[go: up one dir, main page]
More Web Proxy on the site http://driver.im/

Ruzza et al., 2016 - Google Patents

Interactions of GFAP with ceftriaxone and phenytoin: SRCD and molecular docking and dynamic simulation

Ruzza et al., 2016

View HTML
Document ID
11545084324846419903
Author
Ruzza P
Vitale R
Hussain R
Biondi B
Amodeo P
Sechi G
Siligardi G
Publication year
Publication venue
Biochimica et Biophysica Acta (BBA)-General Subjects

External Links

Snippet

Background GFAP is the major intermediate filament protein in mature astrocytes. Its increased expression and aggregation was firstly associated to Alexander's disease, and successively in different neurological diseases including scrapie, Alzheimer's and Creutzfeld …
Continue reading at www.sciencedirect.com (HTML) (other versions)

Classifications

    • C—CHEMISTRY; METALLURGY
    • C07—ORGANIC CHEMISTRY
    • C07K—PEPTIDES
    • C07K14/00—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof
    • C07K14/435—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof from animals; from humans
    • C07K14/46—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof from animals; from humans from vertebrates
    • C07K14/47—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof from animals; from humans from vertebrates from mammals
    • G—PHYSICS
    • G01—MEASURING; TESTING
    • G01N—INVESTIGATING OR ANALYSING MATERIALS BY DETERMINING THEIR CHEMICAL OR PHYSICAL PROPERTIES
    • G01N33/00—Investigating or analysing materials by specific methods not covered by the preceding groups
    • G01N33/48—Investigating or analysing materials by specific methods not covered by the preceding groups biological material, e.g. blood, urine; Haemocytometers
    • G01N33/50—Chemical analysis of biological material, e.g. blood, urine; Testing involving biospecific ligand binding methods; Immunological testing
    • G01N33/68—Chemical analysis of biological material, e.g. blood, urine; Testing involving biospecific ligand binding methods; Immunological testing involving proteins, peptides or amino acids
    • G01N33/6893—Chemical analysis of biological material, e.g. blood, urine; Testing involving biospecific ligand binding methods; Immunological testing involving proteins, peptides or amino acids related to diseases not provided for elsewhere
    • G01N33/6896—Neurological disorders, e.g. Alzheimer's disease
    • A—HUMAN NECESSITIES
    • A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
    • A61K—PREPARATIONS FOR MEDICAL, DENTAL, OR TOILET PURPOSES
    • A61K31/00—Medicinal preparations containing organic active ingredients
    • A61K31/33—Heterocyclic compounds
    • A61K31/395—Heterocyclic compounds having nitrogen as a ring hetero atom, e.g. guanethidine, rifamycins

Similar Documents

Publication Publication Date Title
Ruzza et al. Interactions of GFAP with ceftriaxone and phenytoin: SRCD and molecular docking and dynamic simulation
Yu et al. Nuclear magnetic resonance structural studies of a potassium channel− charybdotoxin complex
Durany et al. Human post-mortem striatal α4β2 nicotinic acetylcholine receptor density in schizophrenia and Parkinson's syndrome
Carver et al. The interaction of the molecular chaperone α-crystallin with unfolding α-lactalbumin: a structural and kinetic spectroscopic study
Do et al. Interactions between amyloid-β and tau fragments promote aberrant aggregates: implications for amyloid toxicity
Haerd et al. Cooperativity and specificity in the interactions between DNA and the glucocorticoid receptor DNA binding domain
Moran et al. Amyloid fiber formation in human γD-crystallin induced by UV–B photodamage
Khoo et al. Structure of the analgesic μ-conotoxin KIIIA and effects on the structure and function of disulfide deletion
Kumar et al. Exploring the aggregation-prone regions from structural domains of human TDP-43
Pivato et al. Covalent α-synuclein dimers: chemico-physical and aggregation properties
Almagor et al. The role of a voltage-dependent Ca2+ channel intracellular linker: a structure-function analysis
Natalello et al. Co-fibrillogenesis of wild-type and D76N β2-microglobulin: the crucial role of fibrillar seeds
Kanchi et al. Polyproline chains destabilize the Alzheimer’s amyloid-β protofibrils: A molecular dynamics simulation study
Hoefgen et al. Heparin induced dimerization of APP is primarily mediated by E1 and regulated by its acidic domain
CA3087461A1 (en) Panda as novel therapeutic
Lubula et al. Structural insights into recognition of acetylated histone ligands by the BRPF1 bromodomain
Torres-Bugeau et al. Characterization of heparin-induced glyceraldehyde-3-phosphate dehydrogenase early amyloid-like oligomers and their implication in α-synuclein aggregation
Ghadami et al. Amyloid fibril formation by native and modified bovine β-lactoglobulins proceeds through unfolded form of proteins: A comparative study
Naik et al. Probing structurally altered and aggregated states of therapeutically relevant proteins using G roEL coupled to bio‐layer interferometry
Han et al. In vitro characterization and molecular dynamics simulation reveal mechanism of 14-3-3ζ regulated phase separation of the tau protein
Haerianardakani et al. Phenylalanine mutation to cyclohexylalanine facilitates triangular trimer formation by β-hairpins derived from Aβ
JP6660877B2 (en) Amyloid-β-binding peptide and its use for the treatment and diagnosis of Alzheimer's dementia
Gusev et al. Stabilization by a disulfide bond of the N-terminal domain of a mutant troponin C (TnC48/82).
Carrington et al. Human skeletal myopathy myosin mutations disrupt myosin head sequestration
Ray et al. A structural and functional study of Gln147 deamidation in αA-crystallin, a site of modification in human cataract