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pro vyhledávání: '"Yong-Jiang Cao"'
Autor:
Yong-Jiang Cao, Ariel Quiñones, Christof M. Kramm, Nikolai G. Rainov, Karl-Ulrich Dobberstein, Constanze Nafe
Publikováno v:
Life Sciences. 73:1847-1860
Recombinant retroviruses (RV) have been widely used as vectors for clinical gene therapy of malignant brain tumors. Because of the very limited stability of these vectors in vivo, RV producing cells (VPC) are routinely used for intratumoral RV releas
Publikováno v:
FEBS Letters. 469:142-146
The pituitary adenylate cyclase activating polypeptide (PACAP) type I receptor belongs to the glucagon/secretin/vasoactive intestinal polypeptide (VIP) receptor family. We mutated and deleted an amino acid residue (E261) which is located within the s
Autor:
Marek Jasionowski, Gerald Gimpl, Franciszek Kasprzykowski, Falk Fahrenholz, Elzbieta Kojro, Leszek Lankiewicz, Yong-Jiang Cao
Publikováno v:
European Journal of Biochemistry. 244:400-406
To identify residues and domains of the peptide hormone pituitary adenylate-cyclase-activating polypeptide (PACAP) that interact with the type I receptor, two photoreactive analogues of PACAP-( 1-27)peptide were synthesized using solid-phase peptide
Publikováno v:
Biochimica et Biophysica Acta (BBA) - Molecular Cell Research. 1222:432-440
In pig brain a type I receptor for pituitary adenylate cyclase activating polypeptide (PACAP) has been identified and structurally characterized. Scatchard analysis of the equilibrium binding data indicates a single class of binding sites with Kd of
Autor:
Yong-Jiang Cao, Gerald Gimpl
Publikováno v:
Biochimica et biophysica acta. 1548(1)
In the present study, we have analyzed a previously identified constitutively active pituitary adenylate cyclase activating polypeptide (PACAP) type I (PAC1) receptor with a deletion of the single amino acid residue Glu 261 (Y.-J. Cao, G. Gimpl, F. F
Publikováno v:
Hybridoma. 18(4)
Pituitary adenylate cyclase activating polypeptide type I receptor (PACAPr) belongs to the novel subfamily of the G-protein coupled receptors with a long extracellular N-terminus, which functions as a major binding site for the PACAP. Three different
Autor:
Falk Fahrenholz, Elzbieta Kojro, Yong-Jiang Cao, Zbigniew Grzonka, Marek Jasionowski, Leszek Lankiewicz
Publikováno v:
Annals of the New York Academy of Sciences. 865
Structure-function studies and photoaffinity labeling experiments were performed to identify residues and domains of PACAP involved in the interaction with PACAP receptors. For this purpose, a series of photoreactive analogues of PACAP(1-27) containi
Publikováno v:
Biochemical and biophysical research communications. 212(2)
The PACAP receptor represents a member of a novel subfamily of G-protein coupled receptors with a common structurally conserved extracellular domain of about 150 amino acids. We have addressed the question whether this extracellular amino-terminus of