about
Heterodimers of nanoparticles: formation at a liquid-liquid interface and particle-specific surface modification by functional moleculesSupramolecular hydrogels inspired by collagen for tissue engineering.Use of activity-based probes to develop high throughput screening assays that can be performed in complex cell extracts.Disulfide bond as a cleavable linker for molecular self-assembly and hydrogelation.Self-assembling choline mimicks with enhanced binding affinities to C-LytA proteinExceptionally small supramolecular hydrogelators based on aromatic-aromatic interactions.Biocompatible fluorescent supramolecular nanofibrous hydrogel for long-term cell tracking and tumor imaging applicationsDesign, syntheses, and evaluation of Taspase1 inhibitorsDephosphorylation of D-peptide derivatives to form biofunctional, supramolecular nanofibers/hydrogels and their potential applications for intracellular imaging and intratumoral chemotherapy.Evaluation of alpha,beta-unsaturated ketone-based probes for papain-family cysteine proteases.Enzyme-instructed self-assembly of peptide derivatives to form nanofibers and hydrogels.Recombinant proteins as cross-linkers for hydrogelations.Using phosphatases to generate self-assembled nanostructures and their applications.Self-assembling small molecules for the detection of important analytes.Nanostructure formation-induced fluorescence turn-on for selectively detecting protein thiols in solutions, bacteria and live cells.Far-red/near-infrared fluorescence light-up probes for specific in vitro and in vivo imaging of a tumour-related proteinShort-peptide-based molecular hydrogels: novel gelation strategies and applications for tissue engineering and drug delivery.Gd(III)-induced Supramolecular Hydrogelation with Enhanced Magnetic Resonance Performance for Enzyme Detection.A Glycyrrhetinic Acid-Modified Curcumin Supramolecular Hydrogel for liver tumor targeting therapy.Cooperative self-assembly of peptide gelators and proteins.Spatiotemporal Control of Supramolecular Self-Assembly and Function.Enzyme-controllable F-NMR turn on through disassembly of peptide-based nanospheres for enzyme detection.A saccharide-based supramolecular hydrogel for cell culture.Peptide-Induced AIEgen Self-Assembly: A New Strategy to Realize Highly Sensitive Fluorescent Light-Up Probes.Multifunctional biohybrid hydrogels for cell culture and controlled drug release.Glutathione-triggered formation of molecular hydrogels for 3D cell culture.Surface-induced hydrogelation inhibits platelet aggregation.Integrating Enzymatic Self-Assembly and Mitochondria Targeting for Selectively Killing Cancer Cells without Acquired Drug Resistance.A hybrid hydrogel for efficient removal of methyl violet from aqueous solutions.Synthetic studies on nonthrombogenic biomaterials 14: synthesis and characterization of poly(ether-urethane) bearing a Zwitterionic structure of phosphorylcholine on the surface.Small molecule hydrogels based on a class of antiinflammatory agents.Molecular recognition remolds the self-assembly of hydrogelators and increases the elasticity of the hydrogel by 10(6)-fold.Enzyme promotes the hydrogelation from a hydrophobic small molecule.Using a kinase/phosphatase switch to regulate a supramolecular hydrogel and forming the supramolecular hydrogel in vivo.Kinetic control over supramolecular hydrogelation and anticancer properties of taxol.Cancer vaccines using supramolecular hydrogels of NSAID-modified peptides as adjuvants abolish tumorigenesis.Supramolecular "Trojan Horse" for Nuclear Delivery of Dual Anticancer Drugs.Tandem Molecular Self-Assembly in Liver Cancer Cells.Supramolecular nanofibers of self-assembling peptides and proteins for protein delivery.Self-assembly-induced far-red/near-infrared fluorescence light-up for detecting and visualizing specific protein-Peptide interactions.
P50
Q28301024-FF42618C-DA95-40A9-B6FB-599920493A83Q33587679-8A5A08E6-73AA-4AFA-B863-962A3D82F980Q33654142-737830B6-010B-48A3-B608-4ED2494E129FQ33756368-44FBAEFF-7E2F-4ADC-9A4E-6E8A6FB5B68CQ34340896-81C9B7CC-5CDD-4018-9BB4-961376759AEAQ34712029-E717B5B4-A9D8-497E-98A8-57AE42B88F23Q36287316-A903F5EA-5295-4EE7-8394-21823F3536DBQ36442063-1FCAB1A7-41EC-4F21-87D8-30D3C9E16B10Q37061570-FE4CEC4E-C0E4-444C-869E-C97C539314D9Q37137274-564DD8E2-7C61-4324-B89D-62EC6D4DB697Q37679108-4E8E4CA4-E4C5-4636-926E-A49A2CB4E205Q38061361-E33B23B0-7970-441F-9084-FFB777EB4646Q38158090-75030144-6647-435F-BFD7-CAB8C422EBE4Q38233798-C906DEE3-C584-47C9-9325-75F81BE644FAQ38866558-03C09359-F277-4F44-B372-F953E8A65C35Q39063834-28326C08-CA38-47D0-A3A3-870140A6DA09Q39583024-68145C49-E660-45ED-A421-748EA3AE4B94Q41196370-E2E81552-8F11-4C38-9D45-9518B52CA0ABQ41890555-AD5CA595-7121-49EC-AE35-EF96737B5DD9Q42690861-F7847C1E-8DD4-463C-B606-764974D86172Q42802405-6655C674-247A-4DDF-AFB8-461C68184770Q42807651-733C9CC4-A161-449C-A185-A4CF1E5A3158Q42811977-DA4F6737-4460-4378-8612-ED797C0CB072Q42813263-88921EF5-3202-4084-A3A6-C562042FEDB1Q42816412-E9E2FEBF-4BEF-4A52-BF77-569CEF7ECDC9Q42823136-EFD2004E-FCCD-4397-AD12-8A8C16C4502EQ42827895-A5D3E8FF-A7FA-4BF8-8624-24F398B0C3AEQ43237773-DB61D7CC-B864-4B90-AA68-67B1BDF7C511Q43318877-5F041EA1-E610-4EB5-B885-BF58DC3D7D1BQ44539890-164F8449-C86B-4A9B-AED9-4072409AF96DQ44737776-C948E3A9-6DEA-43B5-8474-572EF6BA1749Q45153082-B38B838E-1249-4184-A180-F6F4D76504E7Q45204927-5700CD41-66F4-4E84-A822-50FDB3BAA7C4Q46967689-7E4A8461-DC7C-4989-BBB7-63228F8320C2Q47195271-BD97FB70-6B68-4786-8DE1-6111B844DE57Q47685811-6CD8CC5E-4074-4241-9686-CE69497ECEA2Q48247685-FD557243-8186-4A9B-82A8-A09CFEEC0591Q48350583-1906C637-A8EC-45DA-944A-9253D5B662E6Q50249422-3B9EA56E-9AC0-4EF7-B990-9CC7C1DB8D46Q50481072-D52CB4E9-04EC-4234-9022-630A81009A39
P50
description
onderzoeker
@nl
researcher ORCID ID = 0000-0003-2967-6920
@en
name
Zhimou Yang
@ast
Zhimou Yang
@en
Zhimou Yang
@es
Zhimou Yang
@nl
type
label
Zhimou Yang
@ast
Zhimou Yang
@en
Zhimou Yang
@es
Zhimou Yang
@nl
prefLabel
Zhimou Yang
@ast
Zhimou Yang
@en
Zhimou Yang
@es
Zhimou Yang
@nl
P106
P31
P496
0000-0003-2967-6920