about
Crystal structures of a purple acid phosphatase, representing different steps of this enzyme's catalytic cycleThe crystal structure of free human hypoxanthine-guanine phosphoribosyltransferase reveals extensive conformational plasticity throughout the catalytic cycleInhibition of hypoxanthine-guanine phosphoribosyltransferase by acyclic nucleoside phosphonates: a new class of antimalarial therapeuticsHerbicide-binding sites revealed in the structure of plant acetohydroxyacid synthaseCrystal structure of yeast acetohydroxyacid synthase: a target for herbicidal inhibitorsThree-dimensional structure of an immunoglobulin light-chain dimer with amyloidogenic propertiesStructure of CcmG/DsbE at 1.14 A resolution: high-fidelity reducing activity in an indiscriminately oxidizing environmentThe crystal structures of Klebsiella pneumoniae acetolactate synthase with enzyme-bound cofactor and with an unusual intermediateCrystal structures of two novel sulfonylurea herbicides in complex with Arabidopsis thaliana acetohydroxyacid synthaseCrystal structure of textilinin-1, a Kunitz-type serine protease inhibitor from the venom of the Australian common brown snake (Pseudonaja textilis)The organophosphate-degrading enzyme from Agrobacterium radiobacter displays mechanistic flexibility for catalysisPhosphate-bound structure of an organophosphate-degrading enzyme from Agrobacterium radiobacterBacterial and plant ketol-acid reductoisomerases have different mechanisms of induced fit during the catalytic cycleAcyclic nucleoside phosphonates containing a second phosphonate group are potent inhibitors of 6-oxopurine phosphoribosyltransferases and have antimalarial activityRole of human hypoxanthine guanine phosphoribosyltransferase in activation of the antiviral agent T-705 (favipiravir)Inhibition of the Escherichia coli 6-oxopurine phosphoribosyltransferases by nucleoside phosphonates: potential for new antibacterial agentsAza-acyclic nucleoside phosphonates containing a second phosphonate group as inhibitors of the human, Plasmodium falciparum and vivax 6-oxopurine phosphoribosyltransferases and their prodrugs as antimalarial agentsCommercial Herbicides Can Trigger the Oxidative Inactivation of Acetohydroxyacid SynthaseThree-dimensional structure of the alpha-conotoxin GI at 1.2 A resolutionThree-dimensional structure of a human Fab with high affinity for tetanus toxoidSystematic characterization of mutations in yeast acetohydroxyacid synthase. Interpretation of herbicide-resistance data.Structure-activity relationships for a new family of sulfonylurea herbicides.Identification of a non-purple tartrate-resistant acid phosphatase: an evolutionary link to Ser/Thr protein phosphatases?Phosphate forms an unusual tripodal complex with the Fe-Mn center of sweet potato purple acid phosphatase.A focused sulfated glycoconjugate Ugi library for probing heparan sulfate-binding angiogenic growth factors.Structure and mechanism of inhibition of plant acetohydroxyacid synthase.The crystal structure of a bacterial class II ketol-acid reductoisomerase: domain conservation and evolution.The catalytic mechanisms of binuclear metallohydrolases.6-oxopurine phosphoribosyltransferase: a target for the development of antimalarial drugs.Binuclear metallohydrolases: complex mechanistic strategies for a simple chemical reaction.The applications of binuclear metallohydrolases in medicine: recent advances in the design and development of novel drug leads for purple acid phosphatases, metallo-β-lactamases and arginases.Characterization and structural analysis of a potent anticoagulant phospholipase A2 from Pseudechis australis snake venom.Structural aspects of conformational changes in ligand binding by antibody fragments.The effect of novel [3-fluoro-(2-phosphonoethoxy)propyl]purines on the inhibition of Plasmodium falciparum, Plasmodium vivax and human hypoxanthine-guanine-(xanthine) phosphoribosyltransferases.Sulfonylureas have antifungal activity and are potent inhibitors of Candida albicans acetohydroxyacid synthase.Synthesis of novel N-branched acyclic nucleoside phosphonates as potent and selective inhibitors of human, Plasmodium falciparum and Plasmodium vivax 6-oxopurine phosphoribosyltransferases.Synthesis of 9-phosphonoalkyl and 9-phosphonoalkoxyalkyl purines: evaluation of their ability to act as inhibitors of Plasmodium falciparum, Plasmodium vivax and human hypoxanthine-guanine-(xanthine) phosphoribosyltransferases.Plasmodium vivax hypoxanthine-guanine phosphoribosyltransferase: a target for anti-malarial chemotherapy.Crystallization and preliminary X-ray analysis of a Kunitz-type inhibitor, textilinin-1 from Pseudonaja textilis textilis.Synthesis of branched 9-[2-(2-phosphonoethoxy)ethyl]purines as a new class of acyclic nucleoside phosphonates which inhibit Plasmodium falciparum hypoxanthine-guanine-xanthine phosphoribosyltransferase.
P50
Q21256411-0044B4E5-3579-44DE-941B-2901368D1643Q24306496-0401FF9D-B41A-4BFF-9DFD-335B8EA55632Q24338428-D18C541C-3556-480B-A354-FBB687AAE4E7Q24536540-7E160DB6-A60C-42CA-8209-01878F4415C0Q27638401-6905FC55-CD2A-4A94-B403-B8E5970E9375Q27638904-F1788EE8-CA36-41C3-AC69-DE57C83274CBQ27639369-95781B4C-FCEB-476D-8484-AFC06A46CD17Q27642352-43B7996F-698C-47AD-9265-E6F1CDB73EA3Q27653623-97CB1C62-4EC1-44B8-9E05-98ABCD0DEC7DQ27655713-805437BA-1595-472D-BB89-7C0EDE519A41Q27664660-2DE31898-97CC-44B1-B041-D0CD6FAAA098Q27675780-9EA9AADA-8647-4612-9E92-07FF04FDC476Q27682670-75C47DB3-0CF6-44EB-B775-FAA8DFF60917Q27684093-3E32EE6D-6E89-4240-ABD6-20D867A37FCBQ27685318-A5E978C7-A3AB-4754-87E7-C560D086887BQ27685350-DF38459F-9437-4B58-8874-1D2BF67DEFD0Q27696829-37998283-8549-4688-8910-259D8177E95FQ27704198-13DA06DE-268D-45A3-8E94-435F5E543C84Q27733331-B9668976-8814-4612-B67B-EBB0BB87EF04Q27749024-F3BB3348-4501-484B-8916-E36AB394D63FQ30806344-7BB9EC1E-4D75-4F52-9047-6986EFA8E0FBQ33230213-B9F6397C-BBF3-44D1-98D0-12240F528369Q33366856-1CA9E3D7-8A16-4D2F-AA29-943795E7BBC3Q33723112-8CB0B8E8-F1FC-4D70-B59F-A67AD20AAF96Q34396718-2488EE9A-51AC-48C1-A1F2-9839CBB6F23DQ34743495-A2E841BA-086F-4808-A7A5-D502BA39158CQ36476590-A20183B1-B63D-4ABA-83E1-C65BD3DE4330Q36559654-3E522440-6577-4948-8FAA-BBD410883E43Q37880921-377F7BA9-19FD-4BEB-B918-B3573E08CA12Q38018749-2EF2F3C4-B4AC-45FC-BE22-CA9CD8352DE2Q38192387-5B1297AD-A8C5-4B44-AABF-45BB54E73AE7Q40127191-EDE09FB8-67B7-4A86-ACB9-B166C02B0D81Q40659726-D9F1692C-65B3-4DE9-A56A-C6B112D9D077Q42710276-CE4977A6-4E10-47A3-B07E-AC7932DC6330Q42713822-4406EFD5-BBC2-49BD-8FE9-9893A546BCFEQ42717330-662C8A4C-5D59-4D7F-85FE-5C2E75C163EEQ42722793-8A881538-38CA-45D0-88A3-3262C24DE4ADQ42994704-98A52043-9B60-4449-A414-8B9E52CF4188Q43044053-3B685581-A8B3-4E8A-9157-1B91D41125BCQ43295327-B8CE1379-33F7-4363-8B14-E477A9FDA524
P50
description
hulumtues
@sq
researcher
@en
wetenschapper
@nl
հետազոտող
@hy
name
Luke W Guddat
@es
Luke W. Guddat
@en
Luke W. Guddat
@nl
Luke W. Guddat
@sl
type
label
Luke W Guddat
@es
Luke W. Guddat
@en
Luke W. Guddat
@nl
Luke W. Guddat
@sl
prefLabel
Luke W Guddat
@es
Luke W. Guddat
@en
Luke W. Guddat
@nl
Luke W. Guddat
@sl
P106
P1153
7004857189
P21
P31
P496
0000-0002-8204-8408
P5008
P569
2000-01-01T00:00:00Z