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2
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0033621158
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Protein synthesis by native chemical ligation: Expanded scope by using straightforward methodology
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Hackeng T.M., Griffin J.H., Dawson P.E. Protein synthesis by native chemical ligation: expanded scope by using straightforward methodology. Proc Natl Acad Sci USA. 96:1999;10068-10073.
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Proc Natl Acad Sci USA
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Hackeng, T.M.1
Griffin, J.H.2
Dawson, P.E.3
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3
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0005464510
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Native chemical ligation of polypeptides
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Camarero J.A., Muir T.W. Native chemical ligation of polypeptides. Curr Prot Prot Sci. 18.4:1999;1-21.
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Curr Prot Prot Sci
, vol.184
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Camarero, J.A.1
Muir, T.W.2
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4
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0030973396
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Modulation of reactivity in native chemical ligation through the use of thiol additives
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Dawson P.E., Churchill M., Ghadiri M.R., Kent S.B.H. Modulation of reactivity in native chemical ligation through the use of thiol additives. J Am Chem Soc. 119:1997;4325-4329.
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Dawson, P.E.1
Churchill, M.2
Ghadiri, M.R.3
Kent, S.B.H.4
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5
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0030711495
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Protein synthesis by chemical ligation of unprotected peptides in aqueous solution
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Muir T.W., Dawson P.E., Kent S.B.H. Protein synthesis by chemical ligation of unprotected peptides in aqueous solution. Methods Enzymol. 289:1997;266-298.
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Methods Enzymol
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Muir, T.W.1
Dawson, P.E.2
Kent, S.B.H.3
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7
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0028810342
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Chemical ligation of cysteine-containing peptides: Synthesis of a 22 kDa tethered dimer of HIV-1 protease
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Baca M., Muir T.W., Schnölzer M., Kent S.B.H. Chemical ligation of cysteine-containing peptides: synthesis of a 22 kDa tethered dimer of HIV-1 protease. J Am Chem Soc. 117:1995;1881-1887.
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(1995)
J Am Chem Soc
, vol.117
, pp. 1881-1887
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Baca, M.1
Muir, T.W.2
Schnölzer, M.3
Kent, S.B.H.4
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8
-
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0029140496
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Total chemical synthesis of a unique transcription factor-related protein: cMyc-Max
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Canne L.E., Ferré-D'Amaré A.R., Burley S.K., Kent S.B.H.Total chemical synthesis of a unique transcription factor-related protein: cMyc-Max J Am Chem Soc. 117:1995;2998-3007.
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(1995)
J Am Chem Soc
, vol.117
, pp. 2998-3007
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Canne, L.E.1
Ferré-D'Amaré, A.R.2
Burley, S.K.3
Kent, S.B.H.4
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9
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0033615313
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Chemical protein synthesis by solid phase ligation of unprotected peptide segments
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Taking advantage of modern solid-phase chemistry technology, the authors significantly increased the accessible range of chemically synthetic proteins by performing multiple native chemical ligations onto a resin-bound peptide
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Canne L.E., Botti P., Simon R.J., Chen Y., Dennis E.A., Kent S.B.H. Chemical protein synthesis by solid phase ligation of unprotected peptide segments. J Am Chem Soc. 121:1999;8720-8727. Taking advantage of modern solid-phase chemistry technology, the authors significantly increased the accessible range of chemically synthetic proteins by performing multiple native chemical ligations onto a resin-bound peptide.
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(1999)
J Am Chem Soc
, vol.121
, pp. 8720-8727
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-
Canne, L.E.1
Botti, P.2
Simon, R.J.3
Chen, Y.4
Dennis, E.A.5
Kent, S.B.H.6
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10
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0344351815
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Semisynthesis of cytotoxic proteins using a modified protein splicing element
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Evans T.C., Benner J., Xu M.Q. Semisynthesis of cytotoxic proteins using a modified protein splicing element. Protein Sci. 11:1998;2256-2264.
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Protein Sci
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, pp. 2256-2264
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Evans, T.C.1
Benner, J.2
Xu, M.Q.3
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11
-
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0032499752
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Expressed protein ligation: A general method for protein engineering
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This paper describes the application of expressed protein ligation for the incorporation of a labeled carboxy-terminal peptide into an ~600 residue protein. This demonstrates the application of a new technology to a biologically relevant problem
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Muir T.W., Sondhi D., Cole P.A. Expressed protein ligation: a general method for protein engineering. Proc Natl Acad Sci USA. 95:1998;6705-6710. This paper describes the application of expressed protein ligation for the incorporation of a labeled carboxy-terminal peptide into an ~600 residue protein. This demonstrates the application of a new technology to a biologically relevant problem.
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(1998)
Proc Natl Acad Sci USA
, vol.95
, pp. 6705-6710
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Muir, T.W.1
Sondhi, D.2
Cole, P.A.3
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12
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0032568924
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Expressed protein ligation, a novel method for studying protein-protein interactions in transcription
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Severinov K., Muir T.W. Expressed protein ligation, a novel method for studying protein-protein interactions in transcription. J Biol Chem. 273:1998;16205-16209.
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(1998)
J Biol Chem
, vol.273
, pp. 16205-16209
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Severinov, K.1
Muir, T.W.2
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13
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0039374819
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The in vitro ligation of bacterially expressed proteins using an intein from Methanobacterium thermoautotrophicum
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Evans T., Benner J., Xu M. The in vitro ligation of bacterially expressed proteins using an intein from Methanobacterium thermoautotrophicum. J Biol Chem. 274:1999;3923-3926.
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J Biol Chem
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, pp. 3923-3926
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Evans, T.1
Benner, J.2
Xu, M.3
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14
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0033582287
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Chemical ligation of folded recombinant proteins: Segmental isotopic labeling of domains for NMR studies
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15N-labeled. A neat approach to the study of protein domains in the context of larger multidomain complexes by NMR
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15N-labeled. A neat approach to the study of protein domains in the context of larger multidomain complexes by NMR.
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(1999)
Proc Natl Acad Sci USA
, vol.96
, pp. 388-393
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Xu, R.1
Ayers, B.2
Cowburn, D.3
Muir, T.W.4
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15
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0033540665
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Insertion of a synthetic peptide into a recombinant protein framework: A protein biosensor
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Cotton G.J., Ayers B., Xu R., Muir T.W. Insertion of a synthetic peptide into a recombinant protein framework: a protein biosensor. J Am Chem Soc. 121:1999;1100-1101.
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(1999)
J Am Chem Soc
, vol.121
, pp. 1100-1101
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Cotton, G.J.1
Ayers, B.2
Xu, R.3
Muir, T.W.4
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16
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0030482408
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The leucine zipper domain controls the orientation of AP-1 in the NFAT.AP-1.DNA complex
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Erlanson D.A., Chytil M., Verdine G.L. The leucine zipper domain controls the orientation of AP-1 in the NFAT.AP-1.DNA complex. Chem Biol. 3:1996;981-991.
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Chem Biol
, vol.3
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Erlanson, D.A.1
Chytil, M.2
Verdine, G.L.3
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17
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0033532889
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Conformationally assisted protein ligation using C-terminal thioester peptides
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Performing chemical ligation under folding conditions, the authors observed a significant increase in the rate of ligation. This technique also shows potential in overcoming some of the sequence dependence of native chemical ligation
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Beligere G., Dawson P.E. Conformationally assisted protein ligation using C-terminal thioester peptides. J Am Chem Soc. 121:1999;6332-6333. Performing chemical ligation under folding conditions, the authors observed a significant increase in the rate of ligation. This technique also shows potential in overcoming some of the sequence dependence of native chemical ligation.
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(1999)
J Am Chem Soc
, vol.121
, pp. 6332-6333
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Beligere, G.1
Dawson, P.E.2
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18
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0029102380
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Peptide ligation and semisynthesis
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Wallace C.J. Peptide ligation and semisynthesis. Curr Opin Biotechnol. 6:1995;403-410.
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Curr Opin Biotechnol
, vol.6
, pp. 403-410
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Wallace, C.J.1
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20
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0032951699
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NMR structure of a minimized human agouti related protein prepared by total chemical synthesis
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Bolin K.A., Anderson D.J., Trulson J.A., Thompson D.A., Wilken J., Kent S.B.H., Gantz I., Millhauser G.L. NMR structure of a minimized human agouti related protein prepared by total chemical synthesis. FEBS Lett. 451:1999;125-131.
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FEBS Lett
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, pp. 125-131
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Bolin, K.A.1
Anderson, D.J.2
Trulson, J.A.3
Thompson, D.A.4
Wilken, J.5
Kent, S.B.H.6
Gantz, I.7
Millhauser, G.L.8
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21
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0030759182
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Chemically synthesized SDF-1alpha analogue, N33A, is a potent chemotactic agent for CXCR4/Fusin/LESTR-expressing human leukocytes
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Ueda H., Siani M.A., Gong W., Thompson D.A., Brown G.G., Wang J.M. Chemically synthesized SDF-1alpha analogue, N33A, is a potent chemotactic agent for CXCR4/Fusin/LESTR-expressing human leukocytes. J Biol Chem. 272:1997;24966-24970.
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J Biol Chem
, vol.272
, pp. 24966-24970
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Ueda, H.1
Siani, M.A.2
Gong, W.3
Thompson, D.A.4
Brown, G.G.5
Wang, J.M.6
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22
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0032499791
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Crystal structure of chemically synthesized [N33A] stromal cell-derived factor 1alpha, a potent ligand for the HIV-1 fusin coreceptor
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Dealwis C., Fernandez E.J., Thompson D.A., Simon R.J., Siani M.A., Lolis E. Crystal structure of chemically synthesized [N33A] stromal cell-derived factor 1alpha, a potent ligand for the HIV-1 fusin coreceptor. Proc Natl Acad Sci USA. 95:1998;6941-6946.
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(1998)
Proc Natl Acad Sci USA
, vol.95
, pp. 6941-6946
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Dealwis, C.1
Fernandez, E.J.2
Thompson, D.A.3
Simon, R.J.4
Siani, M.A.5
Lolis, E.6
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23
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0032422921
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Accessibility of selenomethionine proteins by total chemical synthesis: Structural studies of human herpesvirus-8 MIP-II
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Shao W., Fernandez E., Wilken J., Thompson D.A., Siani M.A., West J., Lolis E., Schweitzer B.I. Accessibility of selenomethionine proteins by total chemical synthesis: structural studies of human herpesvirus-8 MIP-II. FEBS Lett. 441:1998;77-82.
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(1998)
FEBS Lett
, vol.441
, pp. 77-82
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Shao, W.1
Fernandez, E.2
Wilken, J.3
Thompson, D.A.4
Siani, M.A.5
West, J.6
Lolis, E.7
Schweitzer, B.I.8
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24
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0030951442
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Potent inhibition of HIV-1 infectivity in macrophages and lymphocytes by a novel CCR5 antagonist
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Simmons G., Clapham P.R., Picard L., Offord R.E., Rosenkilde M.M., Schwartz T.W., Buser R., Wells T.N.C., Proudfoot A.E. Potent inhibition of HIV-1 infectivity in macrophages and lymphocytes by a novel CCR5 antagonist. Science. 276:1997;276-279.
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Science
, vol.276
, pp. 276-279
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Simmons, G.1
Clapham, P.R.2
Picard, L.3
Offord, R.E.4
Rosenkilde, M.M.5
Schwartz, T.W.6
Buser, R.7
Wells, T.N.C.8
Proudfoot, A.E.9
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25
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0032782574
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Total chemical synthesis and high-resolution crystal structure of the potent anti-HIV protein AOP-RANTES
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Wilken J., Hoover D., Thompson D.A., Barlow P.N., McSparron H., Picard L., Wlodawer A., Lubkowski J., Kent S.B.H. Total chemical synthesis and high-resolution crystal structure of the potent anti-HIV protein AOP-RANTES. Chem Biol. 6:1999;43-51.
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(1999)
Chem Biol
, vol.6
, pp. 43-51
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-
Wilken, J.1
Hoover, D.2
Thompson, D.A.3
Barlow, P.N.4
McSparron, H.5
Picard, L.6
Wlodawer, A.7
Lubkowski, J.8
Kent, S.B.H.9
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26
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0033554426
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Total chemical synthesis of the integral membrane protein influenza A virus M2: Role of its C-terminal domain in tetramer assembly
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The total chemical synthesis of an integral membrane protein, the influenza A M2 proton channel, is reported. This is currently the most rapid way to get access to large quantities of small membrane proteins. Structure/function studies relating to the oligomerization state were carried out
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Kochendoerfer G.G., Salom D., Lear J.D., Wilk-Orescan R., Kent S.B.H., DeGrado W.F. Total chemical synthesis of the integral membrane protein influenza A virus M2: role of its C-terminal domain in tetramer assembly. Biochemistry. 38:1999;11905-11913. The total chemical synthesis of an integral membrane protein, the influenza A M2 proton channel, is reported. This is currently the most rapid way to get access to large quantities of small membrane proteins. Structure/function studies relating to the oligomerization state were carried out.
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(1999)
Biochemistry
, vol.38
, pp. 11905-11913
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Kochendoerfer, G.G.1
Salom, D.2
Lear, J.D.3
Wilk-Orescan, R.4
Kent, S.B.H.5
Degrado, W.F.6
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27
-
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0033168207
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Probing intermolecular backbone H-bonding in serine proteinase-protein inhibitor complexes
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The use of protein 'backbone engineering' by chemical protein synthesis to systematically dissect the role of hydrogen bonds in protein-protein interactions is described. This is ture 'molecular' biology: protein structure analysis bond by bond
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Lu W., Randal M., Kossiakoff A., Kent S.B.H. Probing intermolecular backbone H-bonding in serine proteinase-protein inhibitor complexes. Chem Biol. 6:1999;419-427. The use of protein 'backbone engineering' by chemical protein synthesis to systematically dissect the role of hydrogen bonds in protein-protein interactions is described. This is ture 'molecular' biology: protein structure analysis bond by bond.
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(1999)
Chem Biol
, vol.6
, pp. 419-427
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Lu, W.1
Randal, M.2
Kossiakoff, A.3
Kent, S.B.H.4
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28
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0032573867
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Design, synthesis, and properties of a novel cytochrome b model
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Rau H.K., Haehnel W. Design, synthesis, and properties of a novel cytochrome b model. J Am Chem Soc. 120:1998;468-476.
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(1998)
J Am Chem Soc
, vol.120
, pp. 468-476
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Rau, H.K.1
Haehnel, W.2
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29
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0033554037
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Integration of a reconstituted de novo synthesized hemoprotein and native metalloproteins with electrode supports for bioelectronic and bioelectrocatalytic applications
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A clever application of TASP (template-assembled synthetic protein) to the design of a directional electron transfer device that transfers electrons from an electrode to a redox protein. A great example of how chemical protein synthesis provides access to novel biomaterials
-
Willner I., Heleg-Shabtai V., Katz E., Rau H., Haehnel W. Integration of a reconstituted de novo synthesized hemoprotein and native metalloproteins with electrode supports for bioelectronic and bioelectrocatalytic applications. J Am Chem Soc. 121:1999;6455-6468. A clever application of TASP (template-assembled synthetic protein) to the design of a directional electron transfer device that transfers electrons from an electrode to a redox protein. A great example of how chemical protein synthesis provides access to novel biomaterials.
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(1999)
J Am Chem Soc
, vol.121
, pp. 6455-6468
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Willner, I.1
Heleg-Shabtai, V.2
Katz, E.3
Rau, H.4
Haehnel, W.5
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30
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0032578392
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Modular synthesis of de novo-designed metalloproteins for light-induced electron transfer
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Rau H.K., DeJonge N., Haehnel W. Modular synthesis of de novo-designed metalloproteins for light-induced electron transfer. Proc Natl Acad Sci USA. 95:1998;11526-11531.
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(1998)
Proc Natl Acad Sci USA
, vol.95
, pp. 11526-11531
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Rau, H.K.1
Dejonge, N.2
Haehnel, W.3
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31
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0032508968
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Rational fine-tuning of the redox potentials in chemically synthesized rubredoxins
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The systematic variation of a single conserved tyrosine residue close to the redox center of rubredoxin by non-native amino acid replacement reveals the importance of this residue in the molecular mechanism of redox tuning
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Low D.W., Hill M.G. Rational fine-tuning of the redox potentials in chemically synthesized rubredoxins. J Am Chem Soc. 120:1998;11536-11537. The systematic variation of a single conserved tyrosine residue close to the redox center of rubredoxin by non-native amino acid replacement reveals the importance of this residue in the molecular mechanism of redox tuning.
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(1998)
J Am Chem Soc
, vol.120
, pp. 11536-11537
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Low, D.W.1
Hill, M.G.2
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32
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0033529274
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Design, total chemical synthesis, and binding properties of a [Leu-91-N1-methyl-7-azaTrp]Ras-binding domain of c-Raf-1
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Sydor J.R., Herrmann C., Kent S.B.H., Goody R.S., Engelhard M. Design, total chemical synthesis, and binding properties of a [Leu-91-N1-methyl-7-azaTrp]Ras-binding domain of c-Raf-1. Proc Natl Acad Sci USA. 96:1999;7865-7870.
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(1999)
Proc Natl Acad Sci USA
, vol.96
, pp. 7865-7870
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Sydor, J.R.1
Herrmann, C.2
Kent, S.B.H.3
Goody, R.S.4
Engelhard, M.5
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34
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0031932170
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Favorable domain size in proteins
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Xu D., Nussinov R. Favorable domain size in proteins. Fold Des. 27:1997;11-17.
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Fold des
, vol.27
, pp. 11-17
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Xu, D.1
Nussinov, R.2
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