about
Modular design of redox-responsive stabilizers for nanocrystals.Peptide/protein-polymer conjugates: synthetic strategies and design concepts.Targeting of injectable drug nanocrystals.Bile acids as constituents for dental composites: in vitro cytotoxicity of (meth)acrylate and other ester derivatives of bile acids.Tracking the bioreduction of disulfide-containing cationic dendrimers.New dental composites containing multimethacrylate derivatives of bile acids: a comparative study with commercial monomers.Lipase is essential for the study of in vitro release kinetics from organogels.Twin disulfides for orthogonal disulfide pairing and the directed folding of multicyclic peptides.A new method for quantifying the intensity of the C=C band of dimethacrylate dental monomers in their FTIR and Raman spectra.Thiol-functionalized polymeric micelles: from molecular recognition to improved mucoadhesion.Sustained gastrointestinal activity of dendronized polymer-enzyme conjugates.Redox-responsive drug delivery.Complex single-chain polymer topologies locked by positionable twin disulfide cyclic bridgesPlant/Bacterial Virus-Based Drug Discovery, Drug Delivery, and Therapeutics.Releasable and traceless PEGylation of arginine-rich antimicrobial peptides.Arginine-specific modification of proteins with polyethylene glycolPEG nanocages as non-sheddable stabilizers for drug nanocrystalsCrosslinkable polymers for nanocrystal stabilizationInterplay of chemical microenvironment and redox environment on thiol-disulfide exchange kineticsBio-reduction of redox-sensitive albumin conjugates in FcRn-expressing cellsEvidence, Manipulation, and Termination of pH 'Nanobuffering' for Quantitative Homogenous Scavenging of Monoclonal AntibodiesRoom-Temperature and Selective Triggering of Supramolecular DNA Assembly/Disassembly by Nonionizing RadiationThe phage display of Bacillus subtilis Lipase A significantly enhances catalytic activity due to altered nanoscale distribution in colloidal solutionHomogenous Scavenging Resolves Low-Purification Yield/Selectivity Caused by Secondary Binding of Protein-A to Antigen-Binding Antibody FragmentsUltra-sub-stoichiometric "Dynamic" Bioconjugation Reduces Viscosity by Disrupting Immunoglobulin Oligomerization
P50
Q34966728-EE7103EB-B225-4CD6-B87A-63D646F254A2Q37184093-8314EF10-B140-4891-BC47-695898DD8B63Q38207104-481043FB-2D29-4775-8E12-80B955755590Q38619954-61219C0C-E08B-4400-8CA3-564E1FDAA1F3Q39248951-A3CE3D5C-EC0D-4011-ADE0-B4EB3FA1578BQ43113506-882B57A7-8DBE-4F50-A5BD-19ED0A1981F8Q44061329-CF60E70D-10BC-473C-ADC1-66FA67FCD0E1Q45023232-29E47AB7-C8B7-4150-9A18-A883EED62D5FQ46527994-872E8F43-BF91-4AD4-AAB1-D6951707D0ADQ46608321-51EA903D-9385-42EA-8B39-DA20E32FE15CQ50890445-C4B59D2B-337C-4C89-A261-EFE5A18EDA54Q51737530-BDE8972A-FBCD-4E38-88B5-5BB32F1A0E3CQ57752250-D2BC6F61-72FA-4006-921A-A83AA29DB373Q64882705-001C5484-65D0-45CE-878A-8C1E909E0FB6Q64883507-A4308466-BC68-4AD6-A9AC-4AD4811FBE1EQ83015937-8DA45625-8D7D-49D7-AA2E-06E485D8F0F5Q83378774-9774457E-1FC3-46CE-A778-5FB8008DD927Q83999445-D1DCD736-F64E-4E1C-951C-936DA0428B0AQ84584513-85C92492-6BA3-4941-8969-DCC31E9C2C53Q88149006-CE77C747-4766-4A63-8A05-13639B17181EQ90770085-E4DB4CB1-E628-443A-B247-4F725215A9A5Q91302732-F246E225-54DB-4190-8EE6-3ECDD2171302Q91407512-CC48A55E-B015-40A1-B473-9C1414F259C9Q92007315-0AE992B7-FB58-4515-8C5F-103E5032462BQ92522897-3755B35B-77A7-41B8-97E0-2ACE82740699
P50
description
hulumtues
@sq
researcher
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wetenschapper
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հետազոտող
@hy
name
Marc A Gauthier
@ast
Marc A Gauthier
@en
Marc A Gauthier
@es
Marc A Gauthier
@nl
Marc A Gauthier
@sl
type
label
Marc A Gauthier
@ast
Marc A Gauthier
@en
Marc A Gauthier
@es
Marc A Gauthier
@nl
Marc A Gauthier
@sl
prefLabel
Marc A Gauthier
@ast
Marc A Gauthier
@en
Marc A Gauthier
@es
Marc A Gauthier
@nl
Marc A Gauthier
@sl
P1053
B-3191-2011
P106
P108
P21
P31
P3829
P496
0000-0002-5408-6570