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  1. Article ; Online: Green, S., & Flemons, D. (2018). Quickies: The Handbook of Brief Sex Therapy (3rd ed.). New York, NY: W. W. Norton & Company.

    Meyer, Cynthia J

    Journal of marital and family therapy

    2019  Volume 45, Issue 4, Page(s) 733–734

    Language English
    Publishing date 2019-10-12
    Publishing country United States
    Document type Journal Article ; Review
    ZDB-ID 224679-x
    ISSN 1752-0606 ; 0194-472X
    ISSN (online) 1752-0606
    ISSN 0194-472X
    DOI 10.1111/jmft.12379
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  2. Article ; Online: Development of a Covalent Inhibitor of c-Jun N-Terminal Protein Kinase (JNK) 2/3 with Selectivity over JNK1.

    Lu, Wenchao / Liu, Yao / Gao, Yang / Geng, Qixiang / Gurbani, Deepak / Li, Lianbo / Ficarro, Scott B / Meyer, Cynthia J / Sinha, Dhiraj / You, Inchul / Tse, Jason / He, Zhixiang / Ji, Wenzhi / Che, Jianwei / Kim, Audrey Y / Yu, Tengteng / Wen, Kenneth / Anderson, Kenneth C / Marto, Jarrod A /
    Westover, Kenneth D / Zhang, Tinghu / Gray, Nathanael S

    Journal of medicinal chemistry

    2023  Volume 66, Issue 5, Page(s) 3356–3371

    Abstract: The c-Jun N-terminal kinases (JNKs) are members of the mitogen-activated protein kinase (MAPK) family, which includes JNK1-JNK3. Interestingly, JNK1 and JNK2 show opposing functions, with JNK2 activity favoring cell survival and JNK1 stimulating ... ...

    Abstract The c-Jun N-terminal kinases (JNKs) are members of the mitogen-activated protein kinase (MAPK) family, which includes JNK1-JNK3. Interestingly, JNK1 and JNK2 show opposing functions, with JNK2 activity favoring cell survival and JNK1 stimulating apoptosis. Isoform-selective small molecule inhibitors of JNK1 or JNK2 would be useful as pharmacological probes but have been difficult to develop due to the similarity of their ATP binding pockets. Here, we describe the discovery of a covalent inhibitor YL5084, the first such inhibitor that displays selectivity for JNK2 over JNK1. We demonstrated that YL5084 forms a covalent bond with Cys116 of JNK2, exhibits a 20-fold higher
    MeSH term(s) JNK Mitogen-Activated Protein Kinases ; Mitogen-Activated Protein Kinase 8/metabolism ; Mitogen-Activated Protein Kinase 9/metabolism ; Mitogen-Activated Protein Kinases/metabolism ; Phosphorylation
    Chemical Substances JNK Mitogen-Activated Protein Kinases (EC 2.7.11.24) ; Mitogen-Activated Protein Kinase 8 (EC 2.7.11.24) ; Mitogen-Activated Protein Kinase 9 (EC 2.7.1.24) ; Mitogen-Activated Protein Kinases (EC 2.7.11.24) ; YL5084
    Language English
    Publishing date 2023-02-24
    Publishing country United States
    Document type 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.
    ZDB-ID 218133-2
    ISSN 1520-4804 ; 0022-2623
    ISSN (online) 1520-4804
    ISSN 0022-2623
    DOI 10.1021/acs.jmedchem.2c01834
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  3. Article ; Online: The p-type ATPase superfamily.

    Chan, Henry / Babayan, Vartan / Blyumin, Elya / Gandhi, Charmy / Hak, Kunal / Harake, Danielle / Kumar, Kris / Lee, Perry / Li, Tze T / Liu, Hao Yi / Lo, Tony Chung Tung / Meyer, Cynthia J / Stanford, Steven / Zamora, Krista S / Saier, Milton H

    Journal of molecular microbiology and biotechnology

    2010  Volume 19, Issue 1-2, Page(s) 5–104

    Abstract: P-type ATPases function to provide homeostasis in higher eukaryotes, but they are essentially ubiquitous, being found in all domains of life. Thever and Saier [J Memb Biol 2009;229:115-130] recently reported analyses of eukaryotic P-type ATPases, ... ...

    Abstract P-type ATPases function to provide homeostasis in higher eukaryotes, but they are essentially ubiquitous, being found in all domains of life. Thever and Saier [J Memb Biol 2009;229:115-130] recently reported analyses of eukaryotic P-type ATPases, dividing them into nine functionally characterized and 13 functionally uncharacterized (FUPA) families. In this report, we analyze P-type ATPases in all major prokaryotic phyla for which complete genome sequence data are available, and we compare the results with those for eukaryotic P-type ATPases. Topological type I (heavy metal) P-type ATPases predominate in prokaryotes (approx. tenfold) while type II ATPases (specific for Na(+),K(+), H(+) Ca(2+), Mg(2+) and phospholipids) predominate in eukaryotes (approx. twofold). Many P-type ATPase families are found exclusively in prokaryotes (e.g. Kdp-type K(+) uptake ATPases (type III) and all ten prokaryotic FUPA familes), while others are restricted to eukaryotes (e.g. phospholipid flippases and all 13 eukaryotic FUPA families). Horizontal gene transfer has occurred frequently among bacteria and archaea, which have similar distributions of these enzymes, but rarely between most eukaryotic kingdoms, and even more rarely between eukaryotes and prokaryotes. In some bacterial phyla (e.g. Bacteroidetes, Flavobacteria and Fusobacteria), ATPase gene gain and loss as well as horizontal transfer occurred seldom in contrast to most other bacterial phyla. Some families (i.e. Kdp-type ATPases) underwent far less horizontal gene transfer than other prokaryotic families, possibly due to their multisubunit characteristics. Functional motifs are better conserved across family lines than across organismal lines, and these motifs can be family specific, facilitating functional predictions. In some cases, gene fusion events created P-type ATPases covalently linked to regulatory catalytic enzymes. In one family (FUPA Family 24), a type I ATPase gene (N-terminal) is fused to a type II ATPase gene (C-terminal) with retention of function only for the latter. Several pseudogene-encoded nonfunctional ATPases were identified. Genome minimalization led to preferential loss of P-type ATPase genes. We suggest that in prokaryotes and some unicellular eukaryotes, the primary function of P-type ATPases is protection from extreme environmental stress conditions. The classification of P-type ATPases of unknown function into phylogenetic families provides guides for future molecular biological studies.
    MeSH term(s) Adenosine Triphosphatases/classification ; Adenosine Triphosphatases/genetics ; Amino Acid Motifs ; Archaea/enzymology ; Archaea/genetics ; Bacteria/enzymology ; Bacteria/genetics ; Base Sequence ; Conserved Sequence ; Eukaryota/enzymology ; Eukaryota/genetics ; Gene Transfer, Horizontal ; Genome, Bacterial ; Ion Pumps/metabolism ; Ion Transport ; Molecular Sequence Data ; Phylogeny ; Pseudogenes
    Chemical Substances Ion Pumps ; Adenosine Triphosphatases (EC 3.6.1.-)
    Language English
    Publishing date 2010
    Publishing country Switzerland
    Document type Journal Article ; Review
    ZDB-ID 2006915-7
    ISSN 1660-2412 ; 1464-1801
    ISSN (online) 1660-2412
    ISSN 1464-1801
    DOI 10.1159/000319588
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  4. Article: The P-Type ATPase Superfamily

    Chan, Henry / Babayan, Vartan / Blyumin, Elya / Gandhi, Charmy / Hak, Kunal / Harake, Danielle / Kumar, Kris / Lee, Perry / Li, Tze T. / Liu, Hao Yi / Lo, Tony Chung Tung / Meyer, Cynthia J. / Stanford, Steven / Zamora, Krista S. / Saier Jr., Milton H.

    Journal of Molecular Microbiology and Biotechnology

    2010  Volume 19, Issue 1-2, Page(s) 5–104

    Abstract: P-type ATPases function to provide homeostasis in higher eukaryotes, but they are essentially ubiquitous, being found in all domains of life. Thever and Saier [J Memb Biol 2009;229:115–130] recently reported analyses of eukaryotic P-type ATPases, ... ...

    Institution Division of Biological Sciences, University of California at San Diego, La Jolla, Calif., USA
    Abstract P-type ATPases function to provide homeostasis in higher eukaryotes, but they are essentially ubiquitous, being found in all domains of life. Thever and Saier [J Memb Biol 2009;229:115–130] recently reported analyses of eukaryotic P-type ATPases, dividing them into nine functionally characterized and 13 functionally uncharacterized (FUPA) families. In this report, we analyze P-type ATPases in all major prokaryotic phyla for which complete genome sequence data are available, and we compare the results with those for eukaryotic P-type ATPases. Topological type I (heavy metal) P-type ATPases predominate in prokaryotes (approx. tenfold) while type II ATPases (specific for Na,K, H Ca2+, Mg2+ and phospholipids) predominate in eukaryotes (approx. twofold). Many P-type ATPase families are found exclusively in prokaryotes (e.g. Kdp-type K uptake ATPases (type III) and all ten prokaryotic FUPA familes), while others are restricted to eukaryotes (e.g. phospholipid flippases and all 13 eukaryotic FUPA families). Horizontal gene transfer has occurred frequently among bacteria and archaea, which have similar distributions of these enzymes, but rarely between most eukaryotic kingdoms, and even more rarely between eukaryotes and prokaryotes. In some bacterial phyla (e.g. Bacteroidetes, Flavobacteria and Fusobacteria), ATPase gene gain and loss as well as horizontal transfer occurred seldom in contrast to most other bacterial phyla. Some families (i.e. Kdp-type ATPases) underwent far less horizontal gene transfer than other prokaryotic families, possibly due to their multisubunit characteristics. Functional motifs are better conserved across family lines than across organismal lines, and these motifs can be family specific, facilitating functional predictions. In some cases, gene fusion events created P-type ATPases covalently linked to regulatory catalytic enzymes. In one family (FUPA Family 24), a type I ATPase gene (N-terminal) is fused to a type II ATPase gene (C-terminal) with retention of function only for the latter. Several pseudogene-encoded nonfunctional ATPases were identified. Genome minimalization led to preferential loss of P-type ATPase genes. We suggest that in prokaryotes and some unicellular eukaryotes, the primary function of P-type ATPases is protection from extreme environmental stress conditions. The classification of P-type ATPases of unknown function into phylogenetic families provides guides for future molecular biological studies.
    Keywords Conserved motifs ; Ion pumps ; Ion transport ; Prokaryotes ; Phylogeny ; P-type ATPase ; Superfamily ; Topology
    Language English
    Publishing date 2010-10-20
    Publisher S. Karger AG
    Publishing place Basel, Switzerland
    Document type Article
    Note Paper
    ZDB-ID 2006915-7
    ISBN 978-3-8055-9597-1 ; 978-3-8055-9598-8 ; 3-8055-9597-2 ; 3-8055-9598-0
    ISSN 1660-2412 ; 1464-1801
    ISSN (online) 1660-2412
    ISSN 1464-1801
    DOI 10.1159/000319588
    Database Karger publisher's database

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    In stock of ZB MED Cologne/Königswinter

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    Jg. 1995 - 2021: Lesesall (2.OG)
    ab Jg. 2022: Lesesaal (EG)

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  5. Article ; Online: The P-Type ATPase Superfamily

    Chan, Henry / Babayan, Vartan / Blyumin, Elya / Gandhi, Charmy / Hak, Kunal / Harake, Danielle / Kumar, Kris / Lee, Perry / Li, Tze T. / Liu, Hao Yi / Lo, Tony Chung Tung / Meyer, Cynthia J. / Stanford, Steven / Zamora, Krista S. / Saier, Jr., Milton H.

    Journal of Molecular Microbiology and Biotechnology

    2010  Volume 19, Issue 1-2, Page(s) 104–105

    Abstract: P-type ATPases function to provide homeostasis in higher eukaryotes, but they are essentially ubiquitous, being found in all domains of life. Thever and Saier [J Memb Biol 2009;229:115-130] recently reported analyses of eukaryotic P-type ATPases, ... ...

    Abstract P-type ATPases function to provide homeostasis in higher eukaryotes, but they are essentially ubiquitous, being found in all domains of life. Thever and Saier [J Memb Biol 2009;229:115-130] recently reported analyses of eukaryotic P-type ATPases, dividing them into nine functionally characterized and 13 functionally uncharacterized (FUPA) families. In this report, we analyze P-type ATPases in all major prokaryotic phyla for which complete genome sequence data are available, and we compare the results with those for eukaryotic P-type ATPases. Topological type I (heavy metal) P-type ATPases predominate in prokaryotes (approx. tenfold) while type II ATPases (specific for Na+,K+, H+ Ca2+, Mg2+ and phospholipids) predominate in eukaryotes (approx. twofold). Many P-type ATPase families are found exclusively in prokaryotes (e.g. Kdp-type K+ uptake ATPases (type III) and all ten prokaryotic FUPA familes), while others are restricted to eukaryotes (e.g. phospholipid flippases and all 13 eukaryotic FUPA families). Horizontal gene transfer has occurred frequently among bacteria and archaea, which have similar distributions of these enzymes, but rarely between most eukaryotic kingdoms, and even more rarely between eukaryotes and prokaryotes. In some bacterial phyla (e.g. Bacteroidetes, Flavobacteria and Fusobacteria), ATPase gene gain and loss as well as horizontal transfer occurred seldom in contrast to most other bacterial phyla. Some families (i.e. Kdp-type ATPases) underwent far less horizontal gene transfer than other prokaryotic families, possibly due to their multisubunit characteristics. Functional motifs are better conserved across family lines than across organismal lines, and these motifs can be family specific, facilitating functional predictions. In some cases, gene fusion events created P-type ATPases covalently linked to regulatory catalytic enzymes. In one family (FUPA Family 24), a type I ATPase gene (N-terminal) is fused to a type II ATPase gene (C-terminal) with retention of function only for the latter. Several pseudogene-encoded nonfunctional ATPases were identified. Genome minimalization led to preferential loss of P-type ATPase genes. We suggest that in prokaryotes and some unicellular eukaryotes, the primary function of P-type ATPases is protection from extreme environmental stress conditions. The classification of P-type ATPases of unknown function into phylogenetic families provides guides for future molecular biological studies.
    Keywords Conserved motifs ; Ion pumps ; Ion transport ; Prokaryotes ; Phylogeny ; P-type ATPase ; Superfamily ; Topology
    Language English
    Publisher S. Karger AG
    Publishing place Basel
    Publishing country Switzerland
    Document type Article ; Online
    ZDB-ID 2006915-7
    ISSN 1660-2412 ; 1464-1801 ; 1464-1801
    ISSN (online) 1660-2412
    ISSN 1464-1801
    DOI 10.1159/000319588
    Database Karger publisher's database

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    In stock of ZB MED Cologne/Königswinter

    Zs.A 5804: Show issues Location:
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    Jg. 1995 - 2021: Lesesall (2.OG)
    ab Jg. 2022: Lesesaal (EG)

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