Paper alert

Folding and Design - Tập 1 - Trang R39-R43 - 1996
Lynne Regan1, Andrej Šali2, Amnon Horovitz3, Charles Wilson4
1Lynne Regan, Department of Molecular Biophysics and Biochemistry, Yale University, 266 Whitney Avenue, Box 6666, New Haven, CT 06520, USA
2Andrej Šali, Box 270, Rockefeller University, 1230 York Avenue, New York, NY 10021-6399, USA
3Amnon Horovitz, Department of Structural Biology, Weizmann Institute, IL-76100, Rehovot, Israel
4Charles Wilson, Department of Biology and Center for the Molecular Biology of RNA, University of California, Santa Cruz, CA 95064, USA

Tài liệu tham khảo

Wen, 1996, Exploring the allowed sequence space of a membrane protein, Nature Struct. Biol, 3, 141, 10.1038/nsb0296-141 Ye, 1995, Molecular recognition in the bovine immunodeficiency virus Tat peptide–TAR RNA complex, Chem. Biol, 2, 827, 10.1016/1074-5521(95)90089-6 Mollah, 1996, Core packing defects in an engineered Cro monomer corrected by combinatorial mutagenesis, Biochemistry, 35, 743, 10.1021/bi951959f Struthers, 1996, Design of a monomeric 23-residue polypeptide with defined tertiary structure, Science, 271, 342, 10.1126/science.271.5247.342 McGee, 1996, Thermodynamic cycles as probes of structure in unfolded proteins, Biochemistry, 35, 1995, 10.1021/bi951228f Mayhew, 1996, Protein folding in the central cavity of the GroEL–GroES chaperonin complex, Nature, 379, 420, 10.1038/379420a0 Martin, 1996, Coupling protein design and in vitro selection strategies: improving specificity and affinity of a designed β-protein IL-6 antagonist, J. Mol. Biol, 255, 86, 10.1006/jmbi.1996.0008 Shakhnovich, 1996, Conserved residues and the mechanism of protein folding, Nature, 379, 96, 10.1038/379096a0 Yue, 1996, Folding proteins with a simple energy function and extensive conformational searching, Protein Sci, 5, 254, 10.1002/pro.5560050209 Lathrop, 1996, Global optimum protein threading with gapped alignment and empirical pair score functions, J. Mol. Biol, 255, 641, 10.1006/jmbi.1996.0053 Hutchinson, 1996, PROMOTIF —  a program to identify and analyze structural motifs in proteins, Protein Sci, 5, 212, 10.1002/pro.5560050204 Walther, 1996, Principles of helix–helix packing in proteins: the helical lattice superposition model, J. Mol. Biol, 255, 536, 10.1006/jmbi.1996.0044 Sfatos, 1996, Simulations of chaperone-assisted folding, Biochemistry, 35, 334, 10.1021/bi952033a Mande, 1996, Structure of the heat shock protein chaperonin-10 of Mycobacterium leprae, Science, 271, 203, 10.1126/science.271.5246.203 Hunt, 1996, The crystal structure of the GroES co-chaperonin at 2.8 å resolution, Nature, 379, 37, 10.1038/379037a0 Kandror, 1995, Trigger factor is involved in GroEL-dependent protein degradation in Escherichia coli and promotes binding of GroEL to unfolded proteins, EMBO J, 14, 6021, 10.1002/j.1460-2075.1995.tb00290.x Frech, 1996, Preferential binding of an unfolded protein to DsbA, EMBO J, 15, 392, 10.1002/j.1460-2075.1996.tb00369.x Thiyagarajan, 1996, Solution structures of GroEL and its complex with rhodanese from small-angle neutron scattering, Structure, 4, 79, 10.1016/S0969-2126(96)00011-1 Szabo, 1996, A zinc finger-like domain of the molecular chaperone DnaJ is involved in binding to denatured protein substrates, EMBO J, 15, 408, 10.1002/j.1460-2075.1996.tb00371.x Weeks, 1996, Assembly of a ribonucleoprotein catalyst by tertiary structure capture, Science, 271, 345, 10.1126/science.271.5247.345 Hermann, 1995, Determination of nucleotide distances in RNA by means of copper phenanthroline-generated hydroxyl radical cleavage pattern, RNA, 1, 1009 Laughrea, 1996, Kissing-loop model of HIV-1 genome dimerization: HIV-1 RNAs can assume alternative dimeric forms, and all sequences upstream or downstream of hairpin 248–271 are dispensable for dimer formation, Biochemistry, 35, 1589, 10.1021/bi951838f Basti, 1996, Design biological activity and NMR-solution structure of a DNA analogue of yeast tRNAPhe anticodon domain, Nature Struct. Biol, 3, 38, 10.1038/nsb0196-38 Been, 1995, Optimal self-cleavage activity of the hepatitis delta virus RNA is dependent on a homopurine base pair in the ribozyme core, RNA, 1, 1061