Pages that link to "Q41778192"

The following pages link to Use of protein unfolding studies to determine the conformational and dimeric stabilities of HIV-1 and SIV proteases (Q41778192):

Displaying 41 items.

• Thermal stability of hexameric and tetrameric nucleoside diphosphate kinases. Effect of subunit interaction (Q27732846) (← links)
• Denaturant m values and heat capacity changes: relation to changes in accessible surface areas of protein unfolding (Q29620340) (← links)
• Intradimer/Intermolecular interactions suggest autoinhibition mechanism in endophilin A1 (Q30009458) (← links)
• The folding free-energy surface of HIV-1 protease: insights into the thermodynamic basis for resistance to inhibitors (Q30157397) (← links)
• Protein folding modulates the swapped dimerization mechanism of methyl-accepting chemotaxis heme sensors (Q30421855) (← links)
• Thermodynamic linkage between the binding of protons and inhibitors to HIV-1 protease (Q30480872) (← links)
• Genetic selection for dissociative inhibitors of designated protein-protein interactions (Q31801167) (← links)
• HIV protease: enzyme function and drug resistance (Q33834118) (← links)
• Slow, reversible, coupled folding and binding of the spectrin tetramerization domain (Q34314714) (← links)
• Reversible oxidative modification as a mechanism for regulating retroviral protease dimerization and activation (Q34756370) (← links)
• Human immunodeficiency virus (HIV) type 1 transframe protein can restore activity to a dimerization-deficient HIV protease variant. (Q35155106) (← links)
• Protein Folding Mechanism of the Dimeric AmphiphysinII/Bin1 N-BAR Domain (Q35774580) (← links)
• Structural features differentiate the mechanisms between 2S (2 state) and 3S (3 state) folding homodimers (Q35841435) (← links)
• Mechanism of dissociative inhibition of HIV protease and its autoprocessing from a precursor (Q36162047) (← links)
• Mechanism and evolution of protein dimerization (Q36280901) (← links)
• Drug resistance mutations can effect dimer stability of HIV-1 protease at neutral pH. (Q36281663) (← links)
• Kinetics of the dimerization of retroviral proteases: the "fireman's grip" and dimerization. (Q36631356) (← links)
• HIV-1 protease: structure, dynamics, and inhibition (Q36857092) (← links)
• Analysis and characterization of dimerization inhibition of a multi-drug-resistant human immunodeficiency virus type 1 protease using a novel size-exclusion chromatographic approach (Q37357408) (← links)
• Folding is coupled to dimerization of Tctex-1 dynein light chain. (Q39350739) (← links)
• The use of fluorescence methods to monitor unfolding transitions in proteins (Q39454755) (← links)
• Importance of the N terminus of rous sarcoma virus protease for structure and enzymatic function (Q39602769) (← links)
• A decision tree model for the prediction of homodimer folding mechanism (Q40189184) (← links)
• Conformational stability of dimeric proteins: quantitative studies by equilibrium denaturation (Q40529724) (← links)
• HIV protease as an inhibitor target for the treatment of AIDS. (Q40762915) (← links)
• Macromolecular inhibitors of HIV-1 protease. Characterization of designed heterodimers (Q41723045) (← links)
• Analysis of the stability of multimeric proteins by effective DeltaG and effective m-values (Q41838807) (← links)
• Systematic mutational analysis of the active-site threonine of HIV-1 proteinase: rethinking the "fireman's grip" hypothesis (Q42068562) (← links)
• Equilibrium dissociation and unfolding of the dimeric human papillomavirus strain-16 E2 DNA-binding domain (Q42078440) (← links)
• Design of HIV-1-PR inhibitors that do not create resistance: blocking the folding of single monomers (Q43057874) (← links)
• Revisiting monomeric HIV-1 protease. Characterization and redesign for improved properties (Q44240364) (← links)
• Metal ions modulate the folding and stability of the tumor suppressor protein S100A2. (Q46097265) (← links)
• The effect of inhibitor binding on the structural stability and cooperativity of the HIV-1 protease. (Q52209873) (← links)
• Stability of Escherichia coli single-stranded DNA binding protein (EcoSSB) (Q53012508) (← links)
• Conformational stability of the DNA-binding histone-like protein, HBsu, fromBacillus subtilis, and of the four HBsu variants [F29W], [F47W], [F50W] and [F79W] (Q57973578) (← links)
• Domain-specific spectroscopy of 5-hydroxytryptophan-containing variants of Escherichia coli DnaJ (Q59600023) (← links)
• Conformational stability and catalytic activity of HIV-1 protease are both enhanced at high salt concentration (Q71058497) (← links)
• Enhancement of HIV-1 proteinase activity by HIV-1 reverse transcriptase (Q71670085) (← links)
• Ionization states of the catalytic residues in HIV-1 protease (Q71745952) (← links)
• Rate-determining steps in HIV-1 protease catalysis. The hydrolysis of the most specific substrate (Q71833687) (← links)
• Real time NMR monitoring of local unfolding of HIV-1 protease tethered dimer driven by autolysis (Q73934665) (← links)