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D. C. Fry, V. S. Madison, D. R. Bolin, et al., “Solution Structure of an Analogue of Vasoactive Intestinal Peptide as Determined by Two-Dimensional NMR and Circular Dichroism Spectroscopies and constrained Molecular Dynamics,” Biochemistry, Vol. 28, No. 6, 1989, pp. 2399-2409. doi:10.1021/bi00432a010

has been cited by the following article:

• TITLE: Vasoactive Intestinal Peptide (VIP) and VIP Receptors-Elucidation of Structure and Function for Therapeutic Applications

  AUTHORS: Hisato Igarashi, Nao Fujimori, Tetsuhide Ito, Taichi Nakamura, Takamasa Oono, Kazuhiko Nakamura, Koichi Suzuki, Robert T Jensen, Ryoichi Takayanagi

  KEYWORDS: Vasoactive Intestinal Peptide, VIP, VPAC

  JOURNAL NAME: International Journal of Clinical Medicine, Vol.2 No.4, September 30, 2011

  ABSTRACT: Vasoactive intestinal peptide (VIP) is a 28-amino acid polypeptide first isolated from swine duodenum. VIP is a neurotransmitter that is extensively distributed in tissues. According to published reports, VPAC1 and VPAC2 act as VIP receptors and are widely present in the central nervous system and peripheral tissues. VIP exerts diverse actions on the cardiovascular system, pancreas, digestive tract, respiratory system, and urological system. Recent reports indicated that VIP has immunological and neuroprotective effects and also affects cell growth. While primary investigations for developing therapeutic applications for various pathological conditions and diseases are underway, the structure and function of VIP should be analyzed in more detail.