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46 profiles
A methylquinolinium compound carrying a primary amine substitution, studied as an inhibitor of nicotinamide N-methyltransferase in enzyme assays, in cultured cells and in rodent models.
Adamax is a catalog name rather than a chemical identity: the name alone does not identify a substance, because it does not fix a sequence, a molecular formula, or a constituent list.
A synthetic peptide corresponding to the carboxyl-terminal region of human growth hormone, residues 177 to 191, with an added N-terminal tyrosine, studied in adipose tissue preparations, in rodent models and in analytical work.
An eleven-residue peptide designed from the aqueous face of helix B of erythropoietin, studied as a ligand that engages the erythropoietin receptor and CD131 heterocomplex without the erythropoietic activity of the parent protein.
A 15-residue sequence described as a partial sequence of a protein isolated from gastric juice, studied in tendon explant and tendon fibroblast culture, in vascular endothelial culture, and in analytical work that sequenced the contents of confiscated vials.
Two separately studied peptides sold under one name. The references below belong to the individual constituents: a 15-residue gastric peptide sequence and an acetylated seven-residue fragment of thymosin beta-4. No study of the mixture itself is cited.
A lipidated analogue of the pancreatic hormone amylin, developed against amylin's propensity to form amyloid fibrils, and characterized in calcitonin-family receptor pharmacology and in rodent and cross-species brainstem work.
A maleimide-bearing analogue of human growth hormone releasing factor 1-29, designed to form a covalent conjugate with the free thiol of serum albumin.
A named pairing of a growth hormone releasing factor analogue with a pentapeptide secretagogue, where the CJC name alone does not establish whether the albumin-reactive modification is present. Every reference here belongs to one constituent or the other. No study of the mixture itself is cited.
A metabolically stabilized three-residue analogue derived from angiotensin IV, studied in rodent and zebrafish models of the hepatocyte growth factor pathway, and carrying a retracted mechanism paper that the field still cites.
A nine-residue peptide isolated from rabbit and characterized alongside its synthetic fragments, later studied in intestinal cell monolayer metabolism, isolated brain mitochondria, immunohistochemistry and polymer matrix entrapment.
A four-residue peptide built from the amino acid analysis of a pineal polypeptide complex and later found inside it, studied in telomerase and telomere length assays, stem cell differentiation cultures and nucleic acid binding work.
A cysteine-rich single-chain protein first isolated from ovarian follicular fluid and since resolved by crystallography in complex with activins, myostatin and inhibin A. The cited work is structural and biophysical, and it distinguishes isoforms, fusion constructs and related follistatin-type proteins from one another.
A three-residue peptide studied together with the copper it binds. The cited work is largely solution chemistry: which species form, how stable they are, and how pH, competing ligands and albumin change the answer, with cell culture work reported against that background.
GLOW is a catalog name rather than a chemical identity: the name alone does not identify a substance, because it fixes neither a constituent list nor the amount of any constituent.
A thiol tripeptide resolved bound in enzyme and transporter structures, measured as a redox couple inside living cells, and characterized chemically as a molecule that copper can turn from a reductant into a source of radicals.
A two-subunit glycoprotein hormone whose fold, subunit interface, receptor interaction and glycoform distribution are described in crystallographic, single-molecule and mass spectrometry work.
A synthetic hexapeptide of the growth hormone releasing peptide family, mapped to a binding site on the scavenger receptor CD36 and studied in macrophage, adipocyte and neuronal cell culture.
A recombinant analogue of insulin-like growth factor I carrying an N-terminal extension and an arginine at position 3, built so that it binds poorly to the IGF binding proteins. Almost every cited result is a comparison against native IGF-I under a defined binding protein condition.
A synthetic pentapeptide characterized in growth hormone secretagogue receptor assays on primary rat pituitary cells and used since as a scaffold for labeled receptor ligands.
A ten-residue RF-amide fragment of the kisspeptin family, studied through KISS1 receptor binding and signaling work and through cell culture experiments in fibroblasts, chondrocytes and carcinoma lines.
KLOW is a catalog name rather than a chemical identity: the name alone does not identify a substance, because it is neither an amino-acid sequence nor a composition statement.
The C-terminal three residues of alpha-melanocyte stimulating hormone, studied as a substrate of the di and tripeptide transporter PepT1 and as an inhibitor of NF-kappaB signalling in epithelial and immune cell cultures.
A small zwitterionic molecule studied as the substrate of the OCTN2 carnitine transporter and of the carnitine acyltransferase enzymes, characterized in transport assays across several cell types and in crystal structures of two acyltransferases.
LIPO-C is a formulation name rather than a chemical identity: the name alone does not identify a substance, because it does not fix which constituents are present, in what proportions, or in what solvent.
A cyclic melanotropin closed by a lactam bridge between an aspartate and a lysine side chain, arrived at through a ring-size series and since used as the template for structure-activity work at the human melanocortin receptors. The exact ring and its contents, not the trade name, decide what the material does in the cited assays.
A linear 13-residue analogue of alpha-melanocyte stimulating hormone carrying norleucine at position 4 and D-phenylalanine at position 7, characterised in amphibian skin and mouse melanoma assays, in forced degradation work and in melanocortin receptor binding studies.
A 16-residue peptide encoded by a short open reading frame within the mitochondrial 12S ribosomal RNA gene, studied in muscle cell lines, in nuclear translocation experiments and in rodent metabolic models.
The oxidized form of a dinucleotide redox cofactor, resolved bound in enzyme crystal structures, consumed by sirtuins and ADP-ribosyltransferases, and measured as free concentrations inside separate subcellular compartments.
A nine-residue disulfide-bridged peptide hormone whose receptor has been resolved in agonist-bound and antagonist-bound states, and which is studied through cation coordination, cholesterol allostery and receptor variant work.
A three-residue peptide studied in oxidative stress cell models, in nucleic acid binding experiments and in molecular dynamics work on its interaction with the DNA major groove.
A cyclic melanocortin peptide analogue, present as a ligand in a melanocortin-4 receptor structure and characterised by forced degradation and high resolution mass spectrometry.
A single peptide reported to act at three receptors, the glucagon receptor, the glucose-dependent insulinotropic polypeptide receptor and the GLP-1 receptor, characterized in receptor activity assays and in several rodent models.
A synthetic heptapeptide that extends the tuftsin sequence with a C-terminal Pro-Gly-Pro tripeptide, studied in radioligand binding on isolated brain membranes, hippocampal slice electrophysiology, neuroblastoma gene panels and analytical identification work.
An acylated GLP-1 analogue carrying two substitutions relative to human GLP-1 and a fatty acid attached at lysine 26, characterized in receptor and albumin binding assays, in a cryo-EM structure of the receptor complex, and in rodent and cell-culture work.
A synthetic heptapeptide built from an adrenocorticotropic hormone fragment and a C-terminal Pro-Gly-Pro tripeptide, studied in isolated brain membrane binding assays, artificial membrane aggregation models and rat brain transcriptome work.
A listing that names two separate synthetic heptapeptides, each with its own sequence and its own literature. Everything below is drawn from the component profiles and describes the individual peptides. No study of the mixture itself is cited.
The amidated 1-29 fragment of human growth hormone releasing factor, studied through solution structure, protease kinetics, conjugation chemistry and validated separation methods.
A synthetic pan agonist of the three estrogen-related receptor subtypes, reported as the first such compound with the pharmacokinetic properties needed to serve as a chemical tool in animals, and characterized in muscle cell lines and several rodent models.
A tetrapeptide of alternating cationic and aromatic residues studied for its interaction with cardiolipin in the inner mitochondrial membrane, its mitochondrial protein cross-linking partners and a candidate protein target identified by genetic screening.
A product name that analytical work resolved to Ac-LKKTETQ, the N-terminally acetylated 17 to 23 fragment of thymosin beta-4. The fragment, the unacetylated fragment and the full-length protein are three different materials, and the cited papers keep them apart.
A 44-residue growth hormone releasing factor analogue carrying a trans-3-hexenoyl group on Tyr1, studied in plasma stability work, preclinical pharmacokinetics and analytical detection methods.
Two peptides from different families in one listing: a modified 44-residue growth hormone releasing factor analogue and a pentapeptide secretagogue. Every reference here belongs to one constituent or the other. No study of the mixture itself is cited.
A 28-residue peptide first isolated and sequenced from a calf thymus fraction, later characterised by solution NMR and by chemo-enzymatic synthesis, and studied in cultured human dendritic cells, mononuclear cells and CD8 positive T cells.
A fatty acid modified peptide that activates both the GIP and the GLP-1 receptor, characterized in cell-line signaling assays, in isolated islets, in mice, and in cryo-EM structures of both receptor complexes.
A 28-residue peptide first isolated from porcine small intestine, studied through the cloning and radioligand pharmacology of its two class B receptors, receptor proteolysis in different detergents and structural work on the receptor family.
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