427-38.
Read MoreSuppression of IP3-mediated calcium release and apoptosis by Bcl-2 involves the participation of protein phosphatase 1
Xu, L., Kong, D., Zhu, L., Zhu, W., Andrews, D.W., and Kuo, T.H., Suppression of IP3-mediated calcium release and apoptosis by Bcl-2 involves the participation of protein phosphatase 1. (2007) Mol. Cell Biochem., 295:153-65.
Read MoretBid elicits a conformational alteration in membrane-bound Bcl-2 such that it inhibits Bax pore formation
Peng J., Tan C., Roberts G.J., Nikolaeva O., Zhang, Z., Lapolla S.M., Primorac S., Andrews, D.W., and Lin J., tBid elicits a conformational alteration in membrane-bound Bcl-2 such that it inhibits Bax pore formation. (2006) J. Biol. Chem., 281:35082-11
Read MoreThe Carboxyl-Terminus of Cytochrome b5 Confers Endoplasmic Reticulum Specificity by Preventing Spontaneous Insertion into Membranes
Henderson, M.P.A., Hwang Y.T., Dyer, J.M., Mullen, R.T. and Andrews, D.W., The Carboxyl-Terminus of Cytochrome b5 Confers Endoplasmic Reticulum Specificity by Preventing Spontaneous Insertion into Membranes. (2006) Biochem. J., 401:701-9
Read MoreBcl-XL qualitatively different from and ten times more effective than Bcl-2 when expressed in a breast cancer cell line
Fiebig, A., Zhu, W., Hollerbach, C. Leber, B., and Andrews, D.W., Bcl-XL qualitatively different from and ten times more effective than Bcl-2 when expressed in a breast cancer cell line. (2006) BMC Cancer 6:213 [Highly Accessed]
Read MoreThe Structure of E. coli Signal Recognition Particle Revealed by Scanning Transmission Electron Microscopy
Mainprize, I.L., Beniac, D.R., Falkovskaia E., Cleverley R.M., Gierasch L.M., Ottensmeyer F.P., and Andrews, D.W., The Structure of coli Signal Recognition Particle Revealed by Scanning Transmission Electron Microscopy. (2006) Mol Biol. Cell., 17:5063-74.
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