about
Antibodies to the buried N terminus of rhinovirus VP4 exhibit cross-serotypic neutralizationThe structure of bovine glutamate dehydrogenase provides insights into the mechanism of allosteryThe structure of cucumber mosaic virus and comparison to cowpea chlorotic mottle virusStructures of bovine glutamate dehydrogenase complexes elucidate the mechanism of purine regulationThe structure of apo human glutamate dehydrogenase details subunit communication and allosteryStructural studies on ADP activation of mammalian glutamate dehydrogenase and the evolution of regulationStructural determinants of metal specificity in the zinc transport protein ZnuA from synechocystis 6803Possible regulatory role for the histidine-rich loop in the zinc transport protein, ZnuAThe structure of the iron-binding protein, FutA1, from Synechocystis 6803Starch Catabolism by a Prominent Human Gut Symbiont Is Directed by the Recognition of Amylose HelicesStructure of a SusD Homologue, BT1043, Involved in Mucin O -Glycan Utilization in a Prominent Human Gut Symbiont † , ‡Novel Inhibitors Complexed with Glutamate Dehydrogenase: ALLOSTERIC REGULATION BY CONTROL OF PROTEIN DYNAMICSSusG: a unique cell-membrane-associated alpha-amylase from a prominent human gut symbiont targets complex starch moleculesHigh-Resolution X-Ray Structure and Functional Analysis of the Murine Norovirus 1 Capsid Protein Protruding DomainAtomic Structure of Salutaridine Reductase from the Opium Poppy (Papaver somniferum)A novel mechanism of V-type zinc inhibition of glutamate dehydrogenase results from disruption of subunit interactions necessary for efficient catalysisGreen Tea Polyphenols Control Dysregulated Glutamate Dehydrogenase in Transgenic Mice by Hijacking the ADP Activation SiteMultidomain Carbohydrate-binding Proteins Involved in Bacteroides thetaiotaomicron Starch MetabolismStructural Basis for Broad Detection of Genogroup II Noroviruses by a Monoclonal Antibody That Binds to a Site Occluded in the Viral ParticleThe atomic structure of the virally encoded antifungal protein, KP6Identification of viral mutants by mass spectrometry.Human rhinovirus capsid dynamics is controlled by canyon flexibility.Pocket factors are unlikely to play a major role in the life cycle of human rhinovirus.Crystallization and preliminary X-ray diffraction analysis of salutaridine reductase from the opium poppy Papaver somniferumPutative receptor binding sites on alphaviruses as visualized by cryoelectron microscopyHigh-resolution cryo-electron microscopy structures of murine norovirus 1 and rabbit hemorrhagic disease virus reveal marked flexibility in the receptor binding domains.Structure-activity determinants in antifungal plant defensins MsDef1 and MtDef4 with different modes of action against Fusarium graminearum.Neutralizing antibody to human rhinovirus 14 penetrates the receptor-binding canyon.Mechanism of hyperinsulinism in short-chain 3-hydroxyacyl-CoA dehydrogenase deficiency involves activation of glutamate dehydrogenaseViral capsid mobility: a dynamic conduit for inactivation.Atomic structure of a nitrate-binding protein crucial for photosynthetic productivityStructural studies on antibody-virus complexes.The structure and allosteric regulation of mammalian glutamate dehydrogenase.Aggregation of TMV CP plays a role in CP functions and in coat-protein-mediated resistanceStructure of antibody-neutralized murine norovirus and unexpected differences from viruslike particlesAntiviral agent blocks breathing of the common cold virus.High throughput screening reveals several new classes of glutamate dehydrogenase inhibitorsUntangling the glutamate dehydrogenase allosteric nightmare.Complex glycan catabolism by the human gut microbiota: the Bacteroidetes Sus-like paradigm.The structure and allosteric regulation of glutamate dehydrogenase.
P50
Q24654597-E5CDE2F4-6A49-40E2-AB1A-C3CA4A35EBC4Q27619175-E3ECDB6C-897E-4961-A3D1-8D3CC6AF2EA4Q27625479-7608724A-6D64-4FA9-87F7-16F5A970E849Q27630686-999B97DC-1E6A-49CD-870A-90CB1F8E6038Q27639129-6BDCAD71-19E6-4306-96E4-9743491395A1Q27640767-6D2CE5A7-2E55-4F4E-A6E9-DCB266162865Q27642442-59503FCD-C06D-49BD-9BCB-8375132314B5Q27646575-45C30829-C224-4D6C-9C5D-CD8161C06196Q27646638-17958C01-6ADF-405D-B115-92CADC420950Q27651083-3E3527D5-C525-43EC-AA4C-009F2B9E1CA8Q27653641-67707133-B075-4565-A055-66DF48BFC750Q27655990-617B0D08-BD5C-4153-A136-1E78F0C1E21DQ27659874-4C40D73B-12D4-42AC-ABD3-BB9C77994084Q27660321-CD234D6E-63A9-4CBB-A6C1-9B7F48CD99AFQ27666343-336DB76B-BD73-4DB6-8FE3-B1DC9A82C078Q27670767-4DBE9E93-ECE9-43AD-BC38-A70CD9BA170CQ27671504-C55CF18F-0C77-4439-BED2-057B279945BBQ27671644-4FC95BD7-5EDF-4AC1-8988-AF94C5A26A30Q27676892-F1FA47AD-79B7-433F-BDF7-4F4222F48378Q27683566-3C6E73CF-C0DF-48D7-BA23-725FC50B8ADDQ32052200-5ED06581-E0BC-4389-BFFF-B8DC62CB5982Q33193490-2A6D8E4F-AFF2-483D-902B-0D08BDC12B86Q33281854-AF1B4C35-EE54-464B-B859-F63758877B24Q33627634-64A49EFC-70D2-4C61-960B-9C37C70185FBQ33791727-1DC190DA-C4E3-4CD4-81EA-2B2F82B0AF61Q33877306-DC9B9F3E-531A-49C1-9CEC-AF1026B58B49Q33886808-9F8D9B0D-7851-48A4-AEE9-792AC141AB92Q34063398-E9454472-0F11-464A-A39B-A071EE4CCE5CQ34181596-5FA4546B-D868-43BF-A4AE-4D74ABE7CDF4Q34451722-A140FCF9-4C1D-49D5-BB8B-AF1A2A9BEF27Q34772837-FD4FB539-942E-4F8B-8913-1B8E62B1AB3DQ35291103-42C856EF-C466-48AC-ADBD-A61BB1C44256Q35803204-EB2081AB-A938-451D-8163-EDB00D4C6842Q36082981-96F63508-37F0-4222-A746-CCCB03F89190Q36483872-236CA98E-E4AB-485A-B1FD-E97005230242Q36489398-867C540B-B4A1-4CCE-A6EF-98556F95D6B4Q36736887-C023FC36-94F0-42AC-B1CD-B47218D095E5Q37280168-3D0A4832-B42A-4CA3-8BA6-48CC965B6795Q37375609-0320C616-23A5-4F5D-B6B7-F4D4F669F67EQ37808783-A9E31CE3-8C77-4D54-9CFE-656CD9BA469D
P50
description
researcher at Donald Danforth Plant Science Center
@en
հետազոտող
@hy
name
Thomas J Smith
@nl
Thomas J Smith
@sl
Thomas J. Smith
@en
Thomas J. Smith
@es
type
label
Thomas J Smith
@nl
Thomas J Smith
@sl
Thomas J. Smith
@en
Thomas J. Smith
@es
prefLabel
Thomas J Smith
@nl
Thomas J Smith
@sl
Thomas J. Smith
@en
Thomas J. Smith
@es
P1053
K-9086-2013
P106
P1153
35406650200
P21
P31
P3829
P496
0000-0003-3528-6793