about
Chelatases: distort to select?Structure of ribosomal protein TL5 complexed with RNA provides new insights into the CTC family of stress proteinsInterplay between an AAA module and an integrin I domain may regulate the function of magnesium chelataseMetal binding to Saccharomyces cerevisiae ferrochelataseMetal binding to Bacillus subtilis ferrochelatase and interaction between metal sitesCrystal structure of Plasmodium falciparum spermidine synthase in complex with the substrate decarboxylated S-adenosylmethionine and the potent inhibitors 4MCHA and AdoDATOInhibition of human DHODH by 4-hydroxycoumarins, fenamic acids, and N-(alkylcarbonyl)anthranilic acids identified by structure-guided fragment selectionATP-induced conformational dynamics in the AAA+ motor unit of magnesium chelataseOligomerization Propensity and Flexibility of Yeast Frataxin Studied by X-ray Crystallography and Small-Angle X-ray ScatteringThe Molecular Basis of Iron-induced Oligomerization of Frataxin and the Role of the Ferroxidation Reaction in OligomerizationCrystal structure of ferrochelatase: the terminal enzyme in heme biosynthesisIron superoxide dismutase from the archaeon Sulfolobus solfataricus: analysis of structure and thermostabilityStructural basis for interactions between tenascins and lectican C-type lectin domains: evidence for a crosslinking role for tenascinsA decade of progress in understanding the structural basis of protein synthesis.Resonance Raman Spectroscopic Examination of Ferrochelatase-induced Porphyrin Distortion.FERROCHELATASE: THE CONVERGENCE OF THE PORPHYRIN BIOSYNTHESIS AND IRON TRANSPORT PATHWAYSATPase activity associated with the magnesium chelatase H-subunit of the chlorophyll biosynthetic pathway is an artefact.A new cryo-EM single-particle ab initio reconstruction method visualizes secondary structure elements in an ATP-fueled AAA+ motor.The structures of frataxin oligomers reveal the mechanism for the delivery and detoxification of iron.SAXS and stability studies of iron-induced oligomers of bacterial frataxin CyaY.The AAA(+) motor complex of subunits CobS and CobT of cobaltochelatase visualized by single particle electron microscopy.Biochemical characterisation and novel classification of monofunctional S-adenosylmethionine decarboxylase of Plasmodium falciparum.Cloning, expression, characterisation and three-dimensional structure determination of Caenorhabditis elegans spermidine synthase.Iron-induced oligomerization of human FXN81-210 and bacterial CyaY frataxin and the effect of iron chelators.EM single particle analysis of the ATP-dependent BchI complex of magnesium chelatase: an AAA+ hexamer.Refined structure of Cu-substituted alcohol dehydrogenase at 2.1 A resolution.Ribosomal protein L22 from Thermus thermophilus: sequencing, overexpression and crystallisation.Recessiveness and dominance in barley mutants deficient in Mg-chelatase subunit D, an AAA protein involved in chlorophyll biosynthesis.Transmembrane topology of FRO2, a ferric chelate reductase from Arabidopsis thaliana.Crystallization and preliminary X-ray analysis of the Rhodobacter capsulatus magnesium chelatase BchI subunit.Crystallization and preliminary investigation of single crystals of deoxyuridine triphosphate nucleotidohydrolase from Escherichia coli.Three-dimensional structure of the crystalline surface layer from Aeromonas hydrophilaPurification, crystallization, and preliminary X-ray analysis of Bacillus subtilis ferrochelataseCrystallization and preliminary X-ray analysis of Thermotoga maritima ribosome recycling factorStructural aspects of protein synthesisRefined crystal structure of liver alcohol dehydrogenase-NADH complex at 1.8 A resolutionBacterial ferrochelatase turns human: Tyr13 determines the apparent metal specificity of Bacillus subtilis ferrochelataseTargeting Myeloid Differentiation Using Potent 2-Hydroxypyrazolo[1,5- a]pyridine Scaffold-Based Human Dihydroorotate Dehydrogenase Inhibitors4-Hydroxy-N-[3,5-bis(trifluoromethyl)phenyl]-1,2,5-thiadiazole-3-carboxamide: a novel inhibitor of the canonical NF-κB cascadeN-Acetyl-3-aminopyrazoles block the non-canonical NF-kB cascade by selectively inhibiting NIK
P50
Q24631143-69536C0D-2114-4AF8-86CA-F5B8F525BD5FQ27632703-9ABB7AE4-F87A-4C85-9D49-2F4F9A85EE10Q27633531-A35A2D21-43F9-43FA-B3AC-00269AC8E512Q27639939-2CDB9768-CCC2-4219-8666-17831BC7BD0BQ27641309-F1646292-5B50-4EDF-9FBB-0C8589B6E3A4Q27647920-C8A98D6E-6456-460E-9BA3-74EB61682364Q27660047-E559E26B-6CB2-4944-97C9-15532028EBB0Q27660194-51F06E78-78FD-433B-A406-420D77D63A3CQ27675367-873C7A78-D681-42D6-A030-802A215FE241Q27675978-B3A79247-7D8A-47C7-BD1E-A87FB25268D7Q27748178-7AF497BB-1491-4D63-9767-150F8C9491CFQ27766874-F2E985A7-10FB-4B8A-9E3A-6C211AD41B7DQ28568913-FA0C8EEE-C8C7-406C-91BB-F79532872EE0Q34013688-D1E0213C-D093-4B5F-8C86-08F10450D2D0Q35110484-633375FC-FB0B-4AC3-ABE8-D54FB29BB956Q35165701-F0582788-A3D1-431F-A7ED-1C607520F1A9Q41079895-861A6B4C-31C5-4BDD-B785-307773AE9675Q41623615-D714F2A5-A388-49C0-908F-88D4F2A27596Q41792116-2A76EE45-083A-46C5-BFAE-EBF7BF8D10DDQ42361550-6F3CFE1B-D3B9-4C51-BCB1-E11320BD3AD6Q43867240-29AED661-ADC5-4039-B9ED-417E2ACD1F9EQ44379242-469ACD08-27CC-44C7-B4F7-1FC9288D833AQ46754157-74459A03-888A-4B51-839D-DB9BBFB9D0B3Q47111560-D2CFE280-1338-409F-B4C2-D727FD7BD845Q47904796-A53B6F2C-6961-4B54-8160-1151D356B640Q47982954-6E7FC4BF-CAE6-4A41-8B05-005DEA643EF9Q48071517-1E17261A-08F8-481B-AE3F-637705A33985Q48082964-81D5211A-9DAD-45C5-A797-3E8E3AD7649EQ51163217-7F2BC200-7031-4436-BCA6-8B918C81E75CQ54705856-36EA17E5-A7E5-48E6-960F-D35E0B2FE062Q54757151-05C8F8D0-F0A8-47E0-B77C-5EFF181F210CQ68073874-1FAC86D2-DFEF-4572-B0B3-6F4163B7B581Q71374372-9FC4DF65-C75B-4CFC-A64F-2499544305FFQ73427749-483CED3C-C1C4-41B1-9075-38A3061CD45EQ73798329-42825904-5DC7-4BCA-BE8F-59DE78840FD1Q80426166-CCD71B90-1782-4A42-8AC2-E8DFD847313AQ82322229-0F4D8BBC-9F1B-426A-9370-8319D452EFBCQ89232967-8DD7D87C-6B79-4798-9BB8-1323714F630CQ90950349-9CFB829A-FD21-4C43-B82D-FE5799660693Q90951088-D7182E63-2BEF-4AF7-825D-E3B5BDF93CC7
P50
description
hulumtues
@sq
researcher
@en
wetenschapper
@nl
հետազոտող
@hy
name
Salam Al-Karadaghi
@ast
Salam Al-Karadaghi
@en
Salam Al-Karadaghi
@es
Salam Al-Karadaghi
@nl
Salam Al-Karadaghi
@sl
type
label
Salam Al-Karadaghi
@ast
Salam Al-Karadaghi
@en
Salam Al-Karadaghi
@es
Salam Al-Karadaghi
@nl
Salam Al-Karadaghi
@sl
altLabel
Salam Al-Karadaghi
@en
prefLabel
Salam Al-Karadaghi
@ast
Salam Al-Karadaghi
@en
Salam Al-Karadaghi
@es
Salam Al-Karadaghi
@nl
Salam Al-Karadaghi
@sl
P1053
F-1492-2011
P106
P108
P21
P31
P3829
P496
0000-0001-8608-0635
P569
2000-01-01T00:00:00Z