about
Comparative structural analysis of lipid binding START domainsZinc binding catalytic domain of human tankyrase 1Structure of Escherichia coli pyruvate formate-lyase with pyruvateThe structure ofPseudomonasP51 Cl-muconate lactonizing enzyme: Co-evolution of structure and dynamics with the dehalogenation functionStructure of theStreptococcus agalactiaefamily II inorganic pyrophosphatase at 2.80 Å resolutionStructure of Streptococcus agalactiae serine/threonine phosphataseCrystal structure of the N-terminal NC4 domain of collagen IX, a zinc binding member of the laminin-neurexin-sex hormone binding globulin (LNS) domain familyCompleting the family portrait of the anti-apoptotic Bcl-2 proteins: crystal structure of human Bfl-1 in complex with BimThe DEXD/H-box RNA Helicase DDX19 Is Regulated by an -Helical SwitchStructural basis for inhibitor specificity in human poly(ADP-ribose) polymerase-3Crystal Structures of the ATPase Domains of Four Human Hsp70 Isoforms: HSPA1L/Hsp70-hom, HSPA2/Hsp70-2, HSPA6/Hsp70B', and HSPA5/BiP/GRP78Structural Determination of Functional Domains in Early B-cell Factor (EBF) Family of Transcription Factors Reveals Similarities to Rel DNA-binding Proteins and a Novel Dimerization MotifStructural studies of tri-functional human GARTStructural basis of selective inhibition of human tankyrasesStructural basis and selectivity of tankyrase inhibition by a Wnt signaling inhibitor WIKI4Evaluation and Structural Basis for the Inhibition of Tankyrases by PARP InhibitorsScreening and structural analysis of flavones inhibiting tankyrasesStructural Basis for Regulation of the Human Acetyl-CoA Thioesterase 12 and Interactions with the Steroidogenic Acute Regulatory Protein-related Lipid Transfer (START) DomainSubstrate specificity and oligomerization of human GMP synthetaseDiscovery of tankyrase inhibiting flavones with increased potency and isoenzyme selectivitypara-Substituted 2-phenyl-3,4-dihydroquinazolin-4-ones as potent and selective tankyrase inhibitorsStructure-based design, synthesis and evaluation in vitro of arylnaphthyridinones, arylpyridopyrimidinones and their tetrahydro derivatives as inhibitors of the tankyrasesDiscovery of potent and selective nonplanar tankyrase inhibiting nicotinamide mimicsExploration of the nicotinamide-binding site of the tankyrases, identifying 3-arylisoquinolin-1-ones as potent and selective inhibitors in vitroDevelopment and structural analysis of adenosine site binding tankyrase inhibitorsStructure-activity relationships of 2-arylquinazolin-4-ones as highly selective and potent inhibitors of the tankyrasesInhibition of poly(ADP-ribose) polymerase interferes with Trypanosoma cruzi infection and proliferation of the parasiteStructural studies of metal ions in family II pyrophosphatases: the requirement for a Janus ion.The crystal structure of the Dachshund domain of human SnoN reveals flexibility in the putative protein interaction surface.Homogeneous screening assay for human tankyrase.Crystallization and preliminary crystallographic analysis of two Streptococcus agalactiae proteins: the family II inorganic pyrophosphatase and the serine/threonine phosphataseDisrupted ADP-ribose metabolism with nuclear Poly (ADP-ribose) accumulation leads to different cell death pathways in presence of hydrogen peroxide in procyclic Trypanosoma brucei.Tankyrases as drug targets.Tankyrases: structure, function and therapeutic implications in cancer.Characterization of the DNA dependent activation of human ARTD2/PARP2.Highly Potent and Isoform Selective Dual Site Binding Tankyrase/Wnt Signaling Inhibitors That Increase Cellular Glucose Uptake and Have Antiproliferative Activity.PARP-3 is a mono-ADP-ribosylase that activates PARP-1 in the absence of DNAProximal ADP-ribose Hydrolysis in Trypanosomatids is Catalyzed by a Macrodomain.Structural and Biochemical Characterization of Poly-ADP-ribose Polymerase from Trypanosoma bruceiCrystal structure of a glycyl radical enzyme from Archaeoglobus fulgidus.
P50
Q21135464-403CBA06-B397-4305-9D5A-B115BC75E758Q24328797-31B84003-76B5-4E51-A8DD-661591212BBFQ27640044-AB3A3D70-4389-4D87-B870-6CE373D265DDQ27641881-86B35740-27E4-43E5-A620-FDA27FF988A8Q27644799-60C63CDD-93ED-4D78-A9A3-83FF1B03C7A0Q27644852-2BF5DE60-41E1-475A-AC91-C864319FF864Q27645307-D997F6E7-4B2D-46F4-9B4E-44FA83AB6F5AQ27652276-163EA12F-B691-419F-9AE6-4A757364BC35Q27653950-A3E0A839-8AEF-4633-81C3-2AC0364CE92FQ27654592-44E9FB39-2A5E-4C22-8D06-80DB9CE1F7AAQ27658953-5B3822D1-D210-4E2B-ADDD-9742C763A7DFQ27662927-AC5BA9DC-BA1D-4D34-9935-292D2F4EE75EQ27663462-5D9EA2B4-121F-463A-99FF-9FA20FDAAE08Q27676673-2D3675DC-DAF7-482A-A76B-07C54695EDCEQ27678604-217D4EDD-5276-4AC4-8D01-F206E2BC1EE5Q27684215-2B7892C8-708B-4A7B-A921-DD7CD32EB377Q27684395-ADC2E4A4-5DDB-4AFD-B038-C65EA07457DEQ27684584-E2DDAEBA-30AF-4016-8B41-AC95060F3FD5Q27685162-7007F9E2-F27B-4830-B576-E23C02313ED6Q27687124-C833DCAF-6174-48A9-9CF2-2C55B51A23B3Q27687215-8EAA8F1E-BB75-414E-A6C4-E91BFFB33943Q27700926-A29161FE-EFC6-4FE3-8BE7-8BA71310C066Q27701567-879F9EF1-A235-4EDD-B68B-A6DE69F9A1E4Q27701575-2AF83B7F-5CBA-43E2-B886-B5E0D9C4DE65Q27703255-9A9E703A-D2D4-47C9-A750-F8EAEA8ACECFQ27704836-2AD6A8BB-3D35-456C-9C1C-228C5957DD8AQ28483989-FCA45784-5D70-49F1-815E-89CE071C87C9Q30975729-AFCB941B-0C59-40D3-BDBD-AB6909383E01Q33721809-7940409B-2C83-4F0A-B750-E7BEC2063BE1Q34167299-84EFFCC9-FEE3-42CD-B08D-788DF4B32CD6Q36459423-3E353FAF-C6B3-401F-A006-8E7F3C485D9EQ36725115-78BEC7C4-27A8-4065-8BFA-3174339BACB0Q38104494-D07980B0-0F06-4E5A-89D6-59F7067C8ACAQ38224266-148C4EDE-8BC3-44F9-B974-1985790A111BQ38290704-564866E4-4A45-43F1-BC83-A4B9BA8D344AQ38725895-01D81B1B-2056-4C1E-8F46-3F8D899076CDQ39430828-D5F629F2-2E26-434C-B31A-010866ACE375Q40017593-77A9F580-1AFC-4551-8540-BEFE89E1BD6BQ42041151-71FA1EDB-DA48-4604-A5C8-93C3B463CFC2Q42170557-4F41A859-42A8-458F-B1CC-463D52FAC1D2
P50
description
Finnish biochemist and researcher, PhD, associate professor (Univ, of Oulu)
@en
bioquímicu finlandés
@ast
finnischer Biochemiker
@de
suomalainen biokemisti ja tutkija, dosentti, Oulun yliopiston apulaisprofessori
@fi
name
Lari Lehtiö
@ast
Lari Lehtiö
@ca
Lari Lehtiö
@en
Lari Lehtiö
@es
Lari Lehtiö
@fi
Lari Lehtiö
@fr
Lari Lehtiö
@ga
Lari Lehtiö
@nl
Lari Lehtiö
@sl
Lari Lehtiö
@sq
type
label
Lari Lehtiö
@ast
Lari Lehtiö
@ca
Lari Lehtiö
@en
Lari Lehtiö
@es
Lari Lehtiö
@fi
Lari Lehtiö
@fr
Lari Lehtiö
@ga
Lari Lehtiö
@nl
Lari Lehtiö
@sl
Lari Lehtiö
@sq
prefLabel
Lari Lehtiö
@ast
Lari Lehtiö
@ca
Lari Lehtiö
@en
Lari Lehtiö
@es
Lari Lehtiö
@fi
Lari Lehtiö
@fr
Lari Lehtiö
@ga
Lari Lehtiö
@nl
Lari Lehtiö
@sl
Lari Lehtiö
@sq
P106
P21
P27
P31
P496
0000-0001-7250-832X
P569
2000-01-01T00:00:00Z