Dehydron: a structurally encoded signal for protein interaction.
about
Rational approaches to improving selectivity in drug designWrapping effects within a proposed function-rescue strategy for the Y220C oncogenic mutation of protein p53The nonconserved wrapping of conserved protein folds reveals a trend toward increasing connectivity in proteomic networksMolecular dimension explored in evolution to promote proteomic complexityProtein binding hot spots and the residue-residue pairing preference: a water exclusion perspective.A prion-like mechanism for the propagated misfolding of SOD1 from in silico modeling of solvated near-native conformersPacking defects as selectivity switches for drug-based protein inhibitorsInhibitor design by wrapping packing defects in HIV-1 proteins.Structure and stability insights into tumour suppressor p53 evolutionary related proteins.Toxoplasma gondii Sis1-like J-domain protein is a cytosolic chaperone associated to HSP90/HSP70 complexKeeping dry and crossing membranes.A model for non-obligate oligomer formation in protein aggregration.Kinase packing defects as drug targets.Modulating drug impact by wrapping target proteins.Wrapping mimicking in drug-like small molecules disruptive of protein-protein interfaces.Parallel Structural Evolution of Mitochondrial Ribosomes and OXPHOS Complexes.A mechanism for propagated SOD1 misfolding from frustration analysis of a G85R mutant protein assembly.'Double water exclusion': a hypothesis refining the O-ring theory for the hot spots at protein interfaces.Assessing the accuracy of inhomogeneous fluid solvation theory in predicting hydration free energies of simple solutes.Tyrosine kinase inhibition: Ligand binding and conformational change in c-Kit and c-Abl.Molecular dynamics simulations to investigate the aggregation behaviors of the Abeta(17-42) oligomers.Protein packing defects "heat up" interfacial water.An in silico study of the effect of SOD1 electrostatic loop dynamics on amyloid‑like filament formation.Solvent-exposed backbone loosens the hydration shell of soluble folded proteins.Label-free protein detection using terahertz time-domain spectroscopy.Productive induced metastability in allosteric modulation of kinase function.Dehydron-Rich Proteins in the Order-Disorder Twilight ZoneEpistructural Dynamics of Biological WaterEpistructural Selectivity Filters for Molecular Targeted TherapyInterfacial Physics for Water in BiologyA unifying motif of intermolecular cooperativity in protein associationsThe integrated development of network complexity modulates the diverse evolutionary mutation rates of individual proteinsA Model for Small Heat Shock Protein Inhibition of Polyglutamine Aggregation
P2860
Q26865357-B9C98197-618F-46B1-BADE-1D34C5B5F3F7Q28485288-C4CFFD91-BF44-4746-A393-3C2ABAA7CDA5Q28776171-EA62047D-45C7-46F5-9FDC-9CCC8D233059Q30342810-51BD90FC-793F-45DF-AEA2-A6E14FAAF31BQ33576270-A0B8393D-E734-4B08-92AE-3DCBD38F0B2AQ33638268-126167B6-42BD-42EF-88E8-4CE7B76EE692Q34249752-69B00A70-0A5F-4DDA-8991-7960C44EBDEDQ34338157-9012069D-E8DD-43B0-AB01-D142ABD26EC7Q35016874-92BFA4FD-A3F1-42DB-AAF3-61E0959C6CF6Q35809558-7E37B30E-44EE-4FAE-A225-417D8DBA341EQ35876049-A4C11B79-7928-42CD-93E7-CD5BA6E9C1EEQ36042365-BE3D4EC8-9E53-429B-B006-AE99DD94B82BQ36997505-933A02BD-E3E9-474F-BC3E-73FAE510DBB5Q38089849-76E41959-8D23-4E36-AD49-A417849D61BFQ39640152-C04721B6-1FDB-40B1-B907-270D1CEBDF53Q41605683-05DAB9BF-40C0-42F5-8DBE-7A917963AD75Q41659008-3C1CD866-F0E2-4C5D-9C52-D69A2D071393Q42136717-E2BDA8E9-D583-4BA6-81AF-B4A059C90F6FQ42213043-5577B304-A371-4BDA-A2F0-6D6016AB5A2DQ43297518-4E95E662-E25D-4768-B9E8-3A2CA8CF5FFCQ45957643-EE32428A-F3F5-494C-84E1-DF66FD770C77Q50881802-09F49418-C2E8-40B0-969D-20D220C88181Q51591442-61F1A2F2-3FB1-4FB0-B2D3-61EB180D0450Q51911024-EB44D6FB-7F12-4555-9526-5A71D5E862D7Q52355091-B8D376D0-D0B9-44E6-80D8-01E7476D34ADQ54353061-91F8FAA5-7FE4-4428-A8AD-E87FFAB09D26Q56969929-C768A46F-C724-4A05-B8D4-A819BE77DE01Q56969963-87DD2901-1A8A-4F0E-B85C-77E79C946932Q56969976-BFF86D5C-8074-4B8D-8EB1-AD5AA166A5C7Q56969986-121AD265-E87D-48DA-8D74-E56594CFD761Q56970220-6755B6E4-7C20-465E-A91C-0CF980EDC598Q56970503-444ABF1D-AC7D-4F1A-B8C6-87C4D8AECDAEQ58857959-F4E54F98-16EC-4ED8-8429-4706B6825E67
P2860
Dehydron: a structurally encoded signal for protein interaction.
description
2003 nî lūn-bûn
@nan
2003 թուականի Սեպտեմբերին հրատարակուած գիտական յօդուած
@hyw
2003 թվականի սեպտեմբերին հրատարակված գիտական հոդված
@hy
2003年の論文
@ja
2003年論文
@yue
2003年論文
@zh-hant
2003年論文
@zh-hk
2003年論文
@zh-mo
2003年論文
@zh-tw
2003年论文
@wuu
name
Dehydron: a structurally encoded signal for protein interaction
@nl
Dehydron: a structurally encoded signal for protein interaction.
@ast
Dehydron: a structurally encoded signal for protein interaction.
@en
type
label
Dehydron: a structurally encoded signal for protein interaction
@nl
Dehydron: a structurally encoded signal for protein interaction.
@ast
Dehydron: a structurally encoded signal for protein interaction.
@en
prefLabel
Dehydron: a structurally encoded signal for protein interaction
@nl
Dehydron: a structurally encoded signal for protein interaction.
@ast
Dehydron: a structurally encoded signal for protein interaction.
@en
P2860
P1433
P1476
Dehydron: a structurally encoded signal for protein interaction.
@en
P2093
Ridgway Scott
P2860
P304
P356
10.1016/S0006-3495(03)74619-0
P407
P577
2003-09-01T00:00:00Z