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Identification and Functional Characterization of the NAD Kinase of Leishmania Braziliensis (LbNADK)

https://doi.org/10.2139/ssrn.4152680
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inferredcites →https://doi.org/10.1002/jcc.20084openalex-extracted
UCSF Chimera—A visualization system for exploratory research and analysis
inferredcites →https://doi.org/10.1002/prot.10286openalex-extracted
Structure validation by Cα geometry: ϕ,ψ and Cβ deviation
inferredcites →https://doi.org/10.1006/bbrc.2001.5735openalex-extracted
Structural and Functional Characterization of Human NAD Kinase
inferredcites →https://doi.org/10.1016/j.bbrc.2004.11.163openalex-extracted
NAD-binding mode and the significance of intersubunit contact revealed by the crystal structure of Mycobacterium tuberculosis NAD kinase–NAD complex
inferredcites →https://doi.org/10.1016/j.biochi.2012.09.034openalex-extracted
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inferredcites →https://doi.org/10.1016/j.exppara.2005.07.003openalex-extracted
Trypanosomatid protozoa: A simplified DNA isolation procedure
inferredcites →https://doi.org/10.1016/j.jmb.2005.09.026openalex-extracted
Crystal Structures of an NAD Kinase from Archaeoglobus fulgidus in Complex with ATP, NAD, or NADP
inferredcites →https://doi.org/10.1016/j.tibs.2004.01.007openalex-extracted
The new life of a centenarian: signalling functions of NAD(P)
inferredcites →https://doi.org/10.1021/ac00212a004openalex-extracted
DNA amplification by the polymerase chain reaction
inferredcites →https://doi.org/10.1021/bi049650wopenalex-extracted
Characterization of Mycobacterium tuberculosis NAD Kinase: Functional Analysis of the Full-Length Enzyme by Site-Directed Mutagenesis
inferredcites →https://doi.org/10.1038/nmeth.3213openalex-extracted
The I-TASSER Suite: protein structure and function prediction
inferredcites →https://doi.org/10.1038/nprot.2006.4openalex-extracted
Tricine–SDS-PAGE
inferredcites →https://doi.org/10.1042/bj20061638openalex-extracted
The power to reduce: pyridine nucleotides – small molecules with a multitude of functions
inferredcites →https://doi.org/10.1046/j.1432-1327.2001.02358.xopenalex-extracted
Molecular characterization of Escherichia coli NAD kinase
inferredcites →https://doi.org/10.1073/pnas.1417290112openalex-extracted
NAD kinase controls animal NADP biosynthesis and is modulated via evolutionarily divergent calmodulin-dependent mechanisms
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MJ0917 in Archaeon Methanococcus jannaschii Is a Novel NADP Phosphatase/NAD Kinase
inferredcites →https://doi.org/10.1074/jbc.m701394200openalex-extracted
NAD Kinases Use Substrate-assisted Catalysis for Specific Recognition of NAD
inferredcites →https://doi.org/10.1096/fj.10-157529openalex-extracted
Multiple levels of gene regulation mediate differentiation of the intracellular pathogen Leishmania
inferredcites →https://doi.org/10.1104/pp.104.040428openalex-extracted
Cloning and Characterization of Two NAD Kinases from Arabidopsis. Identification of a Calmodulin Binding Isoform
inferredcites →https://doi.org/10.1111/j.1742-4658.2005.04749.xopenalex-extracted
Identification of ATP‐NADH kinase isozymes and their contribution to supply of NADP(H) in Saccharomyces cerevisiae
inferredcites →https://doi.org/10.1128/cmr.19.1.111-126.2006openalex-extracted
Drug Resistance in Leishmaniasis
inferredcites →https://doi.org/10.1128/jb.181.4.1196-1202.1999openalex-extracted
Two Nucleotide Transport Proteins in Chlamydia trachomatis , One for Net Nucleoside Triphosphate Uptake and the Other for Transport of Energy
inferredcites →https://doi.org/10.1179/174329210x12650506623122openalex-extracted
The phosphate makes a difference: cellular functions of NADP
inferredcites →https://doi.org/10.1271/bbb.70738openalex-extracted
Structure and Function of NAD Kinase and NADP Phosphatase: Key Enzymes That Regulate the Intracellular Balance of NAD(H) and NADP(H)
inferredcites →https://doi.org/10.1385/0-89603-126-8:25openalex-extracted
The Bradford Method for Protein Quantitation
inferredcites →https://doi.org/10.15446/rev.colomb.quim.v48n1.75273openalex-extracted
Functional identification and subcellular localization of NAD kinase in the protozoan parasite Giardia intestinalis
inferredcites →https://doi.org/10.4103/1947-2714.128482openalex-extracted
Western blot: Technique, theory and trouble shooting
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