Proximity versus allostery: the role of regulated protein dimerization in biology
- 30 November 1994
- journal article
- review article
- Published by Elsevier in Chemistry & Biology
- Vol. 1 (3) , 131-136
- https://doi.org/10.1016/1074-5521(94)90002-7
Abstract
No abstract availableKeywords
This publication has 19 references indexed in Scilit:
- Membrane targeting of the nucleotide exchange factor Sos is sufficient for activating the Ras signaling pathwayCell, 1994
- SH2 and SH3 domainsCurrent Biology, 1993
- Binding of a high affinity phosphotyrosyl peptide to the Src SH2 domain: Crystal structures of the complexed and peptide-free formsCell, 1993
- Crystal Structure at 3.5 Å Resolution of HIV-1 Reverse Transcriptase Complexed with an InhibitorScience, 1992
- An energy‐based approach to packing the 7‐helix bundle of bacteriorhodopsinProtein Science, 1992
- Human Growth Hormone and Extracellular Domain of Its Receptor: Crystal Structure of the ComplexScience, 1992
- Dimerization of the Extracellular Domain of the Human Growth Hormone Receptor by a Single Hormone MoleculeScience, 1991
- Inhibition of HIV-1 Replication by a Nonnucleoside Reverse Transcriptase InhibitorScience, 1990
- Crystal structure of trp represser/operator complex at atomic resolutionNature, 1988
- The crystal structure of trp aporepressor at 1.8 Å shows how binding tryptophan enhances DNA affinityNature, 1987