scholarly article | Q13442814 |
P50 | author | Magdalena Makowska-Grzyska | Q47546863 |
Jerzy Osipiuk | Q114783297 | ||
Andrzej Joachimiak | Q28028611 | ||
P2093 | author name string | Youngchang Kim | |
Natalia Maltseva | |||
Lizbeth Hedstrom | |||
Magdalena Makowska-Grzyska | |||
Minjia Zhang | |||
Suresh Kumar Gorla | |||
Deviprasad R Gollapalli | |||
Minyi Gu | |||
Kavitha Mandapati | |||
P2860 | cites work | Cofactor mobility determines reaction outcome in the IMPDH and GMPR (β-α)8 barrel enzymes | Q24294954 |
IMP dehydrogenase: structure, mechanism, and inhibition | Q24642299 | ||
PHENIX: a comprehensive Python-based system for macromolecular structure solution | Q24654617 | ||
MolProbity: all-atom contacts and structure validation for proteins and nucleic acids | Q24684673 | ||
Identification of novel Mt-Guab2 inhibitor series active against M. tuberculosis | Q27306024 | ||
Crystal structure of human type II inosine monophosphate dehydrogenase: implications for ligand binding and drug design | Q27617777 | ||
Characteristics and crystal structure of bacterial inosine-5'-monophosphate dehydrogenase | Q27617878 | ||
Crystal structure of a ternary complex of Tritrichomonas foetus inosine 5'-monophosphate dehydrogenase: NAD+ orients the active site loop for catalysis | Q27639884 | ||
Phthalazinone inhibitors of inosine-5'-monophosphate dehydrogenase from Cryptosporidium parvum. | Q36570032 | ||
Targeting a prokaryotic protein in a eukaryotic pathogen: identification of lead compounds against cryptosporidiosis | Q36740182 | ||
Selective and potent urea inhibitors of cryptosporidium parvum inosine 5'-monophosphate dehydrogenase | Q36791988 | ||
The Structural Biology Center 19ID undulator beamline: facility specifications and protein crystallographic results. | Q37015481 | ||
Allosteric activation via kinetic control: potassium accelerates a conformational change in IMP dehydrogenase | Q38618632 | ||
Unusual conformation of nicotinamide adenine dinucleotide (NAD) bound to diphtheria toxin: a comparison with NAD bound to the oxidoreductase enzymes | Q42167298 | ||
Asp338 controls hydride transfer in Escherichia coli IMP dehydrogenase | Q43505933 | ||
Pharmacophore binding motifs for nicotinamide adenine dinucleotide analogues across multiple protein families: a detailed contact-based analysis of the interaction between proteins and NAD(P) cofactors | Q47928265 | ||
Linking distinct conformations of nicotinamide adenine dinucleotide with protein fold/function. | Q53245439 | ||
Integration of PCR fragments at any specific site within cloning vectors without the use of restriction enzymes and DNA ligase | Q74238681 | ||
PURINE N-OXIDES. XII. PHOTOCHEMICAL CHANGES INDUCED BY ULTRAVIOLET RADIATION | Q76969429 | ||
Differential signatures of bacterial and mammalian IMP dehydrogenase enzymes | Q77950759 | ||
Cofactor-type inhibitors of inosine monophosphate dehydrogenase via modular approach: targeting the pyrophosphate binding sub-domain | Q83419394 | ||
The immunosuppressive agent mizoribine monophosphate forms a transition state analogue complex with inosine monophosphate dehydrogenase | Q27640361 | ||
Crystal structures of Tritrichomonasfoetus inosine monophosphate dehydrogenase in complex with substrate, cofactor and analogs: a structural basis for the random-in ordered-out kinetic mechanism | Q27640406 | ||
The Structural Basis of Cryptosporidium-Specific IMP Dehydrogenase Inhibitor Selectivity | Q27658866 | ||
Bacillus anthracis Inosine 5′-Monophosphate Dehydrogenase in Action: The First Bacterial Series of Structures of Phosphate Ion-, Substrate-, and Product-Bound Complexes | Q27670715 | ||
Structure of Apo- and Monometalated Forms of NDM-1—A Highly Potent Carbapenem-Hydrolyzing Metallo-β-Lactamase | Q27674309 | ||
Structure ofPseudomonas aeruginosainosine 5′-monophosphate dehydrogenase | Q27676976 | ||
Optimization of Benzoxazole-Based Inhibitors of Cryptosporidium parvum Inosine 5′-Monophosphate Dehydrogenase | Q27678115 | ||
Structure and mechanism of inosine monophosphate dehydrogenase in complex with the immunosuppressant mycophenolic acid | Q27733135 | ||
Use of TLS parameters to model anisotropic displacements in macromolecular refinement | Q27860499 | ||
HKL-3000: the integration of data reduction and structure solution--from diffraction images to an initial model in minutes | Q27860502 | ||
Coot: model-building tools for molecular graphics | Q27860505 | ||
Overview of the CCP4 suite and current developments | Q27860782 | ||
Multiple sequence alignment with hierarchical clustering | Q27860956 | ||
Refinement of macromolecular structures by the maximum-likelihood method | Q27861011 | ||
The TIM-barrel fold: a versatile framework for efficient enzymes | Q28205462 | ||
A screening pipeline for antiparasitic agents targeting cryptosporidium inosine monophosphate dehydrogenase | Q28475058 | ||
Triazole-linked inhibitors of inosine monophosphate dehydrogenase from human and Mycobacterium tuberculosis | Q28486568 | ||
Antibiotics for emerging pathogens | Q29615377 | ||
Deciphering key features in protein structures with the new ENDscript server | Q29617219 | ||
Biochemical analysis of the modular enzyme inosine 5'-monophosphate dehydrogenase | Q30175322 | ||
The antibiotic potential of prokaryotic IMP dehydrogenase inhibitors | Q30356398 | ||
Repurposing cryptosporidium inosine 5'-monophosphate dehydrogenase inhibitors as potential antibacterial agents. | Q30371392 | ||
High-throughput protein purification and quality assessment for crystallization | Q30406950 | ||
Structural determinants of inhibitor selectivity in prokaryotic IMP dehydrogenases | Q30430133 | ||
Triazole inhibitors of Cryptosporidium parvum inosine 5'-monophosphate dehydrogenase | Q33604996 | ||
The structure of a domain common to archaebacteria and the homocystinuria disease protein | Q34415436 | ||
Structure-activity relationship study of selective benzimidazole-based inhibitors of Cryptosporidium parvum IMPDH. | Q35787804 | ||
The CBS subdomain of inosine 5'-monophosphate dehydrogenase regulates purine nucleotide turnover | Q36517922 | ||
P433 | issue | 9 | |
P407 | language of work or name | English | Q1860 |
P304 | page(s) | 5893-5911 | |
P577 | publication date | 2015-01-08 | |
P1433 | published in | Journal of Biological Chemistry | Q867727 |
P1476 | title | A novel cofactor-binding mode in bacterial IMP dehydrogenases explains inhibitor selectivity | |
P478 | volume | 290 |
Q41966229 | A nucleotide-controlled conformational switch modulates the activity of eukaryotic IMP dehydrogenases. |
Q40121791 | Benzoxazoles, phthalazinones, and arylurea-based compounds with IMPDH-independent antibacterial activity against Francisella tularensis. |
Q36350988 | Biochemical and structural analysis of an Eis family aminoglycoside acetyltransferase from bacillus anthracis |
Q27702049 | Crystallographic studies of two variants of Pseudomonas aeruginosa IMPDH with impaired allosteric regulation |
Q38573837 | Discovery of a new method for potent drug development using power function of stoichiometry of homomeric biocomplexes or biological nanomotors |
Q53684814 | Expanding benzoxazole based inosine 5'-monophosphate dehydrogenase (IMPDH) inhibitor structure-activity as potential anti-tuberculosis agents. |
Q36320750 | Guanine nucleotide binding to the Bateman domain mediates the allosteric inhibition of eukaryotic IMP dehydrogenases |
Q90157701 | Horizontal transfer of a pathway for coumarate catabolism unexpectedly inhibits purine nucleotide biosynthesis |
Q41105047 | Inhibition of Inosine-5'-monophosphate Dehydrogenase from Bacillus anthracis: Mechanism Revealed by Pre-Steady-State Kinetics |
Q38558374 | Inosine 5'-monophosphate dehydrogenase inhibitors as antimicrobial agents: recent progress and future perspectives. |
Q28550069 | Mycobacterium tuberculosis IMPDH in Complexes with Substrates, Products and Antitubercular Compounds |
Q35592527 | Structure of Cryptosporidium IMP dehydrogenase bound to an inhibitor with in vivo antiparasitic activity |
Q27728459 | The Inosine Monophosphate Dehydrogenase, GuaB2, Is a Vulnerable New Bactericidal Drug Target for Tuberculosis |
Q36934054 | The cystathionine-β-synthase domains on the guanosine 5''-monophosphate reductase and inosine 5'-monophosphate dehydrogenase enzymes from Leishmania regulate enzymatic activity in response to guanylate and adenylate nucleotide levels |
Q90914855 | Unpacking the Pathogen Box-An Open Source Tool for Fighting Neglected Tropical Disease |
Search more.