Inhibiting the assembly of protein-protein interfaces.
暂无分享,去创建一个
[1] The catalytic domain of human immunodeficiency virus integrase: ordered active site in the F185H mutant , 1996, FEBS letters.
[2] M. Jaskólski,et al. Conserved folding in retroviral proteases: crystal structure of a synthetic HIV-1 protease. , 1989, Science.
[3] Thomas Rawson,et al. From Peptide to Non-Peptide. 2. The de Novo Design of Potent, Non-peptidal Inhibitors of Platelet Aggregation Based on a Benzodiazepinedione Scaffold , 1994 .
[4] Y. Nakabeppu,et al. A naturally occurring truncated form of FosB that inhibits Fos/Jun transcriptional activity , 1991, Cell.
[5] C. Heldin,et al. Dimerization of cell surface receptors in signal transduction , 1995, Cell.
[6] T. Gadek,et al. Structural studies of potent constrained RGD peptides , 1992 .
[7] J. Kahn,et al. HIV-1 protease inhibitors. A review for clinicians. , 1997 .
[8] M. Mueckler,et al. Molecular biology of receptors and transporters : receptors , 1992 .
[9] H. Hamm,et al. Arrestin-rhodopsin interaction. Multi-site binding delineated by peptide inhibition. , 1994, The Journal of biological chemistry.
[10] L. Babe,et al. Inhibition of HIV protease activity by heterodimer formation. , 1991, Biochemistry.
[11] H. Hamm,et al. The Carboxyl Terminus of the γ-Subunit of Rod cGMP Phosphodiesterase Contains Distinct Sites of Interaction with the Enzyme Catalytic Subunits and the α-Subunit of Transducin (*) , 1995, The Journal of Biological Chemistry.
[12] R. Goody,et al. Inhibition of human immunodeficiency virus type 1 reverse transcriptase dimerization using synthetic peptides derived from the connection domain. , 1994, The Journal of biological chemistry.
[13] M. Bouziane,et al. A synthetic peptide from the human immunodeficiency virus type-1 integrase exhibits coiled-coil properties and interferes with the in vitro integration activity of the enzyme. Correlated biochemical and spectroscopic results. , 1996, European journal of biochemistry.
[14] I. Brooks,et al. Specific inhibition of herpes simplex virus DNA polymerase by helical peptides corresponding to the subunit interface. , 1995, Proceedings of the National Academy of Sciences of the United States of America.
[15] D. Coen,et al. The extreme C terminus of herpes simplex virus DNA polymerase is crucial for functional interaction with processivity factor UL42 and for viral replication , 1993, Journal of virology.
[16] W Schramm,et al. The inhibition of human immunodeficiency virus proteases by 'interface peptides'. , 1996, Antiviral research.
[17] W Gibson,et al. Structure and assembly of the virion. , 1996, Intervirology.
[18] S. Jones,et al. Principles of protein-protein interactions. , 1996, Proceedings of the National Academy of Sciences of the United States of America.
[19] T. Steitz,et al. Crystal structure at 3.5 A resolution of HIV-1 reverse transcriptase complexed with an inhibitor. , 1992, Science.
[20] H. Hamm,et al. Potent Peptide Analogues of a G Protein Receptor-binding Region Obtained with a Combinatorial Library (*) , 1996, The Journal of Biological Chemistry.
[21] D. Goeddel,et al. Rational design of potent antagonists to the human growth hormone receptor. , 1992, Science.
[22] W. Stites,et al. Protein−Protein Interactions: Interface Structure, Binding Thermodynamics, and Mutational Analysis , 1997 .
[23] M. Garneau,et al. A potent peptidomimetic inhibitor of HSV ribonucleotide reductase with antiviral activity in vivo , 1994, Nature.
[24] Harold Weintraub,et al. The protein Id: A negative regulator of helix-loop-helix DNA binding proteins , 1990, Cell.
[25] R. Heinrikson,et al. Dissociative inhibition of dimeric enzymes. Kinetic characterization of the inhibition of HIV-1 protease by its COOH-terminal tetrapeptide. , 1991, The Journal of biological chemistry.
[26] Carl Frieden. Protein-protein interaction and enzymatic activity. , 1971, Annual review of biochemistry.
[27] R. Zutshi,et al. TARGETING THE DIMERIZATION INTERFACE OF HIV-1 PROTEASE: INHIBITION WITH CROSS-LINKED INTERFACIAL PEPTIDES , 1997 .
[28] Michel Bouvier,et al. A Peptide Derived from a β2-Adrenergic Receptor Transmembrane Domain Inhibits Both Receptor Dimerization and Activation* , 1996, The Journal of Biological Chemistry.
[29] I. Weber,et al. Comparative analysis of the sequences and structures of HIV‐1 and HIV‐2 proteases , 1991, Proteins.