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A roadmap to evaluate the proteome-wide selectivity of covalent kinase inhibitors

Autor: John Charles Kath, Theodore O. Johnson, Landon R. Whitby, Benjamin F. Cravatt, Baoxian Wei, Chu Wang, Mark E. Schnute, Melissa M. Dix, Lee R. Roberts, Laurence O. Whiteley, Adam M. Gilbert, Jonathan J. Hulce, Sherry Niessen, Erik C. Hett, Chris Joslyn, Matthew Merrill Hayward, Bryan R. Lanning, John Douhan

Publikováno v: Nature chemical biology

Kinases are principal components of signal transduction pathways and the focus of intense basic and drug discovery research. Irreversible inhibitors that covalently modify non-catalytic cysteines in kinase active-sites have emerged as valuable probes

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::cf4cc4677878a633174a0e1621180667
http://europepmc.org/articles/PMC4138289

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Stable Transformation of CHO Cells and Human NARP Cybrids Confers Oligomycin Resistance (olir) Following Transfer of a Mitochondrial DNA–Encoded olirATPase6 Gene to the Nuclear Genome: A Model System for mtDNA Gene Therapy

Autor: C R Merril, M Chloupkova, S J Zullo, W A Fenton, J M Eisenstadt, W T Parks, Baoxian Wei, Henry Weiner

Publikováno v: Rejuvenation Research. 8:18-28

Point and deletion mutations and a general depletion of mammalian mitochondrial DNA (mtDNA) give rise to a wide variety of medical syndromes that are refractory to treatment, possibly including aging itself. While gene therapy directed at correcting

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::9b1c0d5f80f893693cdf11ec19cc6257
https://doi.org/10.1089/rej.2005.8.18

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Structural Determinants of Metal Specificity in the Zinc Transport Protein ZnuA from Synechocystis 6803

Autor: Himadri B. Pakrasi, Soojay Banerjee, Thomas J. Smith, Baoxian Wei, Maitrayee Bhattacharyya-Pakrasi

Publikováno v: Journal of Molecular Biology. 333:1061-1069

A number of bacterial metal transporters belong to the cluster 9 family of ABC transporters. The residues in the periplasmic domain thought to be involved in metal binding seem highly conserved and yet the transporters have varying metal specificity.

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::fd4c5d3ef4a4a5f1ff078a3049b001b8
https://doi.org/10.1016/j.jmb.2003.09.008

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Subunit communication in tetrameric class 2 human liver aldehyde dehydrogenase as the basis for half-of-the-site reactivity and the dominance of the oriental subunit in a heterotetramer

Autor: Jianzhong Zhou, Henry Weiner, Baoxian Wei

Publikováno v: Chemico-Biological Interactions. :47-56

Data has been published showing that in heterotetrameric liver mitochondrial aldehyde dehydrogenase composed of the active (E487) and the inactive Oriental-variant (K487) subunit, the Oriental variant was dominant and caused the inactivation of the E

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::0b977cf8c89dd03fb8479fa0aa8be709
https://doi.org/10.1016/s0009-2797(00)00221-0

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Precursor protein is readily degraded in mitochondrial matrix space if the leader is not processed by mitochondrial processing peptidase

Autor: Baoxian Wei, Henry Weiner, Abhijit Mukhopadhyay, Chun-song Yang

Publikováno v: The Journal of biological chemistry. 282(51)

It is not known why leader peptides are removed by the mitochondrial processing peptidase after import into the matrix space. The leaders of yeast aldehyde dehydrogenase (pALDH) and malate dehydrogenase were mutated so that they would not be processe

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::3badc794ac9de88e733e87a2311a14b7
https://pubmed.ncbi.nlm.nih.gov/17959599

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Possible regulatory role for the histidine-rich loop in the zinc transport protein, ZnuA

Autor: Himadri B. Pakrasi, Maitrayee Bhattacharyya-Pakrasi, Baoxian Wei, Thomas J. Smith, Amelia M. Randich

Publikováno v: Biochemistry. 46(30)

A number of bacterial metal transporters belong to the ABC transporter family. To better understand the structural determinants of metal selectivity of one such transporter, we previously determined the structure of the periplasmic domain of a zinc t

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::9a90017be591e3f2869acfc22b4e1e61
https://pubmed.ncbi.nlm.nih.gov/17616151

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Chemical modifications to study mutations that affect the ability of the general base (E268) to function in human liver mitochondrial aldehyde dehydrogenase

Autor: Baoxian Wei, Henry Weiner, Dennis C. Mays, James J. Lipsky

Publikováno v: Chemico-biological interactions.

The action of a general base is needed in two possible steps during the aldehyde dehydrogenase catalyzed oxidation of an aldehyde to an acid. The base is glutamate at position 268 in the cytosolic and mitochondrial class 1 and 2 enzyme. A chemical mo

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::180323e9ab45675108d8cd71cb2e8605
https://pubmed.ncbi.nlm.nih.gov/12604192

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Making an Oriental equivalent of the yeast cytosolic aldehyde dehydrogenase as well as making one with positive cooperativity in coenzyme binding by mutations of glutamate 492 and arginine 480

Autor: Baoxian Wei, Henry Weiner

Publikováno v: Chemico-biological interactions. (1-3)

Yeast has at least three partially characterized aldehyde dehydrogenases. Previous studies by gene disrupted in our laboratory revealed that the Saccharomyces cerevisiae cytosol ALDH1 played an important role in ethanol metabolism as did the class 2

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::934c0a20e35369737af85bfb2a140cd2
https://pubmed.ncbi.nlm.nih.gov/11306041

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Cooperativity in nicotinamide adenine dinucleotide binding induced by mutations of arginine 475 located at the subunit interface in the human liver mitochondrial class 2 aldehyde dehydrogenase

Autor: Henry Weiner, Li Ni, Thomas D. Hurley, Baoxian Wei

Publikováno v: Europe PubMed Central

The low-activity Oriental variant of human mitochondrial aldehyde dehydrogenase possesses a lysine rather than a glutamate at residue 487 in the 500 amino acid homotetrameric enzyme. The glutamate at position 487 formed two salt bonds, one to an argi

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::3001a293a5c85a2f0321c4996d96dd50
https://pubmed.ncbi.nlm.nih.gov/10819999

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