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  1. Book: Sirtuins

    Hirschey, Matthew D.

    methods and protocols

    (Methods in molecular biology ; 1077 ; Springer protocols)

    2013  

    Author's details ed. by Matthew D. Hirschey
    Series title Methods in molecular biology ; 1077
    Springer protocols
    Collection
    Language English
    Size XI, 314 S. : Ill., graph. Darst.
    Publisher Humana Press
    Publishing place New York u.a.
    Publishing country United States
    Document type Book
    HBZ-ID HT017832653
    ISBN 9781627036368 ; 1627036369
    Database Catalogue ZB MED Medicine, Health

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    Shelf markLoan statusLocation
    2013 A 3035 available for loan (reading room) Lesesaal EG

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  2. Article ; Online: Lab life - rebuild it better after coronavirus lockdowns ease.

    Hirschey, Matthew

    Nature

    2020  Volume 582, Issue 7811, Page(s) 184

    MeSH term(s) Betacoronavirus ; COVID-19 ; Coronavirus ; Coronavirus Infections ; Humans ; Infection Control ; Laboratories ; Masks ; Pandemics ; Pneumonia, Viral ; Research ; SARS-CoV-2
    Keywords covid19
    Language English
    Publishing date 2020-06-10
    Publishing country England
    Document type Letter ; Comment
    ZDB-ID 120714-3
    ISSN 1476-4687 ; 0028-0836
    ISSN (online) 1476-4687
    ISSN 0028-0836
    DOI 10.1038/d41586-020-01708-8
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  4. Article ; Online: Discovering the landscape of protein modifications.

    Keenan, E Keith / Zachman, Derek K / Hirschey, Matthew D

    Molecular cell

    2021  Volume 81, Issue 9, Page(s) 1868–1878

    Abstract: Protein modifications modulate nearly every aspect of cell biology in organisms, ranging from Archaea to Eukaryotes. The earliest evidence of covalent protein modifications was found in the early 20th century by studying the amino acid composition of ... ...

    Abstract Protein modifications modulate nearly every aspect of cell biology in organisms, ranging from Archaea to Eukaryotes. The earliest evidence of covalent protein modifications was found in the early 20th century by studying the amino acid composition of proteins by chemical hydrolysis. These discoveries challenged what defined a canonical amino acid. The advent and rapid adoption of mass-spectrometry-based proteomics in the latter part of the 20th century enabled a veritable explosion in the number of known protein modifications, with more than 500 discrete modifications counted today. Now, new computational tools in data science, machine learning, and artificial intelligence are poised to allow researchers to make significant progress in discovering new protein modifications and determining their function. In this review, we take an opportunity to revisit the historical discovery of key post-translational modifications, quantify the current landscape of covalent protein adducts, and assess the role that new computational tools will play in the future of this field.
    MeSH term(s) Animals ; Artificial Intelligence ; Computational Biology ; Databases, Protein ; Humans ; Protein Conformation ; Protein Processing, Post-Translational ; Proteins/chemistry ; Proteins/metabolism ; Proteomics ; Structure-Activity Relationship
    Chemical Substances Proteins
    Language English
    Publishing date 2021-04-01
    Publishing country United States
    Document type Journal Article ; Research Support, N.I.H., Extramural ; Research Support, Non-U.S. Gov't ; Review
    ZDB-ID 1415236-8
    ISSN 1097-4164 ; 1097-2765
    ISSN (online) 1097-4164
    ISSN 1097-2765
    DOI 10.1016/j.molcel.2021.03.015
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  5. Article: Reactive Acyl-CoA Species Modify Proteins and Induce Carbon Stress.

    Trub, Alec G / Hirschey, Matthew D

    Trends in biochemical sciences

    2018  Volume 43, Issue 5, Page(s) 369–379

    Abstract: In recent years, our understanding of the scope and diversity of protein post-translational modifications (PTMs) has rapidly expanded. In particular, mitochondrial proteins are decorated with an array of acyl groups that can occur non-enzymatically. ... ...

    Abstract In recent years, our understanding of the scope and diversity of protein post-translational modifications (PTMs) has rapidly expanded. In particular, mitochondrial proteins are decorated with an array of acyl groups that can occur non-enzymatically. Interestingly, these modifying chemical moieties are often associated with intermediary metabolites from core metabolic pathways. In this Review, we describe biochemical reactions and biological mechanisms that activate carbon metabolites for protein PTM. We explore the emerging links between the intrinsic reactivity of metabolites, non-enzymatic protein acylation, and possible signaling roles for this system. Finally, we propose a model of 'carbon stress', similar to oxidative stress, as an effective way to conceptualize the relationship between widespread protein acylation, nutrient sensing, and metabolic homeostasis.
    MeSH term(s) Acyl Coenzyme A/chemistry ; Acyl Coenzyme A/metabolism ; Animals ; Carbon/chemistry ; Carbon/metabolism ; Humans ; Oxidative Stress ; Protein Processing, Post-Translational ; Substrate Specificity
    Chemical Substances Acyl Coenzyme A ; Carbon (7440-44-0)
    Language English
    Publishing date 2018-02-22
    Publishing country England
    Document type Journal Article ; Research Support, N.I.H., Extramural ; Research Support, Non-U.S. Gov't ; Review
    ZDB-ID 194216-5
    ISSN 1362-4326 ; 0968-0004 ; 0376-5067
    ISSN (online) 1362-4326
    ISSN 0968-0004 ; 0376-5067
    DOI 10.1016/j.tibs.2018.02.002
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  6. Article ; Online: Old enzymes, new tricks: sirtuins are NAD(+)-dependent de-acylases.

    Hirschey, Matthew D

    Cell metabolism

    2011  Volume 14, Issue 6, Page(s) 718–719

    Abstract: Seven mammalian sirtuins are nicotinamide adenine dinucleotide (NAD)(+)-dependent deacetylases and are important modulators of energy metabolism and stress resistance. Two new studies by Du et al. (2011) and Peng et al. (2011) identify a new enzymatic ... ...

    Abstract Seven mammalian sirtuins are nicotinamide adenine dinucleotide (NAD)(+)-dependent deacetylases and are important modulators of energy metabolism and stress resistance. Two new studies by Du et al. (2011) and Peng et al. (2011) identify a new enzymatic activity for SIRT5, expanding the cellular repertoire of posttranslational modifications targeted by the sirtuins.
    Language English
    Publishing date 2011-11-17
    Publishing country United States
    Document type Comment ; Journal Article
    ZDB-ID 2176834-1
    ISSN 1932-7420 ; 1550-4131
    ISSN (online) 1932-7420
    ISSN 1550-4131
    DOI 10.1016/j.cmet.2011.10.006
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  7. Article ; Online: A Prob(e)able Route to Lysine Acylation.

    Wagner, Gregory R / Hirschey, Matthew D

    Cell chemical biology

    2016  Volume 24, Issue 2, Page(s) 126–128

    Abstract: Non-enzymatic modification of proteins by acyl-CoA species involved in intermediary metabolism is a possible explanation for widespread protein acylation. In this issue, Kulkarni et al. (2017) develop a set of chemoproteomic probes to interrogate the ... ...

    Abstract Non-enzymatic modification of proteins by acyl-CoA species involved in intermediary metabolism is a possible explanation for widespread protein acylation. In this issue, Kulkarni et al. (2017) develop a set of chemoproteomic probes to interrogate the role of malonyl-CoA in mediating protein malonylation and find malonylation influences glycolysis in cancer cells.
    MeSH term(s) Acyl Coenzyme A ; Acylation ; Lysine ; Malonyl Coenzyme A ; Proteins
    Chemical Substances Acyl Coenzyme A ; Proteins ; Malonyl Coenzyme A (524-14-1) ; Lysine (K3Z4F929H6)
    Language English
    Publishing date 2016-12-06
    Publishing country United States
    Document type Journal Article ; Comment
    ISSN 2451-9448
    ISSN (online) 2451-9448
    DOI 10.1016/j.chembiol.2017.01.011
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  8. Article ; Online: Sensing Mitochondrial Acetyl-CoA to Tune Respiration.

    Mills, Christine A / Trub, Alec G / Hirschey, Matthew D

    Trends in endocrinology and metabolism: TEM

    2018  Volume 30, Issue 1, Page(s) 1–3

    Abstract: Fatty acid synthesis (FAS) in mitochondria produces a key metabolite called lipoic acid. However, a new study by Van Vranken et al.[1] (Mol. Cell 2018;71:567-580) shows that mitochondrial FAS regulates the assembly of oxidative phosphorylation complexes, ...

    Abstract Fatty acid synthesis (FAS) in mitochondria produces a key metabolite called lipoic acid. However, a new study by Van Vranken et al.[1] (Mol. Cell 2018;71:567-580) shows that mitochondrial FAS regulates the assembly of oxidative phosphorylation complexes, thereby functioning as a nutrient sensor for mitochondrial respiration.
    MeSH term(s) Acetyl Coenzyme A/metabolism ; Acyl Carrier Protein/metabolism ; Eukaryota/metabolism ; Fatty Acids/metabolism ; Mitochondria/metabolism ; Respiration
    Chemical Substances Acyl Carrier Protein ; Fatty Acids ; Acetyl Coenzyme A (72-89-9)
    Language English
    Publishing date 2018-11-12
    Publishing country United States
    Document type Journal Article ; Review
    ZDB-ID 1042384-9
    ISSN 1879-3061 ; 1043-2760
    ISSN (online) 1879-3061
    ISSN 1043-2760
    DOI 10.1016/j.tem.2018.10.003
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  9. Article ; Online: Optical imaging reveals chemotherapy-induced metabolic reprogramming of residual disease and recurrence.

    Sunassee, Enakshi D / Deutsch, Riley J / D'Agostino, Victoria W / Castellano-Escuder, Pol / Siebeneck, Elizabeth A / Ilkayeva, Olga / Crouch, Brian T / Madonna, Megan C / Everitt, Jeffrey / Alvarez, James V / Palmer, Gregory M / Hirschey, Matthew D / Ramanujam, Nirmala

    Science advances

    2024  Volume 10, Issue 14, Page(s) eadj7540

    Abstract: Fewer than 20% of triple-negative breast cancer patients experience long-term responses to mainstay chemotherapy. Resistant tumor subpopulations use alternative metabolic pathways to escape therapy, survive, and eventually recur. Here, we show in vivo, ... ...

    Abstract Fewer than 20% of triple-negative breast cancer patients experience long-term responses to mainstay chemotherapy. Resistant tumor subpopulations use alternative metabolic pathways to escape therapy, survive, and eventually recur. Here, we show in vivo, longitudinal metabolic reprogramming in residual disease and recurrence of triple-negative breast cancer xenografts with varying sensitivities to the chemotherapeutic drug paclitaxel. Optical imaging coupled with metabolomics reported an increase in non-glucose-driven mitochondrial metabolism and an increase in intratumoral metabolic heterogeneity during regression and residual disease in resistant MDA-MB-231 tumors. Conversely, sensitive HCC-1806 tumors were primarily reliant on glucose uptake and minimal changes in metabolism or heterogeneity were observed over the tumors' therapeutic life cycles. Further, day-matched resistant HCC-1806 tumors revealed a higher reliance on mitochondrial metabolism and elevated metabolic heterogeneity compared to sensitive HCC-1806 tumors. Together, metabolic flexibility, increased reliance on mitochondrial metabolism, and increased metabolic heterogeneity are defining characteristics of persistent residual disease, features that will inform the appropriate type and timing of therapies.
    MeSH term(s) Humans ; Metabolic Reprogramming ; Triple Negative Breast Neoplasms/drug therapy ; Triple Negative Breast Neoplasms/genetics ; Triple Negative Breast Neoplasms/pathology ; Carcinoma, Hepatocellular/drug therapy ; Liver Neoplasms/drug therapy ; Antineoplastic Agents/pharmacology ; Optical Imaging ; Cell Line, Tumor
    Chemical Substances Antineoplastic Agents
    Language English
    Publishing date 2024-04-05
    Publishing country United States
    Document type Journal Article
    ZDB-ID 2810933-8
    ISSN 2375-2548 ; 2375-2548
    ISSN (online) 2375-2548
    ISSN 2375-2548
    DOI 10.1126/sciadv.adj7540
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  10. Article ; Online: Metabolic Regulation by Lysine Malonylation, Succinylation, and Glutarylation.

    Hirschey, Matthew D / Zhao, Yingming

    Molecular & cellular proteomics : MCP

    2015  Volume 14, Issue 9, Page(s) 2308–2315

    Abstract: Protein acetylation is a well-studied regulatory mechanism for several cellular processes, ranging from gene expression to metabolism. Recent discoveries of new post-translational modifications, including malonylation, succinylation, and glutarylation, ... ...

    Abstract Protein acetylation is a well-studied regulatory mechanism for several cellular processes, ranging from gene expression to metabolism. Recent discoveries of new post-translational modifications, including malonylation, succinylation, and glutarylation, have expanded our understanding of the types of modifications found on proteins. These three acidic lysine modifications are structurally similar but have the potential to regulate different proteins in different pathways. The deacylase sirtuin 5 (SIRT5) catalyzes the removal of these modifications from a wide range of proteins in different subcellular compartments. Here, we review these new modifications, their regulation by SIRT5, and their emerging role in cellular regulation and diseases.
    MeSH term(s) Acylation ; Animals ; Gene Expression Regulation ; Humans ; Intracellular Space/metabolism ; Lysine/metabolism ; NAD/metabolism ; Protein Processing, Post-Translational ; Proteins/metabolism ; Sirtuins/metabolism
    Chemical Substances Proteins ; NAD (0U46U6E8UK) ; SIRT5 protein, human (EC 3.5.1.-) ; Sirtuins (EC 3.5.1.-) ; Lysine (K3Z4F929H6)
    Language English
    Publishing date 2015-02-25
    Publishing country United States
    Document type Journal Article ; Research Support, N.I.H., Extramural ; Research Support, Non-U.S. Gov't ; Review
    ZDB-ID 2075924-1
    ISSN 1535-9484 ; 1535-9476
    ISSN (online) 1535-9484
    ISSN 1535-9476
    DOI 10.1074/mcp.R114.046664
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