Use of protein unfolding studies to determine the conformational and dimeric stabilities of HIV-1 and SIV proteases.
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Thermal stability of hexameric and tetrameric nucleoside diphosphate kinases. Effect of subunit interactionDenaturant m values and heat capacity changes: relation to changes in accessible surface areas of protein unfoldingIntradimer/Intermolecular interactions suggest autoinhibition mechanism in endophilin A1The folding free-energy surface of HIV-1 protease: insights into the thermodynamic basis for resistance to inhibitors.Protein folding modulates the swapped dimerization mechanism of methyl-accepting chemotaxis heme sensorsThermodynamic linkage between the binding of protons and inhibitors to HIV-1 protease.Genetic selection for dissociative inhibitors of designated protein-protein interactions.Slow, reversible, coupled folding and binding of the spectrin tetramerization domain.Reversible oxidative modification as a mechanism for regulating retroviral protease dimerization and activationHuman immunodeficiency virus (HIV) type 1 transframe protein can restore activity to a dimerization-deficient HIV protease variant.Protein Folding Mechanism of the Dimeric AmphiphysinII/Bin1 N-BAR Domain.Structural features differentiate the mechanisms between 2S (2 state) and 3S (3 state) folding homodimers.Mechanism of dissociative inhibition of HIV protease and its autoprocessing from a precursor.Mechanism and evolution of protein dimerizationDrug resistance mutations can effect dimer stability of HIV-1 protease at neutral pH.Kinetics of the dimerization of retroviral proteases: the "fireman's grip" and dimerization.Analysis and characterization of dimerization inhibition of a multi-drug-resistant human immunodeficiency virus type 1 protease using a novel size-exclusion chromatographic approachFolding is coupled to dimerization of Tctex-1 dynein light chain.The use of fluorescence methods to monitor unfolding transitions in proteins.Importance of the N terminus of rous sarcoma virus protease for structure and enzymatic function.A decision tree model for the prediction of homodimer folding mechanism.Conformational stability of dimeric proteins: quantitative studies by equilibrium denaturation.Macromolecular inhibitors of HIV-1 protease. Characterization of designed heterodimers.Analysis of the stability of multimeric proteins by effective DeltaG and effective m-valuesSystematic mutational analysis of the active-site threonine of HIV-1 proteinase: rethinking the "fireman's grip" hypothesis.Equilibrium dissociation and unfolding of the dimeric human papillomavirus strain-16 E2 DNA-binding domain.Design of HIV-1-PR inhibitors that do not create resistance: blocking the folding of single monomers.Revisiting monomeric HIV-1 protease. Characterization and redesign for improved properties.Metal ions modulate the folding and stability of the tumor suppressor protein S100A2.The effect of inhibitor binding on the structural stability and cooperativity of the HIV-1 protease.Stability of Escherichia coli single-stranded DNA binding protein (EcoSSB)Conformational stability of the DNA-binding histone-like protein, HBsu, fromBacillus subtilis, and of the four HBsu variants [F29W], [F47W], [F50W] and [F79W]
P2860
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P2860
Use of protein unfolding studies to determine the conformational and dimeric stabilities of HIV-1 and SIV proteases.
description
1992 nî lūn-bûn
@nan
1992年の論文
@ja
1992年論文
@yue
1992年論文
@zh-hant
1992年論文
@zh-hk
1992年論文
@zh-mo
1992年論文
@zh-tw
1992年论文
@wuu
1992年论文
@zh
1992年论文
@zh-cn
name
Use of protein unfolding studi ...... es of HIV-1 and SIV proteases.
@en
type
label
Use of protein unfolding studi ...... es of HIV-1 and SIV proteases.
@en
prefLabel
Use of protein unfolding studi ...... es of HIV-1 and SIV proteases.
@en
P2093
P356
P1433
P1476
Use of protein unfolding studi ...... es of HIV-1 and SIV proteases.
@en
P2093
Deckman IC
Minnich MD
P304
P356
10.1021/BI00154A023
P407
P577
1992-10-01T00:00:00Z