Nothing Special   »   [go: up one dir, main page]

Maftei et al., 2012 - Google Patents

Interaction structure of the complex between neuroprotective factor humanin and Alzheimer's β‐amyloid peptide revealed by affinity mass spectrometry and molecular …

Maftei et al., 2012

Document ID
10962444908911767096
Author
Maftei M
Tian X
Manea M
Exner T
Schwanzar D
von Arnim C
Przybylski M
Publication year
Publication venue
Journal of Peptide Science

External Links

Snippet

Humanin (HN) is a linear 24‐aa peptide recently detected in human Alzheimer's disease (AD) brain. HN specifically inhibits neuronal cell death in vitro induced by ß‐amyloid (Aß) peptides and by amyloid precursor protein and its gene mutations in familial AD, thereby …
Continue reading at onlinelibrary.wiley.com (other versions)

Classifications

    • 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
    • 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
    • C07K14/4701—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof from animals; from humans from vertebrates from mammals not used
    • C07K14/4702—Regulators; Modulating activity
    • 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
    • G01N33/6803—General methods of protein analysis not limited to specific proteins or families of proteins
    • G01N33/6842—Proteomic analysis of subsets of protein mixtures with reduced complexity, e.g. membrane proteins, phosphoproteins, organelle proteins
    • 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
    • G01N33/5005—Chemical analysis of biological material, e.g. blood, urine; Testing involving biospecific ligand binding methods; Immunological testing involving human or animal cells
    • G—PHYSICS
    • G01—MEASURING; TESTING
    • G01N—INVESTIGATING OR ANALYSING MATERIALS BY DETERMINING THEIR CHEMICAL OR PHYSICAL PROPERTIES
    • G01N2800/00—Detection or diagnosis of diseases
    • G01N2800/28—Neurological disorders

Similar Documents

Publication Publication Date Title
Maftei et al. Interaction structure of the complex between neuroprotective factor humanin and Alzheimer's β‐amyloid peptide revealed by affinity mass spectrometry and molecular modeling
Limorenko et al. Revisiting the grammar of Tau aggregation and pathology formation: how new insights from brain pathology are shaping how we study and target Tauopathies
Bu et al. N-terminal acetylation preserves α-synuclein from oligomerization by blocking intermolecular hydrogen bonds
Nguyen et al. Tetrameric Aβ40 and Aβ42 β-barrel structures by extensive atomistic simulations. II. In aqueous solution
Thompson et al. IKK phosphorylates Huntingtin and targets it for degradation by the proteasome and lysosome
Burai et al. Elucidating the role of site-specific nitration of α-synuclein in the pathogenesis of Parkinson’s disease via protein semisynthesis and mutagenesis
Teplow et al. Elucidating amyloid β-protein folding and assembly: a multidisciplinary approach
Mansson et al. Conserved S/T residues of the human chaperone DNAJB6 are required for effective inhibition of Aβ42 amyloid fibril formation
Martemyanov et al. R7BP, a novel neuronal protein interacting with RGS proteins of the R7 family
Bielska et al. Hyperphosphorylation of tau induces local polyproline II helix
Scarff et al. Examination of ataxin-3 (atx-3) aggregation by structural mass spectrometry techniques: a rationale for expedited aggregation upon polyglutamine (polyQ) expansion
Wallon et al. Model for stathmin/OP18 binding to tubulin
Gill et al. Post‐translational hydroxylation at the N‐terminus of the prion protein reveals presence of PPII structure in vivo
Sinsky et al. Physiological tau interactome in brain and its link to tauopathies
Yoon et al. Comparative proteomic profiling of dystroglycan-associated proteins in wild type, mdx, and Galgt2 transgenic mouse skeletal muscle
Cruz et al. Inhibition of β‐amyloid toxicity by short peptides containing N‐methyl amino acids
Zhang et al. Phosphorylation, but not alternative splicing or proteolytic degradation, is conserved in human and mouse cardiac troponin T
Lima et al. Role of Parkinson’s disease-linked mutations and N-Terminal acetylation on the Oligomerization of α-Synuclein Induced by 3, 4-Dihydroxyphenylacetaldehyde
KR101594168B1 (en) Method for modulating autophagy mediated by p62 through ZZ domain and its use
Sargaeva et al. Differentiating N-terminal aspartic and isoaspartic acid residues in peptides
Haußmann et al. Analysis of amino-terminal variants of amyloid-β peptides by capillary isoelectric focusing immunoassay
Rani et al. Phosphorylation-induced structural reorganization in tau-paired helical filaments
Jiang et al. α-Helical motif as inhibitors of toxic amyloid-β oligomer generation via highly specific recognition of amyloid surface
Lu et al. TANGO-inspired design of anti-amyloid cyclic peptides
Lan-Mark et al. Insights into the interactions that trigger the primary nucleation of polymorphic α-synuclein dimers