about
sameAs
Paths reunited: Initiation of the classical and lectin pathways of complement activationOn the Extent and Origins of Genic Novelty in the Phylum NematodaMalaria protein kinase CK2 (PfCK2) shows novel mechanisms of regulationFascaplysin as a specific inhibitor for CDK4: insights from molecular modellingA heme-binding domain controls regulation of ATP-dependent potassium channels.Mining genomes of marine cyanobacteria for elements of zinc homeostasis.Unique residues in the ATP gated human P2X7 receptor define a novel allosteric binding pocket for the selective antagonist AZ10606120.Developmentally regulated expression, alternative splicing and distinct sub-groupings in members of the Schistosoma mansoni venom allergen-like (SmVAL) gene family.Flexible boosting of accelerated failure time models.MicroRNA and tasiRNA diversity in mature pollen of Arabidopsis thalianaAnalogous interactions in initiating complexes of the classical and lectin pathways of complementAcinetobacter insertion sequence ISAba11 belongs to a novel family that encodes transposases with a signature HHEK motifComparative modelling of human PHOSPHO1 reveals a new group of phosphatases within the haloacid dehalogenase superfamily.Structural Insights into Separase Architecture and Substrate Recognition through Computational Modelling of Caspase-Like and Death Domains.Agonist binding evokes extensive conformational changes in the extracellular domain of the ATP-gated human P2X1 receptor ion channel.Molecular evolution of a pervasive natural amino-acid substitution in Drosophila cryptochrome.The splicing landscape is globally reprogrammed during male meiosis.Cysteine scanning mutagenesis (residues Glu52-Gly96) of the human P2X1 receptor for ATP: mapping agonist binding and channel gatingStructural analysis of the adenovirus type 2 E3/19K protein using mutagenesis and a panel of conformation-sensitive monoclonal antibodies.Mechanistic insights from resolving ligand-dependent kinetics of conformational changes at ATP-gated P2X1R ion channels.Use of chimeras, point mutants, and molecular modeling to map the antagonist-binding site of 4,4',4″,4‴-(carbonylbis-(imino-5,1,3-benzenetriylbis(carbonylimino)))tetrakisbenzene-1,3-disulfonic acid (NF449) at P2X1 receptors for ATP.Probing the substrate specificities of human PHOSPHO1 and PHOSPHO2.A novel copper site in a cyanobacterial metallochaperone.Cytosolic metal handling in plants: determinants for zinc specificity in metal transporters and metallothioneins.Functional properties of the alternative NADH:ubiquinone oxidoreductase from E. coli through comparative 3-D modelling.Exploring the primary electron acceptor (QA)-site of the bacterial reaction center from Rhodobacter sphaeroides. Binding mode of vitamin K derivatives.Pitfalls of using out of date databases. Comment on Guo et al. and Guo et al.Flavones as colorectal cancer chemopreventive agents--phenol-o-methylation enhances efficacy.PartiGene--constructing partial genomes.A mechanism for CO regulation of ion channels.Mapping the Allosteric Action of Antagonists A740003 and A438079 Reveals a Role for the Left Flipper in Ligand Sensitivity at P2X7 Receptors.A transcriptomic analysis of the phylum NematodaA Canonical EF-Loop Directs Ca2+-Sensitivity in Phospholipase C-η2ATP-Gated P2X Receptor Channels: Molecular Insights into Functional RolesOrganization of ATP-gated P2X1 receptor intracellular termini in apo and desensitized statesEST Processing: From Trace to SequenceToward a property/function relationship for metallothioneins: histidine coordination and unusual cluster composition in a zinc-metallothionein from plantsMapping the binding site of the P2X receptor antagonist PPADS reveals the importance of orthosteric site charge and the cysteine-rich head regionMapping the Site of Action of Human P2X7 Receptor Antagonists AZ11645373, Brilliant Blue G, KN-62, Calmidazolium, and ZINC58368839 to the Intersubunit Allosteric PocketIdentification of a distinct desensitisation gate in the ATP-gated P2X2 receptor
P50
Q24646047-8CB8CABE-A6B9-4B5F-BCDB-807A030C4989Q27486381-F15ADF89-967B-47FE-B3CA-788113C85FAEQ27973595-66ABC9CD-457B-4FE9-A1AE-7CDBFF27A5EDQ28482234-13BDA370-18AE-4023-9209-F45BB59B4E9EQ30385980-F302F194-FD3D-41CF-BD52-D0422C8273FDQ30512952-26EAC889-1E7B-42EC-A31E-3117EC2B842CQ30850022-B5A67E74-72F8-42EC-A076-714EA52864F8Q33320897-D89D7ECF-2084-4017-A1C2-CCB54698683DQ33327417-A96BAA3C-E0DA-42EC-AC26-657488EA71AEQ33521387-AB412E3F-1C84-4C37-8D84-0EC8A23D1024Q33666670-EBA24375-F246-43D7-B2E2-BFD913394F5FQ34073932-A512B85E-CBC8-4F30-889B-7AC2DC151DC1Q34300917-6C5E7071-E52D-4604-8332-62D9CCF183F7Q35826136-A58013E1-7E5C-44A9-8FA5-BBE9540AB8E5Q35849755-CE848EFF-A7C8-4A52-A226-5CE01930E4BBQ37514294-8B3EA8FF-F9D2-4687-BD8C-B8980F757D22Q37528828-9C720524-471F-43A0-9A43-BBAA6DE397B9Q38673214-DC7DA1B3-14E5-41B4-8D3A-1092B37DA932Q39951932-F8BB9D4D-9979-4D52-A708-8DF358540C95Q41063256-3B7691A7-C53E-4F1E-A9A5-C01253F05DE3Q41893172-A5DF0C07-21B3-4B2C-8855-09FE1ED056FFQ42663820-D20DC425-878E-4404-81E0-5CF3EACA4367Q42732245-C1507A61-C28F-4CCC-A46E-F87EF67FF853Q44751023-0BD6933F-E3DB-4257-A94C-DAB2CC756445Q45175188-0C737AE2-429B-401C-8A51-8AB089606BA9Q45713863-A9631775-6B11-4049-95DF-B6893764774AQ45911365-8EF1658E-2B60-4057-8EBC-B9F41EDEE93BQ45917414-AF84F5E8-A81D-43EC-BC50-330F85E517B8Q48203509-E7E8CDC2-2728-4B33-A3FC-CDEBEA988FD7Q52368879-6DF862DD-11E4-47D0-A193-E5A8637C94B7Q52657401-33DD6132-4415-4864-8E15-69DE7573972CQ57187563-D139B284-4A8F-4A62-97AE-5D5F5F5C41AFQ57232194-8EF35F5F-7A04-4899-B950-1F8EFD5425ABQ57789647-42DD1DC4-967C-4601-A06A-C50B988276BAQ61800294-7A1423B5-1DB0-4FB1-8A9B-337DE962B48CQ63975908-90360360-A178-42DD-A13F-DA7E948E17C6Q80465752-2C3127CC-9AE0-41C4-A3AD-A92007FE3A0FQ89574793-AC5C28B1-114C-432B-B669-6C066E4DB50BQ91528080-BE0B6D0B-0A3B-4A3E-A07C-67EDC6EF950DQ92018669-2EE56F2D-3A01-4318-AE1D-FFAE09410CBB
P50
description
hulumtues
@sq
onderzoeker
@nl
researcher
@en
հետազոտող
@hy
name
Ralf Schmid
@ast
Ralf Schmid
@en
Ralf Schmid
@es
Ralf Schmid
@sl
type
label
Ralf Schmid
@ast
Ralf Schmid
@en
Ralf Schmid
@es
Ralf Schmid
@sl
prefLabel
Ralf Schmid
@ast
Ralf Schmid
@en
Ralf Schmid
@es
Ralf Schmid
@sl
P1053
E-6722-2011
P106
P21
P31
P3829
P496
0000-0002-0203-4023