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

Mierke et al., 1996 - Google Patents

Peptide mimetic of the third cytoplasmic loop of the PTH/PTHrP receptor

Mierke et al., 1996

Document ID
8459640553502606648
Author
Mierke D
Royo M
Pellegrini M
Sun H
Chorev M
Publication year
Publication venue
Journal of the American Chemical Society

External Links

Snippet

The third cytoplasmic loop of seven transmembrane helix receptors is important both for the coupling to and activation of the heterotrimeric G-protein. Here, the structural characterization of two peptides containing the sequence of the putative third cytoplasmic …
Continue reading at pubs.acs.org (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
    • C07K14/705—Receptors; Cell surface antigens; Cell surface determinants
    • C07K14/72—Receptors; Cell surface antigens; Cell surface determinants for hormones
    • 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
    • C07K14/705—Receptors; Cell surface antigens; Cell surface determinants
    • C07K14/70571—Receptors; Cell surface antigens; Cell surface determinants for neuromediators, e.g. serotonin receptor, dopamine receptor
    • 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
    • G01N33/6872—Intracellular protein regulatory factors and their receptors, e.g. including ion channels
    • 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
    • G01N33/5008—Chemical analysis of biological material, e.g. blood, urine; Testing involving biospecific ligand binding methods; Immunological testing involving human or animal cells for testing or evaluating the effect of chemical or biological compounds, e.g. drugs, cosmetics
    • G01N33/502—Chemical analysis of biological material, e.g. blood, urine; Testing involving biospecific ligand binding methods; Immunological testing involving human or animal cells for testing or evaluating the effect of chemical or biological compounds, e.g. drugs, cosmetics for testing non-proliferative effects
    • 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
    • C07K14/705—Receptors; Cell surface antigens; Cell surface determinants
    • C07K14/70503—Immunoglobulin superfamily
    • 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
    • G01N33/53—Immunoassay; Biospecific binding assay
    • 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
    • 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
    • C07K14/575—Hormones
    • G—PHYSICS
    • G01—MEASURING; TESTING
    • G01N—INVESTIGATING OR ANALYSING MATERIALS BY DETERMINING THEIR CHEMICAL OR PHYSICAL PROPERTIES
    • G01N2333/00—Assays involving biological materials from specific organisms or of a specific nature
    • G01N2333/435—Assays involving biological materials from specific organisms or of a specific nature from animals; from humans
    • G01N2333/705—Assays involving receptors, cell surface antigens or cell surface determinants
    • G01N2333/72—Assays involving receptors, cell surface antigens or cell surface determinants for hormones
    • G01N2333/726—G protein coupled receptor, e.g. TSHR-thyrotropin-receptor, LH/hCG receptor, FSH
    • G—PHYSICS
    • G01—MEASURING; TESTING
    • G01N—INVESTIGATING OR ANALYSING MATERIALS BY DETERMINING THEIR CHEMICAL OR PHYSICAL PROPERTIES
    • G01N2500/00—Screening for compounds of potential therapeutic value

Similar Documents

Publication Publication Date Title
Culhane et al. Transmembrane signal transduction by peptide hormones via family BG protein-coupled receptors
Kostenis et al. Molecular basis of receptor/G protein coupling selectivity studied by coexpression of wild type and mutant m2 muscarinic receptors with mutant Gαq subunits
Altenbach et al. Structure and function in rhodopsin: Mapping light-dependent changes in distance between residue 65 in helix TM1 and residues in the sequence 306− 319 at the cytoplasmic end of helix TM7 and in helix H8
Paterlini et al. Molecular simulation of dynorphin A-(1− 10) binding to extracellular loop 2 of the κ-opioid receptor. A model for receptor activation
Oxenoid et al. NMR assignments for a helical 40 kDa membrane protein
Piserchio et al. Characterization of parathyroid hormone/receptor interactions: structure of the first extracellular loop
Hoare et al. Evaluating the signal transduction mechanism of the parathyroid hormone 1 receptor: effect of receptor-G-protein interaction on the ligand binding mechanism and receptor conformation
Pellegrini et al. Binding domain of human parathyroid hormone receptor: from conformation to function
Kostenis et al. Genetic analysis of receptor-Gαq coupling selectivity
Rölz et al. Molecular characterization of the receptor− ligand complex for parathyroid hormone
Mierke et al. Peptide mimetic of the third cytoplasmic loop of the PTH/PTHrP receptor
Bayrhuber et al. Nuclear magnetic resonance solution structure and functional behavior of the human proton channel
Lee et al. Structural dynamics and thermostabilization of neurotensin receptor 1
Simms et al. Photoaffinity cross-linking and unnatural amino acid mutagenesis reveal insights into calcitonin gene-related peptide binding to the calcitonin receptor-like receptor/receptor activity-modifying protein 1 (CLR/RAMP1) complex
Liu et al. A structure-based approach to understanding somatostatin receptor-4 agonism (sst4)
Chai et al. Receptor− Antagonist Interactions in the Complexes of Agouti and Agouti-Related Protein with Human Melanocortin 1 and 4 Receptors
Singh et al. Activation of corticotropin-releasing factor 1 receptor: insights from molecular dynamics simulations
Cong et al. Activation dynamics of the neurotensin G protein-coupled receptor 1
Kim et al. Identification of specific transmembrane residues and ligand-induced interface changes involved in homo-dimer formation of a yeast G protein-coupled receptor
Lee et al. Dynamic behavior of the active and inactive states of the adenosine A2A receptor
Chung et al. NMR structure of the second intracellular loop of the α2A adrenergic receptor: evidence for a novel cytoplasmic helix
Uba et al. Activation mechanism of corticotrophin releasing factor receptor type 1 elucidated using molecular dynamics simulations
Ward et al. Use of an in situ disulfide cross-linking strategy to study the dynamic properties of the cytoplasmic end of transmembrane domain VI of the M3 muscarinic acetylcholine receptor
Xie et al. Preparation of an activated rhodopsin/transducin complex using a constitutively active mutant of rhodopsin
Xu et al. The conserved cysteine 7.38 residue is differentially accessible in the binding-site crevices of the μ, δ, and κ opioid receptors