-
1
-
-
0024040279
-
-
1. Creighton, T.E. Proc. Natl. Acad Sci. U.S.A. 1988, 85, 5082. Protein Folding: Deciphering the Second Half of the Genetic Code; Gierasch, L.M.; King, J. Eds.; American Association for the Advancement of Science: Washington DC, 1990. Creighton, T.E. Biochem. J. 1990, 270, 1; Jaenicke, R. Biochemistry 1991, 30, 3147.
-
(1988)
Proc. Natl. Acad Sci. U.S.A.
, vol.85
, pp. 5082
-
-
Creighton, T.E.1
-
2
-
-
0024040279
-
-
American Association for the Advancement of Science: Washington DC
-
1. Creighton, T.E. Proc. Natl. Acad Sci. U.S.A. 1988, 85, 5082. Protein Folding: Deciphering the Second Half of the Genetic Code; Gierasch, L.M.; King, J. Eds.; American Association for the Advancement of Science: Washington DC, 1990. Creighton, T.E. Biochem. J. 1990, 270, 1; Jaenicke, R. Biochemistry 1991, 30, 3147.
-
(1990)
Protein Folding: Deciphering the Second Half of the Genetic Code
-
-
Gierasch, L.M.1
King, J.2
-
3
-
-
0025179832
-
-
1. Creighton, T.E. Proc. Natl. Acad Sci. U.S.A. 1988, 85, 5082. Protein Folding: Deciphering the Second Half of the Genetic Code; Gierasch, L.M.; King, J. Eds.; American Association for the Advancement of Science: Washington DC, 1990. Creighton, T.E. Biochem. J. 1990, 270, 1; Jaenicke, R. Biochemistry 1991, 30, 3147.
-
(1990)
Biochem. J.
, vol.270
, pp. 1
-
-
Creighton, T.E.1
-
4
-
-
0025876740
-
-
1. Creighton, T.E. Proc. Natl. Acad Sci. U.S.A. 1988, 85, 5082. Protein Folding: Deciphering the Second Half of the Genetic Code; Gierasch, L.M.; King, J. Eds.; American Association for the Advancement of Science: Washington DC, 1990. Creighton, T.E. Biochem. J. 1990, 270, 1; Jaenicke, R. Biochemistry 1991, 30, 3147.
-
(1991)
Biochemistry
, vol.30
, pp. 3147
-
-
Jaenicke, R.1
-
5
-
-
0025373701
-
-
2. Tomalia, D.A.; Naylor, A.M.; Goddard III, W.A. Angew. Chem., Int. Ed. Engl. 1990, 29, 138; Frechet, J.M. J. Science 1994, 263, 1710. To the best of our knowledge although trifunctional amino acid monomers, for example, Lysine (Denkewalter, R.G.; Kole, J.F.; Lukasavage, W.J. U.S. Pat. 4410688, 1979; Rao, C.; Tam, J.P. J. Am. Chem. Soc. 1994, 116, 6975) and Glutamic acid (Twyman, L.J.; Beezer, A.E.; Mitchell, J.C. Tet. Lett. 1994, 35, 4423) have been used as building blocks for the construction of peptide dendrimers, there is no example in literature where these scaffoldings are supported on conformationally well-defined rigid molecular templates.
-
(1990)
Angew. Chem., Int. Ed. Engl.
, vol.29
, pp. 138
-
-
Tomalia, D.A.1
Naylor, A.M.2
Goddard W.A. III3
-
6
-
-
0028218595
-
-
2. Tomalia, D.A.; Naylor, A.M.; Goddard III, W.A. Angew. Chem., Int. Ed. Engl. 1990, 29, 138; Frechet, J.M. J. Science 1994, 263, 1710. To the best of our knowledge although trifunctional amino acid monomers, for example, Lysine (Denkewalter, R.G.; Kole, J.F.; Lukasavage, W.J. U.S. Pat. 4410688, 1979; Rao, C.; Tam, J.P. J. Am. Chem. Soc. 1994, 116, 6975) and Glutamic acid (Twyman, L.J.; Beezer, A.E.; Mitchell, J.C. Tet. Lett. 1994, 35, 4423) have been used as building blocks for the construction of peptide dendrimers, there is no example in literature where these scaffoldings are supported on conformationally well-defined rigid molecular templates.
-
(1994)
Science
, vol.263
, pp. 1710
-
-
Frechet, J.M.J.1
-
7
-
-
0025373701
-
-
W.J. U.S. Pat. 4410688, 1979
-
2. Tomalia, D.A.; Naylor, A.M.; Goddard III, W.A. Angew. Chem., Int. Ed. Engl. 1990, 29, 138; Frechet, J.M. J. Science 1994, 263, 1710. To the best of our knowledge although trifunctional amino acid monomers, for example, Lysine (Denkewalter, R.G.; Kole, J.F.; Lukasavage, W.J. U.S. Pat. 4410688, 1979; Rao, C.; Tam, J.P. J. Am. Chem. Soc. 1994, 116, 6975) and Glutamic acid (Twyman, L.J.; Beezer, A.E.; Mitchell, J.C. Tet. Lett. 1994, 35, 4423) have been used as building blocks for the construction of peptide dendrimers, there is no example in literature where these scaffoldings are supported on conformationally well-defined rigid molecular templates.
-
-
-
Denkewalter, R.G.1
Kole, J.F.2
-
8
-
-
0027947767
-
-
2. Tomalia, D.A.; Naylor, A.M.; Goddard III, W.A. Angew. Chem., Int. Ed. Engl. 1990, 29, 138; Frechet, J.M. J. Science 1994, 263, 1710. To the best of our knowledge although trifunctional amino acid monomers, for example, Lysine (Denkewalter, R.G.; Kole, J.F.; Lukasavage, W.J. U.S. Pat. 4410688, 1979; Rao, C.; Tam, J.P. J. Am. Chem. Soc. 1994, 116, 6975) and Glutamic acid (Twyman, L.J.; Beezer, A.E.; Mitchell, J.C. Tet. Lett. 1994, 35, 4423) have been used as building blocks for the construction of peptide dendrimers, there is no example in literature where these scaffoldings are supported on conformationally well-defined rigid molecular templates.
-
(1994)
J. Am. Chem. Soc.
, vol.116
, pp. 6975
-
-
Rao, C.1
Tam, J.P.2
-
9
-
-
0028290070
-
-
2. Tomalia, D.A.; Naylor, A.M.; Goddard III, W.A. Angew. Chem., Int. Ed. Engl. 1990, 29, 138; Frechet, J.M. J. Science 1994, 263, 1710. To the best of our knowledge although trifunctional amino acid monomers, for example, Lysine (Denkewalter, R.G.; Kole, J.F.; Lukasavage, W.J. U.S. Pat. 4410688, 1979; Rao, C.; Tam, J.P. J. Am. Chem. Soc. 1994, 116, 6975) and Glutamic acid (Twyman, L.J.; Beezer, A.E.; Mitchell, J.C. Tet. Lett. 1994, 35, 4423) have been used as building blocks for the construction of peptide dendrimers, there is no example in literature where these scaffoldings are supported on conformationally well-defined rigid molecular templates.
-
(1994)
Tet. Lett.
, vol.35
, pp. 4423
-
-
Twyman, L.J.1
Beezer, A.E.2
Mitchell, J.C.3
-
10
-
-
0025007175
-
-
3. Montal, M.; Montal, M.S.; Tomich, J.M. Proc. Natl. Acad. Sci. U.S.A. 1990, 87, 6929.
-
(1990)
Proc. Natl. Acad. Sci. U.S.A.
, vol.87
, pp. 6929
-
-
Montal, M.1
Montal, M.S.2
Tomich, J.M.3
-
12
-
-
0001331728
-
-
5. Tam, J.P. Proc. Natl. Acad. Sci. U.S.A. 1988, 55, 5409; Defoort, J.P.; Nardelli, B;. Huang, W.; Ho, D.; Tam, J.P. Proc. Natl. Acad. Sci. U.S.A. 1992, 89, 3879; Nardelli, B.; Lu, Y.A.; Shiu, D.R.; Dalpieire-Defoort, C.; Profy, A.T.; Tam, J.P. J. Immun. 1992, 148, 914; Tam, J.P.; Clavijo, P.; Lu, Y.A.; Nussenzweig, V.; Nussenzweig, R.; Zavala, F. J. Exp. Med. 1990, 171, 299.
-
(1988)
Proc. Natl. Acad. Sci. U.S.A.
, vol.55
, pp. 5409
-
-
Tam, J.P.1
-
13
-
-
0026582230
-
-
5. Tam, J.P. Proc. Natl. Acad. Sci. U.S.A. 1988, 55, 5409; Defoort, J.P.; Nardelli, B;. Huang, W.; Ho, D.; Tam, J.P. Proc. Natl. Acad. Sci. U.S.A. 1992, 89, 3879; Nardelli, B.; Lu, Y.A.; Shiu, D.R.; Dalpieire-Defoort, C.; Profy, A.T.; Tam, J.P. J. Immun. 1992, 148, 914; Tam, J.P.; Clavijo, P.; Lu, Y.A.; Nussenzweig, V.; Nussenzweig, R.; Zavala, F. J. Exp. Med. 1990, 171, 299.
-
(1992)
Proc. Natl. Acad. Sci. U.S.A.
, vol.89
, pp. 3879
-
-
Defoort, J.P.1
Nardelli, B.2
Huang, W.3
Ho, D.4
Tam, J.P.5
-
14
-
-
0026567741
-
-
5. Tam, J.P. Proc. Natl. Acad. Sci. U.S.A. 1988, 55, 5409; Defoort, J.P.; Nardelli, B;. Huang, W.; Ho, D.; Tam, J.P. Proc. Natl. Acad. Sci. U.S.A. 1992, 89, 3879; Nardelli, B.; Lu, Y.A.; Shiu, D.R.; Dalpieire-Defoort, C.; Profy, A.T.; Tam, J.P. J. Immun. 1992, 148, 914; Tam, J.P.; Clavijo, P.; Lu, Y.A.; Nussenzweig, V.; Nussenzweig, R.; Zavala, F. J. Exp. Med. 1990, 171, 299.
-
(1992)
J. Immun.
, vol.148
, pp. 914
-
-
Nardelli, B.1
Lu, Y.A.2
Shiu, D.R.3
Dalpieire-Defoort, C.4
Profy, A.T.5
Tam, J.P.6
-
15
-
-
0025099759
-
-
5. Tam, J.P. Proc. Natl. Acad. Sci. U.S.A. 1988, 55, 5409; Defoort, J.P.; Nardelli, B;. Huang, W.; Ho, D.; Tam, J.P. Proc. Natl. Acad. Sci. U.S.A. 1992, 89, 3879; Nardelli, B.; Lu, Y.A.; Shiu, D.R.; Dalpieire-Defoort, C.; Profy, A.T.; Tam, J.P. J. Immun. 1992, 148, 914; Tam, J.P.; Clavijo, P.; Lu, Y.A.; Nussenzweig, V.; Nussenzweig, R.; Zavala, F. J. Exp. Med. 1990, 171, 299.
-
(1990)
J. Exp. Med.
, vol.171
, pp. 299
-
-
Tam, J.P.1
Clavijo, P.2
Lu, Y.A.3
Nussenzweig, V.4
Nussenzweig, R.5
Zavala, F.6
-
16
-
-
0029840852
-
-
6. Adamantane skeleton functionalized with activated carboxylate groups at 1,3-bridge head positions appeared particularly attractive for supporting dendrons because of the anticipation that these centers would, not only provide most appropriate geometry to mimic a tetrahedral nucleus but the amide side chains carrying dendrons would, in most likelihood prefer to adopt an anti conformation (Karle, I.; Ranganathan D.; Haridas, V. J. Am. Chem. Soc. 1996, 118, 10916; Ranganathan, D.; Haridas, V.; Madhusudanan K. P.; Roy, R.; Nagaraj, R.; John, G. B.; Sukhaswami, M. B. Angew. Chem., Int. Ed. Engl. 1996, 35, 1105) particularly suitable for attaining globular conformation.
-
(1996)
J. Am. Chem. Soc.
, vol.118
, pp. 10916
-
-
Karle, I.1
Ranganathan, D.2
Haridas, V.3
-
17
-
-
0029843729
-
-
6. Adamantane skeleton functionalized with activated carboxylate groups at 1,3-bridge head positions appeared particularly attractive for supporting dendrons because of the anticipation that these centers would, not only provide most appropriate geometry to mimic a tetrahedral nucleus but the amide side chains carrying dendrons would, in most likelihood prefer to adopt an anti conformation (Karle, I.; Ranganathan D.; Haridas, V. J. Am. Chem. Soc. 1996, 118, 10916; Ranganathan, D.; Haridas, V.; Madhusudanan K. P.; Roy, R.; Nagaraj, R.; John, G. B.; Sukhaswami, M. B. Angew. Chem., Int. Ed. Engl. 1996, 35, 1105) particularly suitable for attaining globular conformation.
-
(1996)
Angew. Chem., Int. Ed. Engl.
, vol.35
, pp. 1105
-
-
Ranganathan, D.1
Haridas, V.2
Madhusudanan K, P.3
Roy, R.4
Nagaraj, R.5
John, G.B.6
Sukhaswami, M.B.7
-
18
-
-
0011429195
-
-
4, containing seven chiral centers and eight terminal carbomethoxy groups, in excellent yields. Vapour pressure osmometry experiments conducted with 4mM and 40mM solutions of hexadeca carboxylic acid (sticky solid) of 3b showed that it remains as a monomeric entity in aqueous solution
-
4, containing seven chiral centers and eight terminal carbomethoxy groups, in excellent yields. Vapour pressure osmometry experiments conducted with 4mM and 40mM solutions of hexadeca carboxylic acid (sticky solid) of 3b showed that it remains as a monomeric entity in aqueous solution.
-
-
-
-
19
-
-
0011382399
-
-
note
-
+.
-
-
-
-
20
-
-
0011475858
-
-
note
-
2O mixture as a function of time.
-
-
-
-
21
-
-
0011476996
-
-
The models for Glu scaffoldings were generated using Biosym version 2.3.5 package on a Silicon Graphics IRIS Crimson Elan Work station. The energy minimization was done with INSIGHT and DISCOVER program packages (Biosym Technologies, San Diego, CA), using CVFF force field
-
10. The models for Glu scaffoldings were generated using Biosym version 2.3.5 package on a Silicon Graphics IRIS Crimson Elan Work station. The energy minimization was done with INSIGHT and DISCOVER program packages (Biosym Technologies, San Diego, CA), using CVFF force field.
-
-
-
|