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Article ; Online: Selective Pharmaceutical Inhibition of PARP14 Mitigates Allergen-Induced IgE and Mucus Overproduction in a Mouse Model of Pulmonary Allergic Response.

Eddie, Alex M / Chen, Kevin W / Schenkel, Laurie B / Swinger, Kerren K / Molina, Jennifer R / Kunii, Kaiko / Raybuck, Ariel L / Keilhack, Heike / Gibson-Corley, Katherine N / Niepel, Mario / Peebles, R Stokes / Boothby, Mark R / Cho, Sung Hoon

ImmunoHorizons

2022 Volume 6, Issue 7, Page(s) 432–446

Abstract: The type 2 cytokines IL-4 and IL-13, which share use of an IL-4 receptor α-chain and its nuclear induction of the transcription factor STAT6, are crucial in elicitation and maintenance of allergic conditions including asthma. STAT6 binds poly(ADP-ribose) ...

Abstract	The type 2 cytokines IL-4 and IL-13, which share use of an IL-4 receptor α-chain and its nuclear induction of the transcription factor STAT6, are crucial in elicitation and maintenance of allergic conditions including asthma. STAT6 binds poly(ADP-ribose) polymerase (PARP)14, an ADP-ribosyl monotransferase. Elimination of PARP14 by gene targeting led to attenuation of OVA-specific allergic lung inflammation. However, PARP14 has multiple functional domains apart from the portion that catalyzes ADP-ribosylation, and it is not clear whether inhibition of the catalytic function has any biological consequence. Using BALB/c mice sensitized to the allergen
MeSH term(s)	Allergens ; Animals ; Asthma/drug therapy ; Disease Models, Animal ; Immunoglobulin E ; Mice ; Mucus/metabolism ; Pharmaceutical Preparations/metabolism ; Poly(ADP-ribose) Polymerase Inhibitors/metabolism ; Poly(ADP-ribose) Polymerase Inhibitors/pharmacology ; Poly(ADP-ribose) Polymerase Inhibitors/therapeutic use ; Poly(ADP-ribose) Polymerases/genetics ; Poly(ADP-ribose) Polymerases/metabolism ; Poly(ADP-ribose) Polymerases/therapeutic use
Chemical Substances	Allergens ; Pharmaceutical Preparations ; Poly(ADP-ribose) Polymerase Inhibitors ; Immunoglobulin E (37341-29-0) ; Parp14 protein, mouse (EC 2.4.2.30) ; Poly(ADP-ribose) Polymerases (EC 2.4.2.30)
Language	English
Publishing date	2022-07-11
Publishing country	United States
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ISSN	2573-7732
ISSN (online)	2573-7732
DOI	10.4049/immunohorizons.2100107
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Article ; Online: Forced Self-Modification Assays as a Strategy to Screen MonoPARP Enzymes.

Wigle, Tim J / Church, W David / Majer, Christina R / Swinger, Kerren K / Aybar, Demet / Schenkel, Laurie B / Vasbinder, Melissa M / Brendes, Arne / Beck, Claudia / Prahm, Martin / Wegener, Dennis / Chang, Paul / Kuntz, Kevin W

SLAS discovery : advancing life sciences R & D

2019 Volume 25, Issue 3, Page(s) 241–252

Abstract: Mono(ADP-ribosylation) (MARylation) and poly(ADP-ribosylation) (PARylation) are posttranslational modifications found on multiple amino acids. There are 12 enzymatically active mono(ADP-ribose) polymerase (monoPARP) enzymes and 4 enzymatically active ... ...

Abstract	Mono(ADP-ribosylation) (MARylation) and poly(ADP-ribosylation) (PARylation) are posttranslational modifications found on multiple amino acids. There are 12 enzymatically active mono(ADP-ribose) polymerase (monoPARP) enzymes and 4 enzymatically active poly(ADP-ribose) polymerase (polyPARP) enzymes that use nicotinamide adenine dinucleotide (NAD
MeSH term(s)	ADP Ribose Transferases/antagonists & inhibitors ; ADP Ribose Transferases/chemistry ; ADP Ribose Transferases/genetics ; ADP-Ribosylation/genetics ; Adenosine Diphosphate Ribose/genetics ; Enzyme Inhibitors/isolation & purification ; Enzyme Inhibitors/pharmacology ; High-Throughput Screening Assays ; Humans ; NAD/chemistry ; Poly ADP Ribosylation/genetics ; Poly(ADP-ribose) Polymerase Inhibitors/chemistry ; Poly(ADP-ribose) Polymerase Inhibitors/isolation & purification ; Poly(ADP-ribose) Polymerases/drug effects ; Poly(ADP-ribose) Polymerases/genetics ; Protein Processing, Post-Translational/genetics ; Substrate Specificity
Chemical Substances	Enzyme Inhibitors ; Poly(ADP-ribose) Polymerase Inhibitors ; NAD (0U46U6E8UK) ; Adenosine Diphosphate Ribose (20762-30-5) ; ADP Ribose Transferases (EC 2.4.2.-) ; Poly(ADP-ribose) Polymerases (EC 2.4.2.30)
Language	English
Publishing date	2019-12-19
Publishing country	United States
Document type	Journal Article
ZDB-ID	2885123-7
ISSN	2472-5560 ; 2472-5552
ISSN (online)	2472-5560
ISSN	2472-5552
DOI	10.1177/2472555219883623
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Zs.A 4911: Show issues

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Article: Self-condensation of N-tert-butanesulfinyl aldimines: application to the rapid asymmetric synthesis of biologically important amine-containing compounds.

Schenkel, Laurie B / Ellman, Jonathan A

Organic letters

2004 Volume 6, Issue 20, Page(s) 3621–3624

Abstract: reaction: see text] Highly diastereoselective intra- and intermolecular self-condensation reactions of N-tert-butanesulfinyl aldimines have been developed and applied to the rapid, asymmetric synthesis of trans-2-aminocyclopentanecarboxylic acid and the ...

Abstract	[reaction: see text] Highly diastereoselective intra- and intermolecular self-condensation reactions of N-tert-butanesulfinyl aldimines have been developed and applied to the rapid, asymmetric synthesis of trans-2-aminocyclopentanecarboxylic acid and the drug candidate SC-53116. Key to both syntheses is a novel microwave-assisted reaction in which N-sulfinyl aldimines are cleanly converted into nitriles in high-yielding concerted elimination processes.
MeSH term(s)	Amines/chemical synthesis ; Amines/chemistry ; Benzamides/chemical synthesis ; Catalysis ; Indicators and Reagents ; Microwaves ; Molecular Structure ; Nitriles/chemical synthesis ; Pyrroles/chemical synthesis
Chemical Substances	Amines ; Benzamides ; Indicators and Reagents ; Nitriles ; Pyrroles ; SC 53116 (141196-99-8)
Language	English
Publishing date	2004-09-30
Publishing country	United States
Document type	Journal Article ; Research Support, Non-U.S. Gov't ; Research Support, U.S. Gov't, Non-P.H.S.
ISSN	1523-7060
ISSN	1523-7060
DOI	10.1021/ol048458j
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Article: Application of P,N-sulfinyl imine ligands to iridium-catalyzed asymmetric hydrogenation of olefins.

Schenkel, Laurie B / Ellman, Jonathan A

The Journal of organic chemistry

2004 Volume 69, Issue 6, Page(s) 1800–1802

Abstract: The utility of a novel class of P,N-ligands incorporating a chiral sulfinyl imine moiety is demonstrated in the iridium-catalyzed hydrogenation of both functionalized and unfunctionalized olefins, in which enantioselectivities of up to 94% are achieved. ... ...

Abstract	The utility of a novel class of P,N-ligands incorporating a chiral sulfinyl imine moiety is demonstrated in the iridium-catalyzed hydrogenation of both functionalized and unfunctionalized olefins, in which enantioselectivities of up to 94% are achieved. The modularity of the P,N-sulfinyl ligand class is highlighted by the facile preparation of a variety of sterically and electronically different ligands. Interesting structure-activity data for both the phosphine and sulfinamide components is provided by this expanded ligand set.
MeSH term(s)	Alkenes/chemistry ; Amides/chemistry ; Catalysis ; Hydrogenation ; Imines/chemistry ; Iridium/chemistry ; Ligands ; Phosphines/chemistry ; Stereoisomerism ; Stilbenes/chemistry ; Sulfonium Compounds/chemistry
Chemical Substances	Alkenes ; Amides ; Imines ; Ligands ; Phosphines ; Stilbenes ; Sulfonium Compounds ; Iridium (44448S9773)
Language	English
Publishing date	2004-03-19
Publishing country	United States
Document type	Journal Article ; Research Support, Non-U.S. Gov't ; Research Support, U.S. Gov't, Non-P.H.S.
ZDB-ID	123490-0
ISSN	1520-6904 ; 0022-3263
ISSN (online)	1520-6904
ISSN	0022-3263
DOI	10.1021/jo035675+
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Zs.A 4473: Show issues

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Article ; Online: In Vitro and Cellular Probes to Study PARP Enzyme Target Engagement.

Wigle, Tim J / Blackwell, Danielle J / Schenkel, Laurie B / Ren, Yue / Church, W David / Desai, Hetvi J / Swinger, Kerren K / Santospago, Andrew G / Majer, Christina R / Lu, Alvin Z / Niepel, Mario / Perl, Nicholas R / Vasbinder, Melissa M / Keilhack, Heike / Kuntz, Kevin W

Cell chemical biology

2020 Volume 27, Issue 7, Page(s) 877–887.e14

Abstract: Poly(ADP-ribose) polymerase (PARP) enzymes use nicotinamide adenine dinucleotide ( ... ...

Abstract	Poly(ADP-ribose) polymerase (PARP) enzymes use nicotinamide adenine dinucleotide (NAD
MeSH term(s)	Binding, Competitive ; Fluorescence Resonance Energy Transfer ; Fluorescent Dyes/chemical synthesis ; Fluorescent Dyes/chemistry ; Fluorescent Dyes/metabolism ; HEK293 Cells ; Humans ; Isoenzymes/antagonists & inhibitors ; Isoenzymes/genetics ; Isoenzymes/metabolism ; Kinetics ; NAD/chemistry ; NAD/metabolism ; Nanoparticles/chemistry ; Poly(ADP-ribose) Polymerase Inhibitors/chemical synthesis ; Poly(ADP-ribose) Polymerase Inhibitors/chemistry ; Poly(ADP-ribose) Polymerase Inhibitors/metabolism ; Poly(ADP-ribose) Polymerases/chemistry ; Poly(ADP-ribose) Polymerases/genetics ; Poly(ADP-ribose) Polymerases/metabolism ; Protein Binding ; Recombinant Proteins/biosynthesis ; Recombinant Proteins/isolation & purification ; Recombinant Proteins/metabolism ; Surface Plasmon Resonance
Chemical Substances	Fluorescent Dyes ; Isoenzymes ; Poly(ADP-ribose) Polymerase Inhibitors ; Recombinant Proteins ; NAD (0U46U6E8UK) ; Poly(ADP-ribose) Polymerases (EC 2.4.2.30)
Language	English
Publishing date	2020-08-06
Publishing country	United States
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ISSN	2451-9448
ISSN (online)	2451-9448
DOI	10.1016/j.chembiol.2020.06.009
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Article: Novel sulfinyl imine ligands for asymmetric catalysis.

Schenkel, Laurie B / Ellman, Jonathan A

Organic letters

2003 Volume 5, Issue 4, Page(s) 545–548

Abstract: structure: see text] A novel class of P,N-sulfinyl imine ligands has been prepared that incorporates chirality solely at sulfur. The Pd complex of ligand 14 catalyzes the allylic alkylation reaction with high enantioselectivity (94%), and the first ... ...

Abstract	[structure: see text] A novel class of P,N-sulfinyl imine ligands has been prepared that incorporates chirality solely at sulfur. The Pd complex of ligand 14 catalyzes the allylic alkylation reaction with high enantioselectivity (94%), and the first crystal structure of a Pd-bound sulfinyl imine provides insight into binding mode and origins of stereoselectivity.
Language	English
Publishing date	2003-02-20
Publishing country	United States
Document type	Journal Article
ISSN	1523-7060
ISSN	1523-7060
DOI	10.1021/ol027468m
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Article ; Online: A potent and selective PARP14 inhibitor decreases protumor macrophage gene expression and elicits inflammatory responses in tumor explants.

Cell chemical biology

2021 Volume 28, Issue 8, Page(s) 1158–1168.e13

Abstract: PARP14 has been implicated by genetic knockout studies to promote protumor macrophage polarization and suppress the antitumor inflammatory response due to its role in modulating interleukin-4 (IL-4) and interferon-γ signaling pathways. Here, we describe ... ...

Abstract	PARP14 has been implicated by genetic knockout studies to promote protumor macrophage polarization and suppress the antitumor inflammatory response due to its role in modulating interleukin-4 (IL-4) and interferon-γ signaling pathways. Here, we describe structure-based design efforts leading to the discovery of a potent and highly selective PARP14 chemical probe. RBN012759 inhibits PARP14 with a biochemical half-maximal inhibitory concentration of 0.003 μM, exhibits >300-fold selectivity over all PARP family members, and its profile enables further study of PARP14 biology and disease association both in vitro and in vivo. Inhibition of PARP14 with RBN012759 reverses IL-4-driven protumor gene expression in macrophages and induces an inflammatory mRNA signature similar to that induced by immune checkpoint inhibitor therapy in primary human tumor explants. These data support an immune suppressive role of PARP14 in tumors and suggest potential utility of PARP14 inhibitors in the treatment of cancer.
MeSH term(s)	Animals ; Antineoplastic Agents/chemical synthesis ; Antineoplastic Agents/chemistry ; Antineoplastic Agents/pharmacology ; Dose-Response Relationship, Drug ; Female ; Gene Expression Regulation/drug effects ; Gene Expression Regulation/genetics ; HEK293 Cells ; Humans ; Inflammation/drug therapy ; Inflammation/genetics ; Inflammation/metabolism ; Interleukin-4/antagonists & inhibitors ; Interleukin-4/genetics ; Kidney Neoplasms/drug therapy ; Kidney Neoplasms/genetics ; Kidney Neoplasms/metabolism ; Macrophages/drug effects ; Macrophages/metabolism ; Male ; Mice ; Mice, Inbred C57BL ; Models, Molecular ; Molecular Structure ; Poly(ADP-ribose) Polymerases/genetics ; Poly(ADP-ribose) Polymerases/metabolism ; RAW 264.7 Cells ; RNA, Messenger/drug effects ; RNA, Messenger/genetics ; RNA, Messenger/metabolism
Chemical Substances	Antineoplastic Agents ; RNA, Messenger ; Interleukin-4 (207137-56-2) ; PARP14 protein, human (EC 2.4.2.30) ; Parp14 protein, mouse (EC 2.4.2.30) ; Poly(ADP-ribose) Polymerases (EC 2.4.2.30)
Language	English
Publishing date	2021-03-10
Publishing country	United States
Document type	Journal Article
ISSN	2451-9448
ISSN (online)	2451-9448
DOI	10.1016/j.chembiol.2021.02.010
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Article ; Online: Targeted Degradation of PARP14 Using a Heterobifunctional Small Molecule.

Wigle, Tim J / Ren, Yue / Molina, Jennifer R / Blackwell, Danielle J / Schenkel, Laurie B / Swinger, Kerren K / Kuplast-Barr, Kristy / Majer, Christina R / Church, W David / Lu, Alvin Z / Mo, Jason / Abo, Ryan / Cheung, Anne / Dorsey, Bryan W / Niepel, Mario / Perl, Nicholas R / Vasbinder, Melissa M / Keilhack, Heike / Kuntz, Kevin W

Chembiochem : a European journal of chemical biology

2021 Volume 22, Issue 12, Page(s) 2107–2110

Abstract: PARP14 is an interferon-stimulated gene that is overexpressed in multiple tumor types, influencing pro-tumor macrophage polarization as well as suppressing the antitumor inflammation response by modulating IFN-γ and IL-4 signaling. PARP14 is a 203 kDa ... ...

Abstract	PARP14 is an interferon-stimulated gene that is overexpressed in multiple tumor types, influencing pro-tumor macrophage polarization as well as suppressing the antitumor inflammation response by modulating IFN-γ and IL-4 signaling. PARP14 is a 203 kDa protein that possesses a catalytic domain responsible for the transfer of mono-ADP-ribose to its substrates. PARP14 also contains three macrodomains and a WWE domain which are binding modules for mono-ADP-ribose and poly-ADP-ribose, respectively, in addition to two RNA recognition motifs. Catalytic inhibitors of PARP14 have been shown to reverse IL-4 driven pro-tumor gene expression in macrophages, however it is not clear what roles the non-enzymatic biomolecular recognition motifs play in PARP14-driven immunology and inflammation. To further understand this, we have discovered a heterobifunctional small molecule designed based on a catalytic inhibitor of PARP14 that binds in the enzyme's NAD
MeSH term(s)	Humans ; Macrophages/drug effects ; Macrophages/metabolism ; Molecular Structure ; Poly(ADP-ribose) Polymerases/metabolism ; Small Molecule Libraries/chemical synthesis ; Small Molecule Libraries/chemistry ; Small Molecule Libraries/pharmacology
Chemical Substances	Small Molecule Libraries ; PARP14 protein, human (EC 2.4.2.30) ; Poly(ADP-ribose) Polymerases (EC 2.4.2.30)
Language	English
Publishing date	2021-05-04
Publishing country	Germany
Document type	Journal Article
ZDB-ID	2020469-3
ISSN	1439-7633 ; 1439-4227
ISSN (online)	1439-7633
ISSN	1439-4227
DOI	10.1002/cbic.202100047
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Article ; Online: Discovery of a biarylamide series of potent, state-dependent Na

Schenkel, Laurie B / DiMauro, Erin F / Nguyen, Hanh N / Chakka, Nagasree / Du, Bingfan / Foti, Robert S / Guzman-Perez, Angel / Jarosh, Michael / La, Daniel S / Ligutti, Joseph / Milgram, Benjamin C / Moyer, Bryan D / Peterson, Emily A / Roberts, John / Yu, Violeta L / Weiss, Matthew M

Bioorganic & medicinal chemistry letters

2017 Volume 27, Issue 16, Page(s) 3817–3824

Abstract: ... The ... ...

Abstract	The Na
MeSH term(s)	Amides/chemical synthesis ; Amides/chemistry ; Amides/pharmacology ; Animals ; Dose-Response Relationship, Drug ; Drug Discovery ; Humans ; Mice ; Molecular Structure ; NAV1.7 Voltage-Gated Sodium Channel/metabolism ; Rats ; Structure-Activity Relationship
Chemical Substances	Amides ; NAV1.7 Voltage-Gated Sodium Channel ; SCN9A protein, human ; Scn9a protein, mouse ; Scn9a protein, rat
Language	English
Publishing date	2017--15
Publishing country	England
Document type	Journal Article
ZDB-ID	1063195-1
ISSN	1464-3405 ; 0960-894X
ISSN (online)	1464-3405
ISSN	0960-894X
DOI	10.1016/j.bmcl.2017.06.054
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Zs.A 3203: Show issues

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Article ; Online: Optimization of a Novel Quinazolinone-Based Series of Transient Receptor Potential A1 (TRPA1) Antagonists Demonstrating Potent in Vivo Activity.

Schenkel, Laurie B / Olivieri, Philip R / Boezio, Alessandro A / Deak, Holly L / Emkey, Renee / Graceffa, Russell F / Gunaydin, Hakan / Guzman-Perez, Angel / Lee, Josie H / Teffera, Yohannes / Wang, Weiya / Youngblood, Beth D / Yu, Violeta L / Zhang, Maosheng / Gavva, Narender R / Lehto, Sonya G / Geuns-Meyer, Stephanie

Journal of medicinal chemistry

2016 Volume 59, Issue 6, Page(s) 2794–2809

Abstract: There has been significant interest in developing a transient receptor potential A1 (TRPA1) antagonist for the treatment of pain due to a wealth of data implicating its role in pain pathways. Despite this, identification of a potent small molecule tool ... ...

Abstract	There has been significant interest in developing a transient receptor potential A1 (TRPA1) antagonist for the treatment of pain due to a wealth of data implicating its role in pain pathways. Despite this, identification of a potent small molecule tool possessing pharmacokinetic properties allowing for robust in vivo target coverage has been challenging. Here we describe the optimization of a potent, selective series of quinazolinone-based TRPA1 antagonists. High-throughput screening identified 4, which possessed promising potency and selectivity. A strategy focused on optimizing potency while increasing polarity in order to improve intrinsic clearance culminated with the discovery of purinone 27 (AM-0902), which is a potent, selective antagonist of TRPA1 with pharmacokinetic properties allowing for >30-fold coverage of the rat TRPA1 IC50 in vivo. Compound 27 demonstrated dose-dependent inhibition of AITC-induced flinching in rats, validating its utility as a tool for interrogating the role of TRPA1 in in vivo pain models.
MeSH term(s)	Animals ; Biological Transport, Active ; CHO Cells ; Calcium Channels ; Cricetulus ; Dogs ; Dose-Response Relationship, Drug ; Drug Discovery ; High-Throughput Screening Assays ; Humans ; In Vitro Techniques ; Madin Darby Canine Kidney Cells ; Microsomes, Liver/drug effects ; Microsomes, Liver/metabolism ; Models, Molecular ; Nerve Tissue Proteins/antagonists & inhibitors ; Oxadiazoles/chemical synthesis ; Oxadiazoles/pharmacology ; Pain Measurement/drug effects ; Purines/chemical synthesis ; Purines/pharmacology ; Quinazolines/chemical synthesis ; Quinazolines/pharmacology ; Rats ; Structure-Activity Relationship ; TRPA1 Cation Channel ; Transient Receptor Potential Channels/antagonists & inhibitors
Chemical Substances	AM-0902 ; Calcium Channels ; Nerve Tissue Proteins ; Oxadiazoles ; Purines ; Quinazolines ; TRPA1 Cation Channel ; TRPA1 protein, human ; Transient Receptor Potential Channels
Language	English
Publishing date	2016-03-24
Publishing country	United States
Document type	Journal Article
ZDB-ID	218133-2
ISSN	1520-4804 ; 0022-2623
ISSN (online)	1520-4804
ISSN	0022-2623
DOI	10.1021/acs.jmedchem.6b00039
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Zs.B 151: Show issues			Location: Je nach Verfügbarkeit (siehe Angabe bei Bestand) bis Jg. 2021: Bestellungen von Artikeln über das Online-Bestellformular ab Jg. 2022: Lesesaal (EG)
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