about
Structure of the R3/I5 Chimeric Relaxin Peptide, a Selective GPCR135 and GPCR142 AgonistStructure of human insulin-like peptide 5 and characterization of conserved hydrogen bonds and electrostatic interactions within the relaxin frameworkSolution structure, aggregation behavior, and flexibility of human relaxin-2Cellular disulfide bond formation in bioactive peptides and proteinsRelaxin-3/RXFP3 system regulates alcohol-seeking.Synthesis of fluorescent analogs of relaxin family peptides and their preliminary in vitro and in vivo characterization.ML290 is a biased allosteric agonist at the relaxin receptor RXFP1.Distinct activation modes of the Relaxin Family Peptide Receptor 2 in response to insulin-like peptide 3 and relaxinSignalling profiles of H3 relaxin, H2 relaxin and R3(BΔ23-27)R/I5 acting at the relaxin family peptide receptor 3 (RXFP3)Investigation of interactions at the extracellular loops of the relaxin family peptide receptor 1 (RXFP1).Solid-phase synthesis of europium-labeled human INSL3 as a novel probe for the study of ligand-receptor interactions.Synthetic covalently linked dimeric form of H2 relaxin retains native RXFP1 activity and has improved in vitro serum stability.C-terminus of the B-chain of relaxin-3 is important for receptor activityThe minimal active structure of human relaxin-2Identification of key residues essential for the structural fold and receptor selectivity within the A-chain of human gene-2 (H2) relaxin.Elucidation of relaxin-3 binding interactions in the extracellular loops of RXFP3.The complex binding mode of the peptide hormone H2 relaxin to its receptor RXFP1The relaxin peptide family--structure, function and clinical applications.The roles of the A- and B-chains of human relaxin-2 and -3 on their biological activity.Human relaxin-2: historical perspectives and role in cancer biology.Synthetic relaxins.Intramolecular acyl transfer in peptide and protein ligation and synthesis.Novel Methods for the Chemical Synthesis of Insulin Superfamily Peptides and of Analogues Containing Disulfide Isosteres.Phosphorylation of a full length amyloid-β peptide modulates its amyloid aggregation, cell binding and neurotoxic properties.Amyloid Beta (Aβ) Peptide and Factors that Play Important Roles in Alzheimer's Disease.Development of a Single-Chain Peptide Agonist of the Relaxin-3 Receptor Using Hydrocarbon Stapling.Relaxin family peptides: structure-activity relationship studies.Total Chemical Synthesis of an Intra-A-Chain Cystathionine Human Insulin Analogue with Enhanced Thermal Stability.Imaging the action of antimicrobial peptides on living bacterial cells.Design, synthesis, and characterization of a single-chain peptide antagonist for the relaxin-3 receptor RXFP3.Synthesis, conformational analysis and biological properties of a dicarba derivative of the antimicrobial peptide, brevinin-1BYa.The chemically synthesized human relaxin-2 analog, B-R13/17K H2, is an RXFP1 antagonist.Solid phase synthesis and structural analysis of novel A-chain dicarba analogs of human relaxin-3 (INSL7) that exhibit full biological activity.Effect of helix-promoting strategies on the biological activity of novel analogues of the B-chain of INSL3.Membrane interactions of proline-rich antimicrobial peptide, Chex1-Arg20, multimers.Probing the functional domains of relaxin-3 and the creation of a selective antagonist for RXFP3/GPCR135 over relaxin receptor RXFP1/LGR7.Structural properties of relaxin chimeras.Amphipathic alpha-helical peptide, HP (2-20), and its analogues derived from Helicobacter pylori: pore formation mechanism in various lipid compositions.Improved chemical synthesis and demonstration of the relaxin receptor binding affinity and biological activity of mouse relaxin.Design, synthesis and pharmacological evaluation of cyclic mimetics of the insulin-like peptide 3 (INSL3) B-chain.
P50
Q27650936-3BC5ECFC-A3A4-4183-B659-6520784786DDQ27653600-73B03826-2CEA-439C-A582-C23BF049CA28Q27697265-38FAB637-46D7-4A0F-8C7D-A5026757E264Q28080871-9EEAF9AE-1442-45A1-AF2D-E806C7A065FDQ30560386-9DBFF166-F227-45F6-A535-F92C63409C7EQ30575864-92ACBFCF-9F75-4DDB-B463-EF76E3B6AE62Q33774441-EC563B4B-01B3-4B13-977F-2F4F2333A575Q33789816-A9A5941D-B57B-4D2A-B553-ADA2325902EBQ34570793-FAE94716-42E9-4E11-9AF1-2AFF1AF97226Q34683416-DD2CE9C6-25DC-451F-ADDD-42E22BFBBA93Q34784916-01C331BC-D719-4F5A-98A0-3F056F1A1040Q35050690-4E6D8EF4-2CDB-4E16-ACC3-FB9EB0A9FB12Q35070373-C2258841-9C35-4A56-A441-7673636FE3E6Q35423895-C2DB6FC9-0B59-4C71-AF69-F37DD8407BE6Q36436057-9708B7DE-EAFB-4152-979E-4386F9FF6F9BQ36629045-2A8CCE3F-580B-49BD-BB4F-73A7DDA13745Q36815189-6E371429-FDD1-45AF-8CBD-128997F086DDQ37790739-5314B7AF-FB6B-468A-9D3D-493BFD85E578Q37828609-9005AA05-0138-471E-A726-C7FEE91FC08FQ38031427-715A5B25-9E5A-453C-BA4A-C84D1F884E1DQ38256717-61276470-3761-4A6F-80FE-580E1E8E32D4Q38340077-10C0A2BD-B9C1-44DE-8986-A8CCEA0F5D64Q38638788-7FEB17AA-0294-48FA-B2CF-7FB21CC70B37Q38712867-D02975E2-5D57-4B79-B423-EB260FF51908Q38753734-9C4B6C7D-7A01-4A4C-8620-5C605FA16C0FQ38755370-8442CAA1-F546-4306-A9C6-518699925674Q39030385-7DEA2859-D13F-4DF0-B535-EEBFBB357ECCQ39120979-5A34931B-DCA3-4A61-87EE-C4D0543E204AQ39329479-7DCC07E6-8BFF-44F5-8FF0-794C36A8F118Q39579521-57D2521C-857E-4E0E-823E-2B9EAE10057CQ39594170-F071BDB4-A5DB-40B3-A429-5A6C678E5B42Q39756995-79D71519-DDD3-4DC8-B601-031D50E0E423Q39864557-B5152D85-BDB2-47AD-8EDD-DC10D9857A07Q39907318-73E16042-A3C1-4BDF-9107-E99BBBE301E6Q39960017-161627BF-7CB7-400B-BE62-AC133B64640EQ39982334-D964736E-7257-41DC-A3BB-944AB793BA15Q39982342-30DEF2F3-2B1B-4048-8EB4-83480466CE6DQ40062266-480D2144-4881-477A-A3A7-BB66F4B4CD62Q40147355-51B9705E-0963-4908-9262-9EE28ED10B12Q40205666-4545DBD3-77E4-45E8-A3F4-BFE73A6A01DA
P50
description
researcher ORCID ID = 0000-0002-9961-0006
@en
name
Mohammed Akhter Hossain
@ast
Mohammed Akhter Hossain
@en
Mohammed Akhter Hossain
@es
Mohammed Akhter Hossain
@nl
type
label
Mohammed Akhter Hossain
@ast
Mohammed Akhter Hossain
@en
Mohammed Akhter Hossain
@es
Mohammed Akhter Hossain
@nl
prefLabel
Mohammed Akhter Hossain
@ast
Mohammed Akhter Hossain
@en
Mohammed Akhter Hossain
@es
Mohammed Akhter Hossain
@nl
P106
P21
P31
P496
0000-0002-9961-0006