Interaction of substance P and its N‐ and C‐terminal fragments with Ca2+: Implications for hormone action

scientific article published on 01 December 1992

Interaction of substance P and its N‐ and C‐terminal fragments with Ca2+: Implications for hormone action is …
instance of (P31):
scholarly articleQ13442814

External links are
P356DOI10.1002/BIP.360321217
P953full work available at URLhttps://api.wiley.com/onlinelibrary/tdm/v1/articles/10.1002%2Fbip.360321217
https://onlinelibrary.wiley.com/doi/pdf/10.1002/bip.360321217
P698PubMed publication ID1282041

P2093author name stringV. S. Ananthanarayanan
S. Orlicky
P2860cites workPeptide models for protein-mediated cation transportQ71532716
Substance P and behavior: Opposite effects of N-terminal and C-terminal fragmentsQ72721185
Turns in peptides and proteinsQ28282176
Preferential conformation of substance P in solutionQ30687360
Conformational Analysis of the Tachykinins in Solution: Substance P and PhysalaeminQ31080741
Conformational preferences of [Leu5]enkephalin in biomimetic media. Investigation by 1H NMR.Q34077540
H+- and Ca2+-induced fusion and destabilization of liposomes.Q34199456
A general method, employing arsenazo III in liposomes, for study of calcium ionophores: results with A23187 and prostaglandinsQ36360282
Peptide-membrane interactions and a new principle in quantitative structure-activity relationshipsQ36435277
Inositol trisphosphate as a second messenger in signal transductionQ39661284
Substance P and bombesin elevate cytosolic Ca2+ by different molecular mechanisms in a rat pancreatic acinar cell lineQ41729908
Acyclic model peptides with ionophoretic activity. Pr3+ transport by N-tBoc-Pro-Xxx-Ala-NHCH3.Q42220693
Synthesis and biological activity of Substance P C-terminal hexapeptide and heptapeptide analoguesQ44645049
Differential effects of two C-terminal peptides of substance P on human neutrophilsQ45156367
The substance P(1–7) fragment is a potent modulator of substance P actions in the brainQ48949780
Polypeptide models of collagen. II. Solution properties of (Pro-Gly-Phe)nQ67389649
Substance P Causes Pain—But Also HealsQ67666739
Molecular dynamics simulation provides a possible structure for substance P-like peptides in aqueous solutionQ67674156
Induction of Ca2+ transport in liposomes by insulinQ68126347
Synthetic peptides corresponding to human follicle-stimulating hormone (hFSH)-beta-(1-15) and hFSH-beta-(51-65) induce uptake of 45Ca++ by liposomes: evidence for calcium-conducting transmembrane channel formationQ68237423
Peptides in membranes: lipid-induced secondary structure of substance PQ68993502
The conformational analysis of substance P analogs using high-field NMR techniquesQ69125931
An NMR study of the conformations of N-terminal substance P fragments and antagonistsQ69129201
Quantitation of Ca2+ uptake by Arsenazo III-loaded liposomesQ69624327
Essential adaptation of the calcium influx assay into liposomes with entrapped arsenazo III for studies on the possible calcium translocating properties of acidic phospholipidsQ69948960
Circular dichroism of biological membranes. I. Mitochondria and red blood cell ghostsQ70713697
P433issue12
P407language of work or nameEnglishQ1860
P921main subjectbiochemistryQ7094
biophysicsQ7100
organic chemistryQ11351
P304page(s)1765-1773
P577publication date1992-12-01
P1433published inBiopolymersQ15767528
P1476titleInteraction of substance P and its N- and C-terminal fragments with Ca2+: implications for hormone action
Interaction of substance P and its N‐ and C‐terminal fragments with Ca2+: Implications for hormone action
P478volume32

Reverse relations

cites work (P2860)
Q46414332Anchoring a cytoactive factor in a wound bed promotes healing
Q41784084Conformation and self-association of the peptide hormone substance P: Fourier-transform infrared spectroscopic study
Q34190248Membrane-Induced Structure of Scyliorhinin I: A Dual NK1/NK2 Agonist
Q27640297Solution structure of the tachykinin peptide eledoisin
Q24537743Three-dimensional structure of the mammalian tachykinin peptide neurokinin A bound to lipid micelles

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