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165 related items for PubMed ID: 16195543
1. Solution structure of the low-molecular-weight protein tyrosine phosphatase from Tritrichomonas foetus reveals a flexible phosphate binding loop. Gustafson CL, Stauffacher CV, Hallenga K, Van Etten RL. Protein Sci; 2005 Oct; 14(10):2515-25. PubMed ID: 16195543 [Abstract] [Full Text] [Related]
2. Kinetic and spectroscopic studies of Tritrichomonas foetus low-molecular weight phosphotyrosyl phosphatase. Hydrogen bond networks and electrostatic effects. Thomas CL, McKinnon E, Granger BL, Harms E, Van Etten RL. Biochemistry; 2002 Dec 31; 41(52):15601-9. PubMed ID: 12501188 [Abstract] [Full Text] [Related]
3. Altering the purine specificity of hypoxanthine-guanine-xanthine phosphoribosyltransferase from Tritrichomonas foetus by structure-based point mutations in the enzyme protein. Munagala NR, Wang CC. Biochemistry; 1998 Nov 24; 37(47):16612-9. PubMed ID: 9843428 [Abstract] [Full Text] [Related]
4. Role of the flexible loop of hypoxanthine-guanine-xanthine phosphoribosyltransferase from Tritrichomonas foetus in enzyme catalysis. Munagala N, Basus VJ, Wang CC. Biochemistry; 2001 Apr 10; 40(14):4303-11. PubMed ID: 11284686 [Abstract] [Full Text] [Related]
5. Solution structure of a low-molecular-weight protein tyrosine phosphatase from Bacillus subtilis. Xu H, Xia B, Jin C. J Bacteriol; 2006 Feb 10; 188(4):1509-17. PubMed ID: 16452434 [Abstract] [Full Text] [Related]
6. The apo-structure of the low molecular weight protein-tyrosine phosphatase A (MptpA) from Mycobacterium tuberculosis allows for better target-specific drug development. Stehle T, Sreeramulu S, Löhr F, Richter C, Saxena K, Jonker HR, Schwalbe H. J Biol Chem; 2012 Oct 05; 287(41):34569-82. PubMed ID: 22888002 [Abstract] [Full Text] [Related]
7. Structural Insights into the Active Site Formation of DUSP22 in N-loop-containing Protein Tyrosine Phosphatases. Lai CH, Chang CC, Chuang HC, Tan TH, Lyu PC. Int J Mol Sci; 2020 Oct 12; 21(20):. PubMed ID: 33053837 [Abstract] [Full Text] [Related]
8. Site-directed mutagenesis, kinetic, and spectroscopic studies of the P-loop residues in a low molecular weight protein tyrosine phosphatase. Evans B, Tishmack PA, Pokalsky C, Zhang M, Van Etten RL. Biochemistry; 1996 Oct 22; 35(42):13609-17. PubMed ID: 8885840 [Abstract] [Full Text] [Related]
9. Conservative tryptophan mutants of the protein tyrosine phosphatase YopH exhibit impaired WPD-loop function and crystallize with divanadate esters in their active sites. Moise G, Gallup NM, Alexandrova AN, Hengge AC, Johnson SJ. Biochemistry; 2015 Oct 27; 54(42):6490-500. PubMed ID: 26445170 [Abstract] [Full Text] [Related]
10. Three-dimensional structure and ligand interactions of the low molecular weight protein tyrosine phosphatase from Campylobacter jejuni. Tolkatchev D, Shaykhutdinov R, Xu P, Plamondon J, Watson DC, Young NM, Ni F. Protein Sci; 2006 Oct 27; 15(10):2381-94. PubMed ID: 17008719 [Abstract] [Full Text] [Related]
11. Crystal structure of a ternary complex of Tritrichomonas foetus inosine 5'-monophosphate dehydrogenase: NAD+ orients the active site loop for catalysis. Gan L, Petsko GA, Hedstrom L. Biochemistry; 2002 Nov 05; 41(44):13309-17. PubMed ID: 12403633 [Abstract] [Full Text] [Related]
12. Mechanistic studies on protein tyrosine phosphatases. Zhang ZY. Prog Nucleic Acid Res Mol Biol; 2003 Nov 05; 73():171-220. PubMed ID: 12882518 [Abstract] [Full Text] [Related]
13. Structural basis of the tight binding of pyridoxal 5'-phosphate to a low molecular weight protein tyrosine phosphatase. Zhou M, Van Etten RL. Biochemistry; 1999 Mar 02; 38(9):2636-46. PubMed ID: 10052933 [Abstract] [Full Text] [Related]
14. Probing the molecular basis for potent and selective protein-tyrosine phosphatase 1B inhibition. Guo XL, Shen K, Wang F, Lawrence DS, Zhang ZY. J Biol Chem; 2002 Oct 25; 277(43):41014-22. PubMed ID: 12193602 [Abstract] [Full Text] [Related]
15. Crystal structure and putative substrate identification for the Entamoeba histolytica low molecular weight tyrosine phosphatase. Linford AS, Jiang NM, Edwards TE, Sherman NE, Van Voorhis WC, Stewart LJ, Myler PJ, Staker BL, Petri WA. Mol Biochem Parasitol; 2014 Jan 25; 193(1):33-44. PubMed ID: 24548880 [Abstract] [Full Text] [Related]
16. Conformational and dynamic changes of Yersinia protein tyrosine phosphatase induced by ligand binding and active site mutation and revealed by H/D exchange and electrospray ionization Fourier transform ion cyclotron resonance mass spectrometry. Wang F, Li W, Emmett MR, Hendrickson CL, Marshall AG, Zhang YL, Wu L, Zhang ZY. Biochemistry; 1998 Nov 03; 37(44):15289-99. PubMed ID: 9799489 [Abstract] [Full Text] [Related]
17. Crystal structure of Tritrichomonas foetus inosine monophosphate dehydrogenase in complex with the inhibitor ribavirin monophosphate reveals a catalysis-dependent ion-binding site. Prosise GL, Wu JZ, Luecke H. J Biol Chem; 2002 Dec 27; 277(52):50654-9. PubMed ID: 12235158 [Abstract] [Full Text] [Related]
18. Electrostatic evaluation of the signature motif (H/V)CX5R(S/T) in protein-tyrosine phosphatases. Peters GH, Frimurer TM, Olsen OH. Biochemistry; 1998 Apr 21; 37(16):5383-93. PubMed ID: 9548920 [Abstract] [Full Text] [Related]
19. Kinetic and site-directed mutagenesis studies of the cysteine residues of bovine low molecular weight phosphotyrosyl protein phosphatase. Davis JP, Zhou MM, Van Etten RL. J Biol Chem; 1994 Mar 25; 269(12):8734-40. PubMed ID: 8132604 [Abstract] [Full Text] [Related]
20. The structure of the bovine protein tyrosine phosphatase dimer reveals a potential self-regulation mechanism. Tabernero L, Evans BN, Tishmack PA, Van Etten RL, Stauffacher CV. Biochemistry; 1999 Sep 07; 38(36):11651-8. PubMed ID: 10512620 [Abstract] [Full Text] [Related] Page: [Next] [New Search]