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Membrane‐induced structure of novel human tachykinin hemokinin‐1 (h HK 1)

https://doi.org/10.1002/bip.22734
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Outgoing claims: the papers this work cites, builds on, or argues with.

inferredcites →https://doi.org/10.1002/bip.10312openalex-snapshot
Extracellular domains of the neurokinin‐1 receptor: Structural characterization and interactions with substance P
inferredcites →https://doi.org/10.1002/bip.360321217openalex-snapshot
Interaction of substance P and its N‐ and C‐terminal fragments with Ca2+: Implications for hormone action
inferredcites →https://doi.org/10.1002/j.1460-2075.1996.tb01011.xopenalex-snapshot
Connectivity and orientation of the seven helical bundle in the tachykinin NK‐1 receptor probed by zinc site engineering.
inferredcites →https://doi.org/10.1006/jmbi.1997.1284openalex-snapshot
Torsion angle dynamics for NMR structure calculation with the new program Dyana
inferredcites →https://doi.org/10.1007/978-1-4612-0301-8_7openalex-snapshot
Molecular Biology of Receptors
inferredcites →https://doi.org/10.1007/s00018-004-4035-xopenalex-snapshot
Hemokinins and endokinins
inferredcites →https://doi.org/10.1016/0014-2999(87)90711-4openalex-snapshot
Further studies on the mechanisms of the tachykinin-induced activation of micturition reflex in rats: evidence for the involvement of the capsaicin-sensitive bladder mechanoreceptors
inferredcites →https://doi.org/10.1016/0022-2836(84)90035-4openalex-snapshot
Calibration of the angular dependence of the amide proton-Cα proton coupling constants, 3JHNα, in a globular protein
inferredcites →https://doi.org/10.1016/0143-4179(84)90007-6openalex-snapshot
Comparative potencies of substance P, substance K and neuromedin K on brain substance P receptors
inferredcites →https://doi.org/10.1016/0143-4179(91)90093-xopenalex-snapshot
Influence of the replacement of amino acid by its D-enantiomer in the sequence of substance P. 2. Conformational analysis by NMR and energy calculations
inferredcites →https://doi.org/10.1016/0167-0115(93)90404-vopenalex-snapshot
Molecular aspects of the tachykinin receptors
inferredcites →https://doi.org/10.1016/0167-4838(88)90084-2openalex-snapshot
Analysis of tachykinin-binding site interactions using NMR and energy calculation data of potent cyclic analogues of substance P
inferredcites →https://doi.org/10.1016/0197-0186(91)90180-lopenalex-snapshot
Tachykinin receptor types: Classification and membrane signalling mechanisms
inferredcites →https://doi.org/10.1016/0306-3623(94)00292-uopenalex-snapshot
The mammalian tachykinin receptors
inferredcites →https://doi.org/10.1016/j.bbamem.2010.09.023openalex-snapshot
NMR evidence of GM1-induced conformational change of Substance P using isotropic bicelles
inferredcites →https://doi.org/10.1016/j.bbi.2007.12.010openalex-snapshot
In vivo characterization of the effects of human hemokinin-1 and human hemokinin-1(4-11), mammalian tachykinin peptides, on the modulation of pain in mice
inferredcites →https://doi.org/10.1016/j.bcp.2010.12.007openalex-snapshot
The N-terminal domain of human hemokinin-1 influences functional selectivity property for tachykinin receptor neurokinin-1
inferredcites →https://doi.org/10.1016/j.ejphar.2008.05.049openalex-snapshot
Cardiovascular responses to intravenous administration of human hemokinin-1 and its truncated form hemokinin-1(4-11) in anesthetized rats
inferredcites →https://doi.org/10.1016/j.ejphar.2008.06.097openalex-snapshot
The role of the N-terminal and mid-region residues of substance P in regulating functional selectivity at the tachykinin NK1 receptor
inferredcites →https://doi.org/10.1016/j.jneuroim.2004.06.005openalex-snapshot
Expression of hemokinin 1 mRNA by murine dendritic cells
inferredcites →https://doi.org/10.1016/j.jneuroim.2005.03.016openalex-snapshot
Hemokinin-1 has Substance P-like function in U-251 MG astrocytoma cells: A pharmacological and functional study
inferredcites →https://doi.org/10.1016/j.jsb.2004.08.008openalex-snapshot
Membrane-induced structure of the mammalian tachykinin Neuropeptide gamma
inferredcites →https://doi.org/10.1016/j.jsb.2006.07.006openalex-snapshot
Solution structure of amphibian tachykinin Uperolein bound to DPC micelles
inferredcites →https://doi.org/10.1016/j.jsb.2009.04.008openalex-snapshot
Three-dimensional structure of Phyllomedusin, a NK1 receptor agonist bound to dodecylphosphocholine micelles
inferredcites →https://doi.org/10.1016/j.neulet.2005.09.005openalex-snapshot
Effect of intrathecal administration of hemokinin-1 on the withdrawal response to noxious thermal stimulation of the rat hind paw
inferredcites →https://doi.org/10.1016/j.npep.2010.04.006openalex-snapshot
Effects of rat/mouse hemokinin-1, human hemokinin-1 and human hemokinin-1(4-11), mammalian tachykinin peptides, on rate and perfusion pressure in the isolated guinea pig heart
inferredcites →https://doi.org/10.1016/j.npep.2013.04.001openalex-snapshot
Hemokinin-1 competitively inhibits substance P-induced stimulation of osteoclast formation and function
inferredcites →https://doi.org/10.1016/j.peptides.2011.02.012openalex-snapshot
Expression and proliferative effect of hemokinin-1 in human B-cells
inferredcites →https://doi.org/10.1016/s0006-3495(03)74448-8openalex-snapshot
Engineering Teams Up with Computer-Simulation and Visualization Tools to Probe Biomolecular Mechanisms
inferredcites →https://doi.org/10.1016/s0006-3495(03)74814-0openalex-snapshot
Three-Dimensional Structure of the Mammalian Tachykinin Peptide Neurokinin A Bound to Lipid Micelles
inferredcites →https://doi.org/10.1016/s0006-3495(03)74885-1openalex-snapshot
Solution Structure of the Tachykinin Peptide Eledoisin
inferredcites →https://doi.org/10.1016/s0021-9258(18)46979-7openalex-snapshot
The ligand binding site of the neurokinin 2 receptor. Site-directed mutagenesis and identification of neurokinin A binding residues in the human neurokinin 2 receptor.
inferredcites →https://doi.org/10.1016/s0021-9258(18)53041-6openalex-snapshot
Chimeric NK1 (substance P)/NK3 (neurokinin B) receptors. Identification of domains determining the binding specificity of tachykinin agonists.
inferredcites →https://doi.org/10.1016/s0026-895x(24)08985-5openalex-snapshot
Structural Mimicry in G Protein-Coupled Receptors: Implications of the High-Resolution Structure of Rhodopsin for Structure-Function Analysis of Rhodopsin-Like Receptors
inferredcites →https://doi.org/10.1016/s0026-895x(25)09261-2openalex-snapshot
Determination of the amino acid residues in substance P conferring selectivity and specificity for the rat neurokinin receptors.
inferredcites →https://doi.org/10.1016/s0028-3908(03)00150-3openalex-snapshot
Centrally administered hemokinin-1 (HK-1), a neurokinin NK1 receptor agonist, produces substance P-like behavioral effects in mice and gerbils
inferredcites →https://doi.org/10.1016/s0031-6997(25)06810-3openalex-snapshot
Receptors and antagonists for substance P and related peptides.
inferredcites →https://doi.org/10.1016/s0165-6147(00)01734-xopenalex-snapshot
Erratum
inferredcites →https://doi.org/10.1016/s0378-1119(02)00861-2openalex-snapshot
Identification, localization and receptor characterization of novel mammalian substance P-like peptides
inferredcites →https://doi.org/10.1021/bi00031a029openalex-snapshot
Identification of Residues Involved in Ligand Binding to the Neurokinin-2 Receptor
inferredcites →https://doi.org/10.1021/bi00069a025openalex-snapshot
Conformational behavior of Escherichia coli OmpA signal peptides in membrane mimetic environments
inferredcites →https://doi.org/10.1021/bi00080a010openalex-snapshot
Determination of the solution structure of neuropeptide K by high-resolution nuclear magnetic resonance spectroscopy
inferredcites →https://doi.org/10.1021/bi00121a010openalex-snapshot
The chemical shift index: a fast and simple method for the assignment of protein secondary structure through NMR spectroscopy
inferredcites →https://doi.org/10.1021/bi00126a008openalex-snapshot
Interaction of a substance P agonist and of substance P antagonists with lipid membranes. A thermodynamic analysis
inferredcites →https://doi.org/10.1021/bi00162a019openalex-snapshot
The extracellular domain of the neurokinin-1 receptor is required for high-affinity binding of peptides
inferredcites →https://doi.org/10.1021/bi00176a033openalex-snapshot
Interaction of Substance P with the Second and Seventh Transmembrane Domains of the Neurokinin-1 Receptor
inferredcites →https://doi.org/10.1021/bi001880xopenalex-snapshot
Photoaffinity Labeling of Mutant Neurokinin-1 Receptors Reveals Additional Structural Features of the Substance P/NK-1 Receptor Complex
inferredcites →https://doi.org/10.1021/bi00432a021openalex-snapshot
Binding of a neuropeptide, substance P, to neutral and negatively charged lipids
inferredcites →https://doi.org/10.1021/bi052287oopenalex-snapshot
Three-Dimensional Structure of Neuropeptide K Bound to Dodecylphosphocholine Micelles
inferredcites →https://doi.org/10.1021/bi952434qopenalex-snapshot
Binding of Substance P Agonists to Lipid Membranes and to the Neurokinin-1 Receptor
inferredcites →https://doi.org/10.1021/ci2000264openalex-snapshot
Molecular Modeling of Neurokinin B and Tachykinin NK3Receptor Complex
inferredcites →https://doi.org/10.1021/ci900055xopenalex-snapshot
Molecular Modeling of the Peptide Agonist-Binding Site in a Neurokinin-2 Receptor
inferredcites →https://doi.org/10.1021/ja00901a059openalex-snapshot
Vicinal Proton Coupling in Nuclear Magnetic Resonance
inferredcites →https://doi.org/10.1021/jm970789xopenalex-snapshot
Membrane-Induced Secondary Structures of Neuropeptides: A Comparison of the Solution Conformations Adopted by Agonists and Antagonists of the Mammalian Tachykinin NK1 Receptor
inferredcites →https://doi.org/10.1038/374074a0openalex-snapshot
Conversion of antagonist-binding site to metal-ion site in the tachykinin NK-1 receptor
inferredcites →https://doi.org/10.1038/80826openalex-snapshot
Hemokinin is a hematopoietic-specific tachykinin that regulates B lymphopoiesis
inferredcites →https://doi.org/10.1038/84159openalex-snapshot
Conformation of a peptide ligand bound to its G-protein coupled receptor.
inferredcites →https://doi.org/10.1038/sj.bjp.0704443openalex-snapshot
Pharmacological profile of the novel mammalian tachykinin, hemokinin 1
inferredcites →https://doi.org/10.1051/epn/19861701011openalex-snapshot
NMR with Proteins and Nucleic Acids
inferredcites →https://doi.org/10.1073/pnas.0931458100openalex-snapshot
Characterization of the endokinins: Human tachykinins with cardiovascular activity
inferredcites →https://doi.org/10.1073/pnas.90.13.6194openalex-snapshot
Two nonpeptide tachykinin antagonists act through epitopes on corresponding segments of the NK1 and NK2 receptors.
inferredcites →https://doi.org/10.1073/pnas.93.1.433openalex-snapshot
The peptide binding site of the substance P (NK-1) receptor localized by a photoreactive analogue of substance P: presence of a disulfide bond.
inferredcites →https://doi.org/10.1074/jbc.271.34.20250openalex-snapshot
The Unpredicted High Affinities of a Large Number of Naturally Occurring Tachykinins for Chimeric NK1/NK3 Receptors Suggest a Role for an Inhibitory Domain in Determining Receptor Specificity
inferredcites →https://doi.org/10.1074/jbc.271.42.25797openalex-snapshot
Identification of Methionine as the Site of Covalent Attachment of a p-Benzoyl-Phenylalanine-containing Analogue of Substance P on the Substance P (NK-1) Receptor
inferredcites →https://doi.org/10.1074/jbc.m101057200openalex-snapshot
Molecular Characterization of the Substance P·Neurokinin-1 Receptor Complex
inferredcites →https://doi.org/10.1074/jbc.m106330200openalex-snapshot
Interaction of Met297 in the Seventh Transmembrane Segment of the Tachykinin NK2 Receptor with Neurokinin A
inferredcites →https://doi.org/10.1074/jbc.m312671200openalex-snapshot
Evolutionary Trace of G Protein-coupled Receptors Reveals Clusters of Residues That Determine Global and Class-specific Functions
inferredcites →https://doi.org/10.1080/07391102.1997.10508942openalex-snapshot
Lipid-induced Conformation of Substance P
inferredcites →https://doi.org/10.1080/07391102.2001.10506693openalex-snapshot
Lipid Induced Conformation of the Tachykinin Peptide Kassinin
inferredcites →https://doi.org/10.1080/07391102.2004.10506990openalex-snapshot
Three Dimensional Structure of Mammalian Tachykinin Peptide Neurokinin B Bound to Lipid Micelles
inferredcites →https://doi.org/10.1093/humrep/dem069openalex-snapshot
A role for tachykinins in the regulation of human sperm motility
inferredcites →https://doi.org/10.1093/nar/gkh381openalex-snapshot
PDB2PQR: an automated pipeline for the setup of Poisson-Boltzmann electrostatics calculations
inferredcites →https://doi.org/10.1093/nar/gkm276openalex-snapshot
PDB2PQR: expanding and upgrading automated preparation of biomolecular structures for molecular simulations
inferredcites →https://doi.org/10.1095/biolreprod.103.017111openalex-snapshot
A Role for Tachykinins in Female Mouse and Rat Reproductive Function1
inferredcites →https://doi.org/10.1107/s0021889892008240openalex-snapshot
Quality control of protein models: directional atomic contact analysis
inferredcites →https://doi.org/10.1107/s0021889892009944openalex-snapshot
PROCHECK: a program to check the stereochemical quality of protein structures
inferredcites →https://doi.org/10.1111/j.1432-1033.1994.tb18604.xopenalex-snapshot
Solution structure of seminal plasmin in the presence of micelles
inferredcites →https://doi.org/10.1111/j.1474-8673.1993.tb00396.xopenalex-snapshot
Tachykinin receptors and tachykinin receptor antagonists
inferredcites →https://doi.org/10.1124/jpet.106.109512openalex-snapshot
Functional Selectivity of NK1 Receptor Signaling: Peptide Agonists Can Preferentially Produce Receptor Activation or Desensitization
inferredcites →https://doi.org/10.1124/mol.107.042754openalex-snapshot
Me-Talnetant and Osanetant Interact within Overlapping but Not Identical Binding Pockets in the Human Tachykinin Neurokinin 3 Receptor Transmembrane Domains
inferredcites →https://doi.org/10.1124/mol.53.1.166openalex-snapshot
Steric Hindrance Mutagenesis versus Alanine Scan in Mapping of Ligand Binding Sites in the Tachykinin NK1 Receptor
inferredcites →https://doi.org/10.1124/pr.54.2.285openalex-snapshot
The Tachykinin Peptide Family
inferredcites →https://doi.org/10.1126/science.289.5480.739openalex-snapshot
Crystal Structure of Rhodopsin: A G Protein-Coupled Receptor
inferredcites →https://doi.org/10.1146/annurev.ne.14.030191.001011openalex-snapshot
Mammalian Tachykinin Receptors
inferredcites →https://doi.org/10.1210/edrv.21.1.0390openalex-snapshot
Uncovering Molecular Mechanisms Involved in Activation of G Protein-Coupled Receptors
inferredcites →https://doi.org/10.1529/biophysj.104.053231openalex-snapshot
Membrane-Induced Structure of Scyliorhinin I: A Dual NK1/NK2 Agonist
inferredcites →https://doi.org/10.4049/jimmunol.172.11.6528openalex-snapshot
Cutting Edge: Hemokinin Has Substance P-Like Function and Expression in Inflammation

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inferred← citeshttps://doi.org/10.2139/ssrn.4587162openalex-extracted
inferred← citeshttps://doi.org/10.1002/jsde.12015openalex-snapshot
Nuclear Magnetic Resonance Investigation of the Effect of pH on Micelle Formation by the Amino Acid‐Based Surfactant Undecyl l ‐Phenylalaninate
inferred← citeshttps://doi.org/10.1002/jssc.201901038openalex-snapshot
A design of experiments concept for the minimization of nonspecific peptide adsorption in the mass spectrometric determination of substance P and related hemokinin‐1
inferred← citeshttps://doi.org/10.1002/pep2.24104openalex-snapshot
CB 1 cannabinoid receptor‐phosphorylated fourth intracellular loop structure‐function relationships
inferred← citeshttps://doi.org/10.1016/j.cca.2019.05.014openalex-snapshot
Substance P in cardiovascular diseases – A bioanalytical review
inferred← citeshttps://doi.org/10.1016/j.jevs.2023.104979openalex-snapshot
Evaluation of substance P as a biomarker for pain in equine colic
inferred← citeshttps://doi.org/10.1016/j.npep.2016.12.003openalex-snapshot
Role of hemokinin-1 in health and disease
inferred← citeshttps://doi.org/10.1021/acs.jmedchem.2c02021openalex-snapshot
Development of Neuropeptide Hemokinin-1 Analogues with Antimicrobial and Wound-Healing Activity
inferred← citeshttps://doi.org/10.1080/01932691.2022.2145303openalex-snapshot
NMR investigation of counterion binding to undecyl LL-leucinevalanate micelles
inferred← citeshttps://doi.org/10.54005/geneltip.1302757openalex-snapshot
Could Hemokinin-1 (HK-1) be a Novel Candidate Biomarker for Sarcoidosis?
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