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Novel Natural-based Biomolecules Discovery for Tackling Chronic Diseases
Novel Natural-based Biomolecules Discovery for Tackling Chronic Diseases
Autore Kwok Hang Fai
Pubbl/distr/stampa Basel, Switzerland, : MDPI - Multidisciplinary Digital Publishing Institute, 2021
Descrizione fisica 1 electronic resource (180 p.)
Soggetto topico Humanities
Social interaction
Soggetto non controllato DAPK1
SUMO
SENP
protein degradation
post-translational modification
amphibian Bowman-Birk inhibitor
Tat peptide
molecular cloning
antifungal
drug design
protease inhibitor
natural-based compound
anticancer therapy
lung cancer
survivin
apoptosis
STAT3
colorectal cancer
orientin
cell cycle arrest
Bcl-2 family proteins
Astragalus membranaceus
insulin
PI3K
AKT
PPARγ
PDX-1
Petasites japonicus
Asteraceae
lignan
anti-inflammation
NO
PGE2
iNOS
COX-2
molecular docking
peptides
kynurenines
binding affinity
μ-opioid receptor
pharmacophore
G-protein activation
fucoidan
PLGA
docetaxel
drug delivery system
anticancer therapy/cancer treatment
hIAPP
amyloidogenesis
insulin granules
endoplasmic reticulum
anionic lipids
F23R variant
β-sheet transitions
β-cell cytotoxicity
unfolded protein response
pomegranate
punicalagin
tannins
gingiva
fibroblasts
antioxidant
wound healing
branched-chain fatty acids
Conidiobolus heterosporus
peroxisome proliferator-activated receptor α
lipid metabolism
fatty acid oxidation
hepatocyte
Formato Materiale a stampa
Livello bibliografico Monografia
Lingua di pubblicazione eng
Record Nr. UNINA-9910557607403321
Kwok Hang Fai  
Basel, Switzerland, : MDPI - Multidisciplinary Digital Publishing Institute, 2021
Materiale a stampa
Lo trovi qui: Univ. Federico II
Opac: Controlla la disponibilità qui
Recent Developments on Protein–Ligand Interactions : From Structure, Function to Applications
Recent Developments on Protein–Ligand Interactions : From Structure, Function to Applications
Autore de Brevern Alexandre G
Pubbl/distr/stampa Basel, : MDPI - Multidisciplinary Digital Publishing Institute, 2022
Descrizione fisica 1 electronic resource (282 p.)
Soggetto topico Research & information: general
Biology, life sciences
Biochemistry
Soggetto non controllato pimaricin thioesterase
protein-substrate interaction
macrocyclization
molecular dynamics (MD) simulation
pre-reaction state
folate
folate receptor
peptide conjugation
click reaction
biolayer interferometry
acetylcholinesterase
resistance
organophosphorus
pesticides
molecular modeling
lepidopterous
insects
conserved patterns
similarity
3D-patterns
epigenetics
protein-RNA interaction
RRM domain inhibitor
NMR fragment-based screening
TDP-43
galectin-1
gulopyranosides
fluorescence polarization
benzamide
selective
phospholipase C gamma 1
SLP76
virtual screening
pharmacophore mapping
molecular docking
molecular dynamics
caspase inhibition
protein-ligand binding free energy
Monte Carlo sampling
docking and scoring
molecular conformational sampling
procollagen C-proteinase enhancer-1
glycosaminoglycans
computational analysis of protein-glycosaminoglycan interactions
calcium ions
fragment-based docking
protein–ligand analysis
drug discovery and design
structure–activity relationships
bioremediation
High Energy Molecules
HMX
protein design
nitroreductase
flavoprotein
substrate specificity
pharmacophore
secretoglobin
odorant-binding protein
chemical communication
pheromone
N-phenyl-1-naphthylamine
in silico docking
protein–ligand interactions
2D interaction maps
ligand-binding assays
protein-ligand complexes
dataset
clustering
structural alignment
refinement
PD-1/PD-L1
immune checkpoint inhibitors
biphenyl-conjugated bromotyrosine
amino acid conjugation
amino-X
in silico simulation
IC50
Formato Materiale a stampa
Livello bibliografico Monografia
Lingua di pubblicazione eng
Altri titoli varianti Recent Developments on Protein–Ligand Interactions
Recent Developments on Protein–Ligand Interactions
Record Nr. UNINA-9910566462703321
de Brevern Alexandre G  
Basel, : MDPI - Multidisciplinary Digital Publishing Institute, 2022
Materiale a stampa
Lo trovi qui: Univ. Federico II
Opac: Controlla la disponibilità qui