Page last updated: 2024-09-03

flag peptide and glycine

flag peptide has been researched along with glycine in 2 studies

Compound Research Comparison

Studies (flag peptide)	Trials (flag peptide)	Recent Studies (post-2010) (flag peptide)	Studies (glycine)	Trials (glycine)	Recent Studies (post-2010) (glycine)
544	1	107	35,163	756	8,415

Protein Interaction Comparison

Protein	Taxonomy	glycine (IC50)
Glutamate receptor ionotropic, NMDA 1	Rattus norvegicus (Norway rat)	1.4852
Sodium- and chloride-dependent glycine transporter 1	Homo sapiens (human)	106
Glutamate receptor ionotropic, NMDA 2A	Rattus norvegicus (Norway rat)	0.3253
Glutamate receptor ionotropic, NMDA 2B	Rattus norvegicus (Norway rat)	0.3253
Glutamate receptor ionotropic, NMDA 2C	Rattus norvegicus (Norway rat)	0.3253
Glutamate receptor ionotropic, NMDA 2D	Rattus norvegicus (Norway rat)	0.3253
Glutamate receptor ionotropic, NMDA 3B	Rattus norvegicus (Norway rat)	0.3253
Glutamate receptor ionotropic, NMDA 3A	Rattus norvegicus (Norway rat)	0.3253
Sodium- and chloride-dependent glycine transporter 2	Homo sapiens (human)	128

Research

Studies (2)

Timeframe	Studies, this research(%)	All Research%
pre-1990	0 (0.00)	18.7374
1990's	0 (0.00)	18.2507
2000's	2 (100.00)	29.6817
2010's	0 (0.00)	24.3611
2020's	0 (0.00)	2.80

Authors

Authors	Studies
Ahern, CA; Ding, S; Horn, R; Ingleby, L	1
Arditi, M; Bell, J; Blanco, JC; Boukhvalova, MS; Hemming, VG; Lorenz, E; Medvedev, A; Rallabhandi, P; Segal, DM; Vogel, SN	1

Other Studies

2 other study(ies) available for flag peptide and glycine

Article	Year
Investigating the putative glycine hinge in Shaker potassium channel. The Journal of general physiology, 2005, Volume: 126, Issue:3 Topics: Animals; Binding Sites; Cell Line; Epitopes; Glycine; Glycosylation; Humans; Ion Channel Gating; Membrane Potentials; Mutation; Oligopeptides; Oocytes; Peptides; Point Mutation; Potassium; Potassium Channel Blockers; Potassium Channels; Protein Structure, Secondary; Quaternary Ammonium Compounds; Shaker Superfamily of Potassium Channels; Transfection; Xenopus laevis	2005
Analysis of TLR4 polymorphic variants: new insights into TLR4/MD-2/CD14 stoichiometry, structure, and signaling. Journal of immunology (Baltimore, Md. : 1950), 2006, Jul-01, Volume: 177, Issue:1 Topics: Amino Acid Substitution; Aspartic Acid; Cell Line; Extracellular Space; Genetic Variation; Glycine; Humans; Isoleucine; Lipopolysaccharide Receptors; Lipopolysaccharides; Lymphocyte Antigen 96; Oligopeptides; Peptides; Polymorphism, Genetic; Protein Binding; Protein Structure, Tertiary; Signal Transduction; Threonine; Toll-Like Receptor 4; Transfection	2006

Article

Year

Investigating the putative glycine hinge in Shaker potassium channel.

The Journal of general physiology, 2005, Volume: 126, Issue:3

Topics: Animals; Binding Sites; Cell Line; Epitopes; Glycine; Glycosylation; Humans; Ion Channel Gating; Membrane Potentials; Mutation; Oligopeptides; Oocytes; Peptides; Point Mutation; Potassium; Potassium Channel Blockers; Potassium Channels; Protein Structure, Secondary; Quaternary Ammonium Compounds; Shaker Superfamily of Potassium Channels; Transfection; Xenopus laevis

2005

Analysis of TLR4 polymorphic variants: new insights into TLR4/MD-2/CD14 stoichiometry, structure, and signaling.

Journal of immunology (Baltimore, Md. : 1950), 2006, Jul-01, Volume: 177, Issue:1

Topics: Amino Acid Substitution; Aspartic Acid; Cell Line; Extracellular Space; Genetic Variation; Glycine; Humans; Isoleucine; Lipopolysaccharide Receptors; Lipopolysaccharides; Lymphocyte Antigen 96; Oligopeptides; Peptides; Polymorphism, Genetic; Protein Binding; Protein Structure, Tertiary; Signal Transduction; Threonine; Toll-Like Receptor 4; Transfection

2006