References
- J. Cell Biol. v.76 Allen, R.E.;Stromer, M.H.;Goll. D.E.;Robson, R.M. https://doi.org/10.1083/jcb.76.1.98
- J. Bact. v.131 Bacchi, C.J.;Lipschick, G.Y.;Nathan, H.C.
- Biochim. Biophys. Acta v.952 Beninati, S.;Piacenti, N.;Cocuzzi, E.T.;Autori, F.;Folk, J.E. https://doi.org/10.1016/0167-4838(88)90134-3
- Anal. Biochem. v.72 Bradford, M.M. https://doi.org/10.1016/0003-2697(76)90527-3
- Phill. Trans. R. Soc. Lond. v.B299 Burridge, K.;Kelly, T.;Connell, L.
- Signal Transduction during Biomembrane Fusion David, J.D.;Fitzpatrick, A.;O'DAy, D.H.(ed.)
- Dev. Biol. v.82 David, J.D.;Higgenbotham, C.A.
- Cell v.13 Devlin, R.B.;Emerson, C.P. https://doi.org/10.1016/0092-8674(78)90211-8
- Plant Physiol. v.69 Flores, H.E.;Galston, A.W. https://doi.org/10.1104/pp.69.3.701
- Fed, Proc. Fed. Am. Soc. Exp. Biol. v.45 Goldstone, A.;Koenig, A.;Lu, C.Y.
- Eur. J. Cell Biol. v.30 Grant, N.J.;Oriol-Audit, J.;Dickens, M.J.
- Korean Biochem. J. v.26 Hah, J.C.;Kim, H.D.;Kang, H.S.;Kim, C.R.
- Differentiation v.19 Heby, O. https://doi.org/10.1111/j.1432-0436.1981.tb01123.x
- Adv. Enzyme Regul. v.24 Heby, O. https://doi.org/10.1016/0065-2571(85)90072-X
- Carcinogenesis v.9 Hibasami, H.;Tsukada, T.;Maekawa, S.;Sakurai, M;Nakashima, K. https://doi.org/10.1093/carcin/9.2.199
- Cancer Res. v.49 Hinasami, H.;Maekawa, S.;Murata, T.;Nakashima, K.
- Bilchem. Biophys. Res. Commun. v.133 Iqbal, Z.;Koenig, H. https://doi.org/10.1016/0006-291X(85)90943-X
- Biochem. Biophys. Acta v.473 Janne, J.;Poso, H.;Raina, A.
- J. Neurochem. v.48 Jensen, J.R.;Lynch, G.;Baudry, M. https://doi.org/10.1111/j.1471-4159.1987.tb05583.x
- Exp. Cell. Res. v.183 Kaczmarek, L.;Kaminska, B.
- Exp. Cell Res. v.191 Kaminska, B.;Kaczmarek, L.;Grzelakowska-Sztabert, B. https://doi.org/10.1016/0014-4827(90)90010-8
- FEBS Lett. v.304 Kaminska, B.;Kaczmarek, L.;Grzelakowska-Sztabert, B. https://doi.org/10.1016/0014-5793(92)80618-Q
- Biochem. Biophys. Res. Commun. v.153 Koenig, H.;Goldstone, A.;Lu, C.Y. https://doi.org/10.1016/S0006-291X(88)81352-4
- Nature v.227 Laemmli, U.K. https://doi.org/10.1038/227680a0
- J. Mol. Biol. v.34 Liquori, A.M.;Constantino, L;Crescenzi, V.;Elia, V.;Pultti, R.;DeSanti-Savino, M.;Vitagliano. V.
- J. Cell. Biol. v.108 Mercier, F.;Reggio, H.;Devilliers, G.;Bataille, D.;Mangert, P. https://doi.org/10.1083/jcb.108.2.441
- J. Biol. Chem. v.259 Nicchitta, C.V.;Williamson, J.R.
- J. Lab. Clin. Med. v.62 Nielsen, L.;Ludvigsen, B.
- Biochem. J. v.61 Oliver, I.T. https://doi.org/10.1042/bj0610116
- J. Cell Boil. v.52 O'Neill, M.C.;Stodkdale, F.E. https://doi.org/10.1083/jcb.52.1.52
- Dev. Boil. v.29 Paterson, B.;Strohman, R.C. https://doi.org/10.1016/0012-1606(72)90050-4
- J. Bact. v.152 Paulus, T.J.;Kiyono, P.;David, R.H.
- Biochem. J. v.234 Pegg, A.E. https://doi.org/10.1042/bj2340249
- Cancer Res. v.40 Pleshkewych, A.;Kramer, D.L.;Kelly, E.;Porter, C.W.
- Cancer Res. v.39 Porter, C.W.;Milkes-Robertson, F.;Kramer, D.;Dave, C.
- J. Chromatogr. v.170 Redmond, J.W.;Tseng, A.
- Biochem. J. v.260 Schuber, F. https://doi.org/10.1042/bj2600001
- Dev. Biol. v.25 Shainberg, A;Yagil, G;Yaffe, D. https://doi.org/10.1016/0012-1606(71)90017-0
- Am. J.Physiol. v.264 Sjoholm, A. https://doi.org/10.1152/ajpcell.1993.264.3.C501
- Annu. Rev. Plant Physiol. v.36 Smith, T.A. https://doi.org/10.1146/annurev.pp.36.060185.001001
- Annu, Rev. Biochem. v.45 Tabor, C.W.;Tabor, H. https://doi.org/10.1146/annurev.bi.45.070176.001441
- Annu. Rev. Biochem. v.53 Tabor, C.W.;Tabor, H. https://doi.org/10.1146/annurev.bi.53.070184.003533
- Biochem. J. v.236 Tadolini, B.;Varani, E.;Cabrini, L. https://doi.org/10.1042/bj2360651
- Biochem. J. v.249 Tadolini, B. https://doi.org/10.1042/bj2490033
- J. Cell Biol. v.90 Tilney, LG.;Bonder, E.M.;DeRosier, D.J. https://doi.org/10.1083/jcb.90.2.485
- Biochem. J. v.228 Wakelman, M.J.O. https://doi.org/10.1042/bj2280001
- J. Protozool. v.13 Wallis, O.C. https://doi.org/10.1111/j.1550-7408.1966.tb01900.x
- The Enzymes (Boyer ed.) Vol.III Watts, D.C.
- Adv, Enzyme Regul. v.10 Williams-Ashman, H.G.;Janne, J.;Coppoc, G.L.;Geroch, M.E.;Schenone, A.