Solution structure of pituitary adenylate cyclase activating polypeptide by nuclear magnetic resonance spectroscopy

Solution structure of pituitary adenylate cyclase activating polypeptide by nuclear magnetic resonance spectroscopy

Item
http://www.wikidata.org/entity/Q28269661
Identification of key residues for interaction of vasoactive intestinal peptide with human VPAC1 and VPAC2 receptors and development of a highly selective VPAC1 receptor agonist. Alanine scanning and molecular modeling of the peptideFunctional anthology of intrinsic disorder. 1. Biological processes and functions of proteins with long disordered regions.Solution structure of microcin J25, the single macrocyclic antimicrobial peptide from Escherichia coli.Assessment by 1H NMR spectroscopy of the structural behaviour of human parathyroid-hormone-related protein(1-34) and its close relationship with the N-terminal fragments of human parathyroid hormone in solution.Novel alternatively spliced exon in the extracellular ligand-binding domain of the pituitary adenylate cyclase-activating polypeptide (PACAP) type 1 receptor (PAC1R) selectively increases ligand affinity and alters signal transduction coupling durinDesign and syntheses of peptides which induce or enhance structural changes of recombinant bovine prion protein (rbPrP) and discovery of peptides from bovine brain which accelerate structural conversions of rbPrP.Characterization of a new lipopeptide surfactant produced by thermotolerant and halotolerant subsurface Bacillus licheniformis BAS50Targeting VIP and PACAP receptor signalling: new therapeutic strategies in multiple sclerosis.A structure-function study of PACAP using conformationally restricted analogs: Identification of PAC1 receptor-selective PACAP agonistsStructural aspects of gut peptides with therapeutic potential for type 2 diabetes.Functional characterization of structural alterations in the sequence of the vasodilatory peptide maxadilan yields a pituitary adenylate cyclase-activating peptide type 1 receptor-specific antagonist.The C-terminal part of VIP is important for receptor binding and activation, as evidenced by chimeric constructs of VIP/secretin.Secondary conformational conversion is involved in glycosaminoglycans-mediated cellular uptake of the cationic cell-penetrating peptide PACAP.Identification of binding domains of pituitary adenylate cyclase activating polypeptide (PACAP) for its type 1 receptor by photoaffinity labeling.Structure of recombinant human parathyroid hormone in solution using multidimensional NMR spectroscopy.
P2860

Solution structure of pituitary adenylate cyclase activating polypeptide by nuclear magnetic resonance spectroscopy

Item
http://www.wikidata.org/entity/Q28269661
description
1993 nî lūn-bûn
@nan
1993 թուականի Յունիսին հրատարակուած գիտական յօդուած
@hyw
1993 թվականի հունիսին հրատարակված գիտական հոդված
@hy
1993年の論文
@ja
1993年論文
@yue
1993年論文
@zh-hant
1993年論文
@zh-hk
1993年論文
@zh-mo
1993年論文
@zh-tw
1993年论文
@wuu
name
Solution structure of pituitar ...... agnetic resonance spectroscopy
@ast
Solution structure of pituitar ...... agnetic resonance spectroscopy
@en
Solution structure of pituitar ...... agnetic resonance spectroscopy
@nl
type
label
Solution structure of pituitar ...... agnetic resonance spectroscopy
@ast
Solution structure of pituitar ...... agnetic resonance spectroscopy
@en
Solution structure of pituitar ...... agnetic resonance spectroscopy
@nl
prefLabel
Solution structure of pituitar ...... agnetic resonance spectroscopy
@ast
Solution structure of pituitar ...... agnetic resonance spectroscopy
@en
Solution structure of pituitar ...... agnetic resonance spectroscopy
@nl
P1433
P1476
P2093
P304
P31
P356
P407
P433
P478
P577
P698
P356
P1433
P1476
Solution structure of pituitar ...... agnetic resonance spectroscopy
@en
P2093
P304
P31
P356
P407
P433
P478
P577
P698