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  1. Article ; Online: Probing lysine posttranslational modifications by unnatural amino acids.

    Maas, Marijn N / Hintzen, Jordi C J / Mecinović, Jasmin

    Chemical communications (Cambridge, England)

    2022  Volume 58, Issue 52, Page(s) 7216–7231

    Abstract: Posttranslational modifications, typically small chemical tags attached on amino acids following protein biosynthesis, have a profound effect on protein structure and function. Numerous chemically and structurally diverse posttranslational modifications, ...

    Abstract Posttranslational modifications, typically small chemical tags attached on amino acids following protein biosynthesis, have a profound effect on protein structure and function. Numerous chemically and structurally diverse posttranslational modifications, including methylation, acetylation, hydroxylation, and ubiquitination, have been identified and characterised on lysine residues in proteins. In this feature article, we focus on chemical tools that rely on the site-specific incorporation of unnatural amino acids into peptides and proteins to probe posttranslational modifications of lysine. We highlight that simple amino acid mimics enable detailed mechanistic and functional assignment of enzymes that install and remove such modifications, and proteins that specifically recognise lysine posttranslational modifications.
    MeSH term(s) Acetylation ; Amino Acids/metabolism ; Lysine/chemistry ; Protein Processing, Post-Translational ; Proteins/metabolism ; Ubiquitination
    Chemical Substances Amino Acids ; Proteins ; Lysine (K3Z4F929H6)
    Language English
    Publishing date 2022-06-28
    Publishing country England
    Document type Journal Article ; Review
    ZDB-ID 1472881-3
    ISSN 1364-548X ; 1359-7345 ; 0009-241X
    ISSN (online) 1364-548X
    ISSN 1359-7345 ; 0009-241X
    DOI 10.1039/d2cc00708h
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  2. Article ; Online: Recognition of stapled histone H3K4me3 peptides by epigenetic reader proteins.

    Betlem, Peter / Maas, Marijn N / Middelburg, Jim / Pieters, Bas J G E / Mecinović, Jasmin

    Chemical communications (Cambridge, England)

    2022  Volume 58, Issue 87, Page(s) 12196–12199

    Abstract: The flexible N-terminal histone tails are a subject of numerous posttranslational modifications ...

    Abstract The flexible N-terminal histone tails are a subject of numerous posttranslational modifications, including methylation. We report development of stapled histone peptides bearing trimethyllysine as ligands for epigenetic reader proteins. Stronger or weaker binding affinities have been observed for stapled histone peptides relative to linear histones, indicating that selectivity towards reader proteins can be achieved.
    MeSH term(s) Histones/metabolism ; Methylation ; Peptides/metabolism ; Epigenesis, Genetic
    Chemical Substances histone H3 trimethyl Lys4 ; Histones ; Peptides
    Language English
    Publishing date 2022-11-01
    Publishing country England
    Document type 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/d2cc04294k
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  3. Article: Probing lysine posttranslational modifications by unnatural amino acids

    Maas, Marijn N. / Hintzen, Jordi C. J. / Mecinović, Jasmin

    Chemical communications. 2022 June 28, v. 58, no. 52

    2022  

    Abstract: Posttranslational modifications, typically small chemical tags attached on amino acids following protein biosynthesis, have a profound effect on protein structure and function. Numerous chemically and structurally diverse posttranslational modifications, ...

    Abstract Posttranslational modifications, typically small chemical tags attached on amino acids following protein biosynthesis, have a profound effect on protein structure and function. Numerous chemically and structurally diverse posttranslational modifications, including methylation, acetylation, hydroxylation, and ubiquitination, have been identified and characterised on lysine residues in proteins. In this feature article, we focus on chemical tools that rely on the site-specific incorporation of unnatural amino acids into peptides and proteins to probe posttranslational modifications of lysine. We highlight that simple amino acid mimics enable detailed mechanistic and functional assignment of enzymes that install and remove such modifications, and proteins that specifically recognise lysine posttranslational modifications.
    Keywords acetylation ; hydroxylation ; lysine ; methylation ; peptides ; protein structure ; ubiquitination
    Language English
    Dates of publication 2022-0628
    Size p. 7216-7231.
    Publishing place The Royal Society of Chemistry
    Document type Article
    ZDB-ID 1472881-3
    ISSN 1364-548X ; 1359-7345 ; 0009-241X
    ISSN (online) 1364-548X
    ISSN 1359-7345 ; 0009-241X
    DOI 10.1039/d2cc00708h
    Database NAL-Catalogue (AGRICOLA)

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  4. Article ; Online: Importance of Ile71 in β-actin on histidine methyltransferase SETD3 catalysis.

    Bilgin, Nurgül / Moesgaard, Laust / Maas, Marijn N / Hintzen, Jordi C J / Witecka, Apolonia / Drozak, Jakub / Kongsted, Jacob / Mecinović, Jasmin

    Organic & biomolecular chemistry

    2022  Volume 20, Issue 8, Page(s) 1723–1730

    Abstract: ... SETD3- ... ...

    Abstract SETD3-catalysed
    MeSH term(s) Actins/chemistry ; Actins/metabolism ; Biocatalysis ; Histidine/chemistry ; Histidine/metabolism ; Histone Methyltransferases/metabolism ; Humans ; Isoleucine/chemistry ; Isoleucine/metabolism ; Models, Molecular ; Molecular Conformation
    Chemical Substances Actins ; Isoleucine (04Y7590D77) ; Histidine (4QD397987E) ; Histone Methyltransferases (EC 2.1.1.-) ; SETD3 protein, human (EC 2.1.1.43)
    Language English
    Publishing date 2022-02-23
    Publishing country England
    Document type Journal Article ; Research Support, Non-U.S. Gov't
    ZDB-ID 2097583-1
    ISSN 1477-0539 ; 1477-0520
    ISSN (online) 1477-0539
    ISSN 1477-0520
    DOI 10.1039/d1ob02430b
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  5. Article ; Online: Targeting SARS-CoV-2 spike protein by stapled hACE2 peptides.

    Maas, Marijn N / Hintzen, Jordi C J / Löffler, Philipp M G / Mecinović, Jasmin

    Chemical communications (Cambridge, England)

    2021  Volume 57, Issue 26, Page(s) 3283–3286

    Abstract: SARS-CoV-2 Spike protein RBD interacts with the hACE2 receptor to initiate cell entry and infection. We set out to develop lactam-based i,i + 4 stapled hACE2 peptides targeting SARS-CoV-2. In vitro screening demonstrates the inhibition of the Spike ... ...

    Abstract SARS-CoV-2 Spike protein RBD interacts with the hACE2 receptor to initiate cell entry and infection. We set out to develop lactam-based i,i + 4 stapled hACE2 peptides targeting SARS-CoV-2. In vitro screening demonstrates the inhibition of the Spike protein RBD-hACE2 complex formation by the hACE2
    MeSH term(s) Amino Acid Sequence ; Angiotensin-Converting Enzyme 2/chemistry ; Angiotensin-Converting Enzyme 2/metabolism ; COVID-19/metabolism ; COVID-19/virology ; Humans ; Peptides/chemistry ; Peptides/metabolism ; Peptidomimetics ; SARS-CoV-2/metabolism ; Spike Glycoprotein, Coronavirus/antagonists & inhibitors ; Spike Glycoprotein, Coronavirus/chemistry ; Spike Glycoprotein, Coronavirus/metabolism
    Chemical Substances Peptides ; Peptidomimetics ; Spike Glycoprotein, Coronavirus ; spike protein, SARS-CoV-2 ; ACE2 protein, human (EC 3.4.17.23) ; Angiotensin-Converting Enzyme 2 (EC 3.4.17.23)
    Language English
    Publishing date 2021-03-02
    Publishing country England
    Document type 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/d0cc08387a
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  6. Article ; Online: Trimethyllysine: From Carnitine Biosynthesis to Epigenetics.

    Maas, Marijn N / Hintzen, Jordi C J / Porzberg, Miriam R B / Mecinović, Jasmin

    International journal of molecular sciences

    2020  Volume 21, Issue 24

    Abstract: Trimethyllysine is an important post-translationally modified amino acid with functions in the carnitine biosynthesis and regulation of key epigenetic processes. Protein lysine methyltransferases and demethylases dynamically control protein lysine ... ...

    Abstract Trimethyllysine is an important post-translationally modified amino acid with functions in the carnitine biosynthesis and regulation of key epigenetic processes. Protein lysine methyltransferases and demethylases dynamically control protein lysine methylation, with each state of methylation changing the biophysical properties of lysine and the subsequent effect on protein function, in particular histone proteins and their central role in epigenetics. Epigenetic reader domain proteins can distinguish between different lysine methylation states and initiate downstream cellular processes upon recognition. Dysregulation of protein methylation is linked to various diseases, including cancer, inflammation, and genetic disorders. In this review, we cover biomolecular studies on the role of trimethyllysine in carnitine biosynthesis, different enzymatic reactions involved in the synthesis and removal of trimethyllysine, trimethyllysine recognition by reader proteins, and the role of trimethyllysine on the nucleosome assembly.
    MeSH term(s) Animals ; Carnitine/metabolism ; Epigenesis, Genetic/genetics ; Histone-Lysine N-Methyltransferase/genetics ; Histone-Lysine N-Methyltransferase/metabolism ; Humans ; Lysine/analogs & derivatives ; Lysine/metabolism ; Protein Processing, Post-Translational/genetics ; Protein Processing, Post-Translational/physiology
    Chemical Substances trimethyllysine (3YGF0495O2) ; Histone-Lysine N-Methyltransferase (EC 2.1.1.43) ; Lysine (K3Z4F929H6) ; Carnitine (S7UI8SM58A)
    Language English
    Publishing date 2020-12-11
    Publishing country Switzerland
    Document type Journal Article ; Review
    ZDB-ID 2019364-6
    ISSN 1422-0067 ; 1422-0067 ; 1661-6596
    ISSN (online) 1422-0067
    ISSN 1422-0067 ; 1661-6596
    DOI 10.3390/ijms21249451
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  7. Article ; Online: Trimethyllysine

    Marijn N. Maas / Jordi C.J. Hintzen / Miriam R.B. Porzberg / Jasmin Mecinović

    International Journal of Molecular Sciences, Vol 21, Iss 9451, p

    From Carnitine Biosynthesis to Epigenetics

    2020  Volume 9451

    Abstract: Trimethyllysine is an important post-translationally modified amino acid with functions in the carnitine biosynthesis and regulation of key epigenetic processes. Protein lysine methyltransferases and demethylases dynamically control protein lysine ... ...

    Abstract Trimethyllysine is an important post-translationally modified amino acid with functions in the carnitine biosynthesis and regulation of key epigenetic processes. Protein lysine methyltransferases and demethylases dynamically control protein lysine methylation, with each state of methylation changing the biophysical properties of lysine and the subsequent effect on protein function, in particular histone proteins and their central role in epigenetics. Epigenetic reader domain proteins can distinguish between different lysine methylation states and initiate downstream cellular processes upon recognition. Dysregulation of protein methylation is linked to various diseases, including cancer, inflammation, and genetic disorders. In this review, we cover biomolecular studies on the role of trimethyllysine in carnitine biosynthesis, different enzymatic reactions involved in the synthesis and removal of trimethyllysine, trimethyllysine recognition by reader proteins, and the role of trimethyllysine on the nucleosome assembly.
    Keywords trimethyllysine ; epigenetics ; post-translational modifications ; protein lysine methyltransferases ; protein lysine demethylases ; carnitine ; Biology (General) ; QH301-705.5 ; Chemistry ; QD1-999
    Subject code 570
    Language English
    Publishing date 2020-12-01T00:00:00Z
    Publisher MDPI AG
    Document type Article ; Online
    Database BASE - Bielefeld Academic Search Engine (life sciences selection)

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  8. Article ; Online: Amide-derived lysine analogues as substrates and inhibitors of histone lysine methyltransferases and acetyltransferases.

    Hintzen, Jordi C J / Merx, Jona / Maas, Marijn N / Langens, Sabine G H A / White, Paul B / Boltje, Thomas J / Mecinović, Jasmin

    Organic & biomolecular chemistry

    2021  Volume 20, Issue 1, Page(s) 173–181

    Abstract: Histone lysine methyltransferases and acetyltransferases are two classes of epigenetic enzymes that play pivotal roles in human gene regulation. Although they both recognise and posttranslationally modify lysine residues in histone proteins, their ... ...

    Abstract Histone lysine methyltransferases and acetyltransferases are two classes of epigenetic enzymes that play pivotal roles in human gene regulation. Although they both recognise and posttranslationally modify lysine residues in histone proteins, their difference in histone peptide-based substrates and inhibitors remains to be firmly established. Here, we have synthesised lysine mimics that posses an amide bond linker in the side chain, incorporated them into histone H3 tail peptides, and examined synthetic histone peptides as substrates and inhibitors for human lysine methyltransferases and acetyltransferases. This work demonstrates that histone lysine methyltransferases G9a and GLP do catalyse methylation of the most similar lysine mimic, whereas they typically do not tolerate more sterically demanding side chains. In contrast, histone lysine acetyltransferases GCN5 and PCAF do not catalyse acetylation of the same panel of lysine analogues. Our results also identify potent H3-based inhibitors of GLP methyltransferase, providing a basis for development of peptidomimetics for targeting KMT enzymes.
    MeSH term(s) Acetyltransferases/metabolism ; Amides/chemistry ; Amides/pharmacology ; Enzyme Inhibitors/chemical synthesis ; Enzyme Inhibitors/chemistry ; Enzyme Inhibitors/pharmacology ; Histone-Lysine N-Methyltransferase/antagonists & inhibitors ; Histone-Lysine N-Methyltransferase/metabolism ; Humans ; Lysine/chemical synthesis ; Lysine/chemistry ; Lysine/pharmacology ; Models, Molecular ; Molecular Structure
    Chemical Substances Amides ; Enzyme Inhibitors ; Histone-Lysine N-Methyltransferase (EC 2.1.1.43) ; Acetyltransferases (EC 2.3.1.-) ; Lysine (K3Z4F929H6)
    Language English
    Publishing date 2021-12-22
    Publishing country England
    Document type Journal Article ; Research Support, Non-U.S. Gov't
    ZDB-ID 2097583-1
    ISSN 1477-0539 ; 1477-0520
    ISSN (online) 1477-0539
    ISSN 1477-0520
    DOI 10.1039/d1ob02191e
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  9. Article ; Online: Key role for lipids in cognitive symptoms of schizophrenia.

    Maas, Dorien A / Martens, Marijn B / Priovoulos, Nikos / Zuure, Wieteke A / Homberg, Judith R / Nait-Oumesmar, Brahim / Martens, Gerard J M

    Translational psychiatry

    2020  Volume 10, Issue 1, Page(s) 399

    Abstract: Schizophrenia (SZ) is a psychiatric disorder with a convoluted etiology that includes cognitive symptoms, which arise from among others a dysfunctional dorsolateral prefrontal cortex (dlPFC). In our search for the molecular underpinnings of the cognitive ...

    Abstract Schizophrenia (SZ) is a psychiatric disorder with a convoluted etiology that includes cognitive symptoms, which arise from among others a dysfunctional dorsolateral prefrontal cortex (dlPFC). In our search for the molecular underpinnings of the cognitive deficits in SZ, we here performed RNA sequencing of gray matter from the dlPFC of SZ patients and controls. We found that the differentially expressed RNAs were enriched for mRNAs involved in the Liver X Receptor/Retinoid X Receptor (LXR/RXR) lipid metabolism pathway. Components of the LXR/RXR pathway were upregulated in gray matter but not in white matter of SZ dlPFC. Intriguingly, an analysis for shared genetic etiology, using two SZ genome-wide association studies (GWASs) and GWAS data for 514 metabolites, revealed genetic overlap between SZ and acylcarnitines, VLDL lipids, and fatty acid metabolites, which are all linked to the LXR/RXR signaling pathway. Furthermore, analysis of structural T
    MeSH term(s) Cognition ; Genome-Wide Association Study ; Gray Matter/diagnostic imaging ; Humans ; Lipids ; Magnetic Resonance Imaging ; Prefrontal Cortex ; Schizophrenia/genetics
    Chemical Substances Lipids
    Language English
    Publishing date 2020-11-12
    Publishing country United States
    Document type Journal Article ; Research Support, Non-U.S. Gov't
    ZDB-ID 2609311-X
    ISSN 2158-3188 ; 2158-3188
    ISSN (online) 2158-3188
    ISSN 2158-3188
    DOI 10.1038/s41398-020-01084-x
    Database MEDical Literature Analysis and Retrieval System OnLINE

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