about
Structure of the putative mutarotase YeaD from Salmonella typhimurium: structural comparison with galactose mutarotasesCrystal structure of Salmonella typhimurium 2-methylcitrate synthase: Insights on domain movement and substrate specificityStructural and mechanistic investigations on Salmonella typhimurium acetate kinase (AckA): identification of a putative ligand binding pocket at the dimeric interfaceAnions Mediate Ligand Binding in Adineta vaga Glutamate Receptor Ion ChannelsMechanistic features of Salmonella typhimurium propionate kinase (TdcD): insights from kinetic and crystallographic studiesStructures of substrate- and nucleotide-bound propionate kinase from Salmonella typhimurium: substrate specificity and phosphate-transfer mechanismStructural basis of kainate subtype glutamate receptor desensitization.Structural mechanism of glutamate receptor activation and desensitization.Self-assembled monolayers improve protein distribution on holey carbon cryo-EM supports.Structure and function of enzymes involved in the anaerobic degradation of L-threonine to propionate.Preliminary X-ray crystallographic studies on acetate kinase (AckA) from Salmonella typhimurium in two crystal forms.Preliminary X-ray crystallographic analysis of 2-methylcitrate synthase from Salmonella typhimurium.Crystallization and preliminary X-ray crystallographic analysis of biodegradative threonine deaminase (TdcB) from Salmonella typhimurium.Tyrosine 66 of Pepper vein banding virus genome-linked protein is uridylylated by RNA-dependent RNA polymerase.Preferential assembly of heteromeric kainate and AMPA receptor amino terminal domains.Structural mechanisms of centromeric nucleosome recognition by the kinetochore protein CENP-N.Cryo-EM structures reveal coordinated domain motions that govern DNA cleavage by Cas9Structure of the primed state of the ATPase domain of chromatin remodeling factor ISWI bound to the nucleosomeA Tail-Based Mechanism Drives Nucleosome Demethylation by the LSD2/NPAC Multimeric Complex
P50
Q27643622-DBA6485A-207F-4F3A-9DBE-716EEC262EA6Q27665327-A57ECF4F-1730-4AB8-9C19-FEF743B98CCDQ27674016-849B4985-D53B-459C-B742-1EACE559723EQ27676573-647A931F-079E-4410-845D-CAD5B64B555BQ27684786-B5F45FCF-E3C4-434D-868A-441FE838ED8CQ27701748-83DB5940-8E02-40A2-A42F-A83700CF4B03Q27727973-8B6B00B4-75D3-4855-B1B1-6C0455B7D4EFQ30593263-A3D600DE-BF1D-4A9F-9FBE-F9DE65F6D995Q34529888-F34543C7-4E10-4FC8-B263-AEB18146EFAEQ36978789-2EF06E11-B7EF-4A45-9850-58D5D5CF9D25Q39643695-04093F9B-7D54-4549-9653-4C7718DD1922Q39969694-BA3A0CF2-5A2E-45C3-A39D-D48E4B949B5FQ42113580-B2714676-D168-43FA-9521-016A42D8AF1EQ45466393-D435B91A-CAF2-4B7E-915E-8ECBC9D9E24CQ47100457-08055EA8-B12A-4BC8-A308-DFE0382BB6D9Q47263134-5C4606C4-9F9C-422B-A660-14435C8E8E4CQ91724077-C9FBF7CC-A451-4E1E-8AF3-14A1720FE0C3Q92552709-D79F0E09-08B9-4F49-9942-8F4C31CE8D7BQ93003173-67BE2DD8-7E94-445B-A674-341AFF5192B6
P50
description
researcher
@en
wetenschapper
@nl
հետազոտող
@hy
name
Sagar Chittori
@ast
Sagar Chittori
@en
Sagar Chittori
@es
Sagar Chittori
@nl
Sagar Chittori
@sl
type
label
Sagar Chittori
@ast
Sagar Chittori
@en
Sagar Chittori
@es
Sagar Chittori
@nl
Sagar Chittori
@sl
prefLabel
Sagar Chittori
@ast
Sagar Chittori
@en
Sagar Chittori
@es
Sagar Chittori
@nl
Sagar Chittori
@sl
P106
P1153
8603190900
P1960
c1uFXRUAAAAJ
P2038
Sagar_Chittori
P31
P4012
P496
0000-0003-1417-6552
P569
2000-01-01T00:00:00Z