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  1. AU="Wright, Aaron T"
  2. AU="Jones, T. B."
  3. AU=Shirtliff Mark E.
  4. AU="Riis, Kamilla R"
  5. AU="Xu, Leyao"
  6. AU="Udayakumar, Karthikrajan Parasuraman"
  7. AU="Fry, Brian"

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  1. Artikel ; Online: A transcriptional relationship with a natural product disrupts mitochondrial biogenesis.

    Wright, Aaron T

    Cell chemical biology

    2021  Band 28, Heft 10, Seite(n) 1392–1393

    Abstract: A limonoid natural product disrupts mitochondrial biogenesis and overcomes resistance. In this issue of Cell Chemical Biology, Cho et al. describe an anti-melanoma strategy in which a transcriptional target gene enables the anti-proliferative activity of ...

    Abstract A limonoid natural product disrupts mitochondrial biogenesis and overcomes resistance. In this issue of Cell Chemical Biology, Cho et al. describe an anti-melanoma strategy in which a transcriptional target gene enables the anti-proliferative activity of the limonoid, harrpernoid D.
    Mesh-Begriff(e) Biological Products/pharmacology ; Humans ; Melanoma ; Mitochondria ; Organelle Biogenesis
    Chemische Substanzen Biological Products
    Sprache Englisch
    Erscheinungsdatum 2021-10-21
    Erscheinungsland United States
    Dokumenttyp Journal Article ; Comment
    ISSN 2451-9448
    ISSN (online) 2451-9448
    DOI 10.1016/j.chembiol.2021.10.002
    Datenquelle MEDical Literature Analysis and Retrieval System OnLINE

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  2. Artikel ; Online: Gut commensals make choline too.

    Wright, Aaron T

    Nature microbiology

    2018  Band 4, Heft 1, Seite(n) 4–5

    Mesh-Begriff(e) Choline ; Gastrointestinal Microbiome ; Phospholipase D ; Phospholipases ; Symbiosis
    Chemische Substanzen Phospholipases (EC 3.1.-) ; Phospholipase D (EC 3.1.4.4) ; Choline (N91BDP6H0X)
    Sprache Englisch
    Erscheinungsdatum 2018-12-13
    Erscheinungsland England
    Dokumenttyp Journal Article ; Comment
    ISSN 2058-5276
    ISSN (online) 2058-5276
    DOI 10.1038/s41564-018-0325-1
    Datenquelle MEDical Literature Analysis and Retrieval System OnLINE

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  3. Artikel ; Online: Activity-Based Protein Profiling to Probe Relationships between Cytochrome P450 Enzymes and Early-Age Metabolism of Two Polycyclic Aromatic Hydrocarbons (PAHs): Phenanthrene and Retene.

    Gaither, Kari A / Garcia, Whitney L / Tyrrell, Kimberly J / Wright, Aaron T / Smith, Jordan N

    Chemical research in toxicology

    2024  Band 37, Heft 5, Seite(n) 711–722

    Abstract: A growing body of literature has linked early-life exposures to polycyclic aromatic hydrocarbons (PAH) with adverse neurodevelopmental effects. Once in the body, metabolism serves as a powerful mediator of PAH toxicity by bioactivating and detoxifying ... ...

    Abstract A growing body of literature has linked early-life exposures to polycyclic aromatic hydrocarbons (PAH) with adverse neurodevelopmental effects. Once in the body, metabolism serves as a powerful mediator of PAH toxicity by bioactivating and detoxifying PAH metabolites. Since enzyme expression and activity vary considerably throughout human development, we evaluated infant metabolism of PAHs as a potential contributing factor to PAH susceptibility. We measured and compared rates of phenanthrene and retene (two primary PAH constituents of woodsmoke) metabolism in human hepatic microsomes from individuals ≤21 months of age to a pooled sample (
    Mesh-Begriff(e) Phenanthrenes/metabolism ; Humans ; Cytochrome P-450 Enzyme System/metabolism ; Microsomes, Liver/metabolism ; Infant ; Adult ; Female ; Male ; Polycyclic Aromatic Hydrocarbons/metabolism
    Chemische Substanzen phenanthrene ; retene
    Sprache Englisch
    Erscheinungsdatum 2024-04-11
    Erscheinungsland United States
    Dokumenttyp Journal Article
    ZDB-ID 639353-6
    ISSN 1520-5010 ; 0893-228X
    ISSN (online) 1520-5010
    ISSN 0893-228X
    DOI 10.1021/acs.chemrestox.3c00424
    Datenquelle MEDical Literature Analysis and Retrieval System OnLINE

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  4. Artikel ; Online: Host-pathogen interactions: A cholera surveillance system.

    Wright, Aaron T

    Nature chemical biology

    2016  Band 12, Heft 4, Seite(n) 203–204

    Mesh-Begriff(e) Animals ; Host-Pathogen Interactions/physiology ; Humans ; Intestines ; Lectins/metabolism ; Peptide Hydrolases/metabolism ; Proteomics/methods ; Vibrio cholerae/enzymology
    Chemische Substanzen Lectins ; Peptide Hydrolases (EC 3.4.-)
    Sprache Englisch
    Erscheinungsdatum 2016-04
    Erscheinungsland United States
    Dokumenttyp Comment ; Journal Article
    ZDB-ID 2202962-X
    ISSN 1552-4469 ; 1552-4450
    ISSN (online) 1552-4469
    ISSN 1552-4450
    DOI 10.1038/nchembio.2039
    Datenquelle MEDical Literature Analysis and Retrieval System OnLINE

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  5. Artikel: An activity-based probe targeting the streptococcal virulence factor C5a peptidase

    Krishnamoorthy, Sankarganesh / Steiger, Andrea K. / Nelson, William C. / Egbert, Robert G. / Wright, Aaron T.

    Chemical communications. 2022 July 19, v. 58, no. 58

    2022  

    Abstract: Development of profiling strategies to provide high resolution understanding of enzymes involved in bacterial infections remains an important need. These strategies help resolve enzyme mechanisms of actions and can guide therapeutic development. We have ... ...

    Abstract Development of profiling strategies to provide high resolution understanding of enzymes involved in bacterial infections remains an important need. These strategies help resolve enzyme mechanisms of actions and can guide therapeutic development. We have developed a selective new activity-based probe (ABP) targeting a highly conserved surface bound enzyme, C5a peptidase, present in several pathogenic Streptococci. We demonstrate our probe inhibits C5a peptidase activity and enables detection of C5a peptidase expressing pathogens in microbial mixtures. Our profiling strategy selectively labels the pathogen by phenotype and enables specific isolation of the live bacteria providing a route for further in-depth investigation. This study paves the way towards a rapid detection, isolation, and characterization pipeline for existing and emerging strains of most common pathogenic Streptococci.
    Schlagwörter enzymes ; pathogens ; phenotype ; rapid methods ; therapeutics ; virulence
    Sprache Englisch
    Erscheinungsverlauf 2022-0719
    Umfang p. 8113-8116.
    Erscheinungsort The Royal Society of Chemistry
    Dokumenttyp Artikel
    ZDB-ID 1472881-3
    ISSN 1364-548X ; 1359-7345 ; 0009-241X
    ISSN (online) 1364-548X
    ISSN 1359-7345 ; 0009-241X
    DOI 10.1039/d2cc01517j
    Datenquelle NAL Katalog (AGRICOLA)

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  6. Artikel: Activity-Based Protein Profiling-Enabling Multimodal Functional Studies of Microbial Communities.

    Whidbey, Christopher / Wright, Aaron T

    Current topics in microbiology and immunology

    2018  Band 420, Seite(n) 1–21

    Abstract: Microorganisms living in community are critical to life on Earth, playing numerous and profound roles in the environment and human and animal health. Though their essentiality to life is clear, the mechanistic underpinnings of community structure, ... ...

    Abstract Microorganisms living in community are critical to life on Earth, playing numerous and profound roles in the environment and human and animal health. Though their essentiality to life is clear, the mechanistic underpinnings of community structure, interactions, and functions are largely unexplored and in need of function-dependent technologies to unravel the mysteries. Activity-based protein profiling offers unprecedented molecular-level characterization of functions within microbial communities and provides an avenue to determine how external exposures result in functional alterations to microbiomes. Herein, we illuminate the current state and prospective contributions of ABPP as it relates to microbial communities. We provide details on the design, development, and validation of probes, challenges associated with probing in complex microbial communities, provide some specific examples of the biological applications of ABPP in microbes and microbial communities, and highlight potential areas for development. The future of ABPP holds real promise for understanding and considerable impact in microbiome studies associated with personalized medicine, precision agriculture, veterinary health, environmental studies, and beyond.
    Mesh-Begriff(e) Animals ; Humans ; Microbiological Techniques/methods ; Microbiota/physiology ; Proteome/analysis ; Proteome/chemistry ; Proteome/metabolism ; Proteomics/methods
    Chemische Substanzen Proteome
    Sprache Englisch
    Erscheinungsdatum 2018-11-08
    Erscheinungsland Germany
    Dokumenttyp Journal Article ; Review
    ISSN 0070-217X
    ISSN 0070-217X
    DOI 10.1007/82_2018_128
    Datenquelle MEDical Literature Analysis and Retrieval System OnLINE

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  7. Artikel ; Online: Detecting differential protein abundance by combining peptide level P-values.

    Killinger, Bryan J / Petyuk, Vladislav A / Wright, Aaron T

    Molecular omics

    2020  Band 16, Heft 6, Seite(n) 554–562

    Abstract: The majority of methods for detecting differentially abundant proteins between samples in label-free LC-MS bottom-up proteomics experiments rely on statistically testing inferred protein abundances derived from peptide ionization intensities or averaging ...

    Abstract The majority of methods for detecting differentially abundant proteins between samples in label-free LC-MS bottom-up proteomics experiments rely on statistically testing inferred protein abundances derived from peptide ionization intensities or averaging peptide level statistics. Here, we statistically test peptide ionization intensities directly and combine the resulting dependent P-values using the Empirical Brown's Method (EBM), avoiding error introduced through the estimation of protein abundances or summarizing test statistics. We show that on a spike-in proteomics dataset, a peptide level approach using EBM outperforms differential abundance detection using a protein level approach and several analysis workflows, including MSstats. Additionally, we demonstrate the effectiveness of this approach by detecting enriched proteins from an activity-based protein profiling dataset.
    Mesh-Begriff(e) Amino Acid Sequence ; Databases, Protein ; Glutathione/metabolism ; Humans ; Neoplasms/metabolism ; Peptides/chemistry ; Peptides/metabolism ; Proteomics/methods
    Chemische Substanzen Peptides ; Glutathione (GAN16C9B8O)
    Sprache Englisch
    Erscheinungsdatum 2020-09-14
    Erscheinungsland England
    Dokumenttyp Journal Article ; Research Support, N.I.H., Extramural ; Research Support, U.S. Gov't, Non-P.H.S.
    ISSN 2515-4184
    ISSN (online) 2515-4184
    DOI 10.1039/d0mo00045k
    Datenquelle MEDical Literature Analysis and Retrieval System OnLINE

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  8. Artikel ; Online: Bile salt hydrolase profiling by fluorogenic probes in the human gut microbiome.

    Sveistyte, Agne / Miller, Carson J / Brandvold, Kristoffer R / Wright, Aaron T

    Methods in enzymology

    2021  Band 664, Seite(n) 243–265

    Abstract: Bile is a digestive fluid produced in the liver and stored in the gallbladder. It participates in absorption of fatty nutrients and vitamins, and aids in elimination of metabolic waste and toxins. The major chemical components of bile are bile salts that, ...

    Abstract Bile is a digestive fluid produced in the liver and stored in the gallbladder. It participates in absorption of fatty nutrients and vitamins, and aids in elimination of metabolic waste and toxins. The major chemical components of bile are bile salts that, apart from their function in digestion, are also known to participate in cell signaling by binding host farnesoid X (FXR), vitamin D (VDR), and G-protein coupled bile acid (TGR5) receptors. Microbial bile salt hydrolases (BSHs) catalyze bile salt deconjugation, a gatekeeper reaction that is a prerequisite for all subsequent microbial transformations of bile acids. As a result, BSH determines the composition of the bile salt and acid pools, which in turn affects its nutrient absorption and signaling capabilities. BSH profiling remains a challenge due to a paucity of tools that enable scientists to study its function. In this chapter, we discuss current BSH profiling approaches and demonstrate a novel fluorogenic probe-based assay that circumvents laborious and resource intensive BSH quantification methods. Alongside our assay protocol, we provide the reader with a detailed method for microbial cell extraction from fecal matter. We also cover probe validation protocols that can be adapted for Michaelis-Menten analysis with any BSH expressing strain.
    Mesh-Begriff(e) Amidohydrolases/metabolism ; Bile Acids and Salts ; Feces ; Gastrointestinal Microbiome ; Humans
    Chemische Substanzen Bile Acids and Salts ; Amidohydrolases (EC 3.5.-) ; choloylglycine hydrolase (EC 3.5.1.24)
    Sprache Englisch
    Erscheinungsdatum 2021-12-09
    Erscheinungsland United States
    Dokumenttyp Journal Article ; Research Support, N.I.H., Extramural ; Research Support, Non-U.S. Gov't ; Research Support, U.S. Gov't, Non-P.H.S.
    ISSN 1557-7988
    ISSN (online) 1557-7988
    DOI 10.1016/bs.mie.2021.11.022
    Datenquelle MEDical Literature Analysis and Retrieval System OnLINE

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  9. Artikel ; Online: An activity-based probe targeting the streptococcal virulence factor C5a peptidase.

    Krishnamoorthy, Sankarganesh / Steiger, Andrea K / Nelson, William C / Egbert, Robert G / Wright, Aaron T

    Chemical communications (Cambridge, England)

    2022  Band 58, Heft 58, Seite(n) 8113–8116

    Abstract: Development of profiling strategies to provide high resolution understanding of enzymes involved in bacterial infections remains an important need. These strategies help resolve enzyme mechanisms of actions and can guide therapeutic development. We have ... ...

    Abstract Development of profiling strategies to provide high resolution understanding of enzymes involved in bacterial infections remains an important need. These strategies help resolve enzyme mechanisms of actions and can guide therapeutic development. We have developed a selective new activity-based probe (ABP) targeting a highly conserved surface bound enzyme, C5a peptidase, present in several pathogenic
    Mesh-Begriff(e) Adhesins, Bacterial ; Endopeptidases/genetics ; Endopeptidases/metabolism ; Endopeptidases/pharmacology ; Streptococcus pyogenes ; Virulence Factors
    Chemische Substanzen Adhesins, Bacterial ; Virulence Factors ; Endopeptidases (EC 3.4.-) ; C5a peptidase (EC 3.4.99.-)
    Sprache Englisch
    Erscheinungsdatum 2022-07-19
    Erscheinungsland England
    Dokumenttyp Journal Article
    ZDB-ID 1472881-3
    ISSN 1364-548X ; 1359-7345 ; 0009-241X
    ISSN (online) 1364-548X
    ISSN 1359-7345 ; 0009-241X
    DOI 10.1039/d2cc01517j
    Datenquelle MEDical Literature Analysis and Retrieval System OnLINE

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  10. Artikel ; Online: Snekmer: a scalable pipeline for protein sequence fingerprinting based on amino acid recoding.

    Chang, Christine H / Nelson, William C / Jerger, Abby / Wright, Aaron T / Egbert, Robert G / McDermott, Jason E

    Bioinformatics advances

    2023  Band 3, Heft 1, Seite(n) vbad005

    Abstract: Motivation: The vast expansion of sequence data generated from single organisms and microbiomes has precipitated the need for faster and more sensitive methods to assess evolutionary and functional relationships between proteins. Representing proteins ... ...

    Abstract Motivation: The vast expansion of sequence data generated from single organisms and microbiomes has precipitated the need for faster and more sensitive methods to assess evolutionary and functional relationships between proteins. Representing proteins as sets of short peptide sequences (kmers) has been used for rapid, accurate classification of proteins into functional categories; however, this approach employs an exact-match methodology and thus may be limited in terms of sensitivity and coverage. We have previously used similarity groupings, based on the chemical properties of amino acids, to form reduced character sets and recode proteins. This amino acid recoding (AAR) approach simplifies the construction of protein representations in the form of kmer vectors, which can link sequences with distant sequence similarity and provide accurate classification of problematic protein families.
    Results: Here, we describe Snekmer, a software tool for recoding proteins into AAR kmer vectors and performing either (i) construction of supervised classification models trained on input protein families or (ii) clustering for
    Availability and implementation: Snekmer is written in Python using Snakemake. Code and data used in this article, along with tutorial notebooks, are available at http://github.com/PNNL-CompBio/Snekmer under an open-source BSD-3 license.
    Supplementary information: Supplementary data are available at
    Sprache Englisch
    Erscheinungsdatum 2023-02-02
    Erscheinungsland England
    Dokumenttyp Journal Article
    ISSN 2635-0041
    ISSN (online) 2635-0041
    DOI 10.1093/bioadv/vbad005
    Datenquelle MEDical Literature Analysis and Retrieval System OnLINE

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