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  1. AU="Chou, Chau-Wen"
  2. AU=Kaur Supreet
  3. AU="Yun, Joho"
  4. AU="Tran, Bao G"
  5. AU="Ou Li"
  6. AU="Ting Chen" AU="Ting Chen"
  7. AU="Wilson, Jaymi"
  8. AU="Vane, Christopher H"
  9. AU="Mabbott, Donald"
  10. AU="Martín-Trejo, Jorge Alfonso"
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  1. Artikel: Dissolved organic phosphorus utilization by the marine bacterium Ruegeria pomeroyi DSS‐3 reveals chain length‐dependent polyphosphate degradation

    Adams, Jamee C. / Steffen, Rachel / Chou, Chau‐Wen / Duhamel, Solange / Diaz, Julia M.

    Environmental microbiology. 2022 May, v. 24, no. 5

    2022  

    Abstract: Dissolved organic phosphorus (DOP) is a critical nutritional resource for marine microbial communities. However, the relative bioavailability of different types of DOP, such as phosphomonoesters (P‐O‐C) and phosphoanhydrides (P‐O‐P), is poorly understood. ...

    Abstract Dissolved organic phosphorus (DOP) is a critical nutritional resource for marine microbial communities. However, the relative bioavailability of different types of DOP, such as phosphomonoesters (P‐O‐C) and phosphoanhydrides (P‐O‐P), is poorly understood. Here we assess the utilization of these P sources by a representative bacterial copiotroph, Ruegeria pomeroyi DSS‐3. All DOP sources supported equivalent growth by R. pomeroyi, and all DOP hydrolysis rates were upregulated under phosphorus depletion (−P). A long‐chain polyphosphate (45polyP) showed the lowest hydrolysis rate of all DOP substrates tested, including tripolyphosphate (3polyP). Yet the upregulation of 45polyP hydrolysis under −P was greater than any other substrate analyzed. Proteomics revealed three common P acquisition enzymes potentially involved in polyphosphate utilization, including two alkaline phosphatases, PhoD and PhoX, and one 5′‐nucleotidase (5′‐NT). Results from DOP substrate competition experiments show that these enzymes likely have broad substrate specificities, including chain length‐dependent reactivity toward polyphosphate. These results confirm that DOP, including polyP, are bioavailable nutritional P sources for R. pomeroyi, and possibly other marine heterotrophic bacteria. Furthermore, the chain‐length dependent mechanisms, rates and regulation of polyP hydrolysis suggest that these processes may influence the composition of DOP and the overall recycling of nutrients within marine dissolved organic matter.
    Schlagwörter Ruegeria ; aquatic bacteria ; bioavailability ; dissolved organic matter ; hydrolysis ; organic phosphorus ; proteomics ; tripolyphosphates
    Sprache Englisch
    Erscheinungsverlauf 2022-05
    Umfang p. 2259-2269.
    Erscheinungsort John Wiley & Sons, Inc.
    Dokumenttyp Artikel
    Anmerkung JOURNAL ARTICLE
    ZDB-ID 2020213-1
    ISSN 1462-2920 ; 1462-2912
    ISSN (online) 1462-2920
    ISSN 1462-2912
    DOI 10.1111/1462-2920.15877
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  2. Artikel ; Online: Dissolved organic phosphorus utilization by the marine bacterium Ruegeria pomeroyi DSS-3 reveals chain length-dependent polyphosphate degradation.

    Adams, Jamee C / Steffen, Rachel / Chou, Chau-Wen / Duhamel, Solange / Diaz, Julia M

    Environmental microbiology

    2022  Band 24, Heft 5, Seite(n) 2259–2269

    Abstract: Dissolved organic phosphorus (DOP) is a critical nutritional resource for marine microbial communities. However, the relative bioavailability of different types of DOP, such as phosphomonoesters (P-O-C) and phosphoanhydrides (P-O-P), is poorly understood. ...

    Abstract Dissolved organic phosphorus (DOP) is a critical nutritional resource for marine microbial communities. However, the relative bioavailability of different types of DOP, such as phosphomonoesters (P-O-C) and phosphoanhydrides (P-O-P), is poorly understood. Here we assess the utilization of these P sources by a representative bacterial copiotroph, Ruegeria pomeroyi DSS-3. All DOP sources supported equivalent growth by R. pomeroyi, and all DOP hydrolysis rates were upregulated under phosphorus depletion (-P). A long-chain polyphosphate (45polyP) showed the lowest hydrolysis rate of all DOP substrates tested, including tripolyphosphate (3polyP). Yet the upregulation of 45polyP hydrolysis under -P was greater than any other substrate analyzed. Proteomics revealed three common P acquisition enzymes potentially involved in polyphosphate utilization, including two alkaline phosphatases, PhoD and PhoX, and one 5'-nucleotidase (5'-NT). Results from DOP substrate competition experiments show that these enzymes likely have broad substrate specificities, including chain length-dependent reactivity toward polyphosphate. These results confirm that DOP, including polyP, are bioavailable nutritional P sources for R. pomeroyi, and possibly other marine heterotrophic bacteria. Furthermore, the chain-length dependent mechanisms, rates and regulation of polyP hydrolysis suggest that these processes may influence the composition of DOP and the overall recycling of nutrients within marine dissolved organic matter.
    Mesh-Begriff(e) Dissolved Organic Matter ; Phosphorus/metabolism ; Polyphosphates/metabolism ; Rhodobacteraceae/metabolism
    Chemische Substanzen Dissolved Organic Matter ; Polyphosphates ; Phosphorus (27YLU75U4W)
    Sprache Englisch
    Erscheinungsdatum 2022-02-01
    Erscheinungsland England
    Dokumenttyp Journal Article ; Research Support, Non-U.S. Gov't ; Research Support, U.S. Gov't, Non-P.H.S.
    ZDB-ID 2020213-1
    ISSN 1462-2920 ; 1462-2912
    ISSN (online) 1462-2920
    ISSN 1462-2912
    DOI 10.1111/1462-2920.15877
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  3. Artikel ; Online: Identification of lipidomic profiles associated with drug-resistant prostate cancer cells.

    Ingram, Lishann M / Finnerty, Morgan C / Mansoura, Maryam / Chou, Chau-Wen / Cummings, Brian S

    Lipids in health and disease

    2021  Band 20, Heft 1, Seite(n) 15

    Abstract: Background: The association of circulating lipids with clinical outcomes of drug-resistant castration-resistant prostate cancer (DR-CRPC) is not fully understood. While it is known that increases in select lipids correlate to decreased survival, neither ...

    Abstract Background: The association of circulating lipids with clinical outcomes of drug-resistant castration-resistant prostate cancer (DR-CRPC) is not fully understood. While it is known that increases in select lipids correlate to decreased survival, neither the mechanisms mediating these alterations nor the correlation of resistance to drug treatments is well characterized.
    Methods: This gap-in-knowledge was addressed using in vitro models of non-cancerous, hormone-sensitive, CRPC and drug-resistant cell lines combined with quantitative LC-ESI-Orbitrap-MS (LC-ESI-MS/MS) lipidomic analysis and subsequent analysis such as Metaboanalyst and Lipid Pathway Enrichment Analysis (LIPEA).
    Results: Several lipid regulatory pathways were identified that are associated with Docetaxel resistance in prostate cancer (PCa). These included those controlling glycerophospholipid metabolism, sphingolipid signaling and ferroptosis. In total, 7460 features were identified as being dysregulated between the cell lines studied, and 21 lipid species were significantly altered in drug-resistant cell lines as compared to nonresistant cell lines. Docetaxel resistance cells (PC3-Rx and DU145-DR) had higher levels of phosphatidylcholine (PC), oxidized lipid species, phosphatidylethanolamine (PE), and sphingomyelin (SM) as compared to parent control cells (PC-3 and DU-145). Alterations were also identified in the levels of phosphatidic acid (PA) and diacylglyceride (DAG), whose levels are regulated by Lipin (LPIN), a phosphatidic acid phosphatase that converts PA to DAG. Data derived from cBioPortal demonstrated a population of PCa patients expressing mutations aligning with amplification of LPIN1, LPIN2 and LPIN3 genes. Lipin amplification in these genes correlated to decreased survival in these patients. Lipin-1 mRNA expression also showed a similar trend in PCa patient data. Lipin-1, but not Lipin-2 or - 3, was detected in several prostate cancer cells, and was increased in 22RV1 and PC-3 cell lines. The increased expression of Lipin-1 in these cells correlated with the level of PA.
    Conclusion: These data identify lipids whose levels may correlate to Docetaxel sensitivity and progression of PCa. The data also suggest a correlation between the expression of Lipin-1 in cells and patients with regards to prostate cancer cell aggressiveness and patient survivability. Ultimately, these data may be useful for identifying markers of lethal and/or metastatic prostate cancer.
    Mesh-Begriff(e) Adult ; Aged ; Antineoplastic Agents/administration & dosage ; Antineoplastic Agents/adverse effects ; Cell Line, Tumor ; Docetaxel/administration & dosage ; Docetaxel/adverse effects ; Drug Resistance, Neoplasm/genetics ; Ferroptosis/drug effects ; Gene Expression Regulation, Neoplastic/genetics ; Humans ; Lipid Metabolism/drug effects ; Lipidomics/methods ; Lipids/genetics ; Male ; Middle Aged ; Neoplasm Metastasis ; Nuclear Proteins/genetics ; Phosphatidate Phosphatase/genetics ; Prostatic Neoplasms/drug therapy ; Prostatic Neoplasms/genetics ; Prostatic Neoplasms/pathology ; Signal Transduction/drug effects
    Chemische Substanzen Antineoplastic Agents ; LPIN2 protein, human ; Lipids ; Nuclear Proteins ; Docetaxel (15H5577CQD) ; LPIN1 protein, human (EC 3.1.3.4) ; LPIN3 protein, human (EC 3.1.3.4) ; Phosphatidate Phosphatase (EC 3.1.3.4)
    Sprache Englisch
    Erscheinungsdatum 2021-02-17
    Erscheinungsland England
    Dokumenttyp Journal Article
    ISSN 1476-511X
    ISSN (online) 1476-511X
    DOI 10.1186/s12944-021-01437-5
    Datenquelle MEDical Literature Analysis and Retrieval System OnLINE

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  4. Artikel ; Online: Expression of divergent methyl/alkyl coenzyme M reductases from uncultured archaea.

    Shao, Nana / Fan, Yu / Chou, Chau-Wen / Yavari, Shadi / Williams, Robert V / Amster, I Jonathan / Brown, Stuart M / Drake, Ian J / Duin, Evert C / Whitman, William B / Liu, Yuchen

    Communications biology

    2022  Band 5, Heft 1, Seite(n) 1113

    Abstract: Methanogens and anaerobic methane-oxidizing archaea (ANME) are important players in the global carbon cycle. Methyl-coenzyme M reductase (MCR) is a key enzyme in methane metabolism, catalyzing the last step in methanogenesis and the first step in ... ...

    Abstract Methanogens and anaerobic methane-oxidizing archaea (ANME) are important players in the global carbon cycle. Methyl-coenzyme M reductase (MCR) is a key enzyme in methane metabolism, catalyzing the last step in methanogenesis and the first step in anaerobic methane oxidation. Divergent mcr and mcr-like genes have recently been identified in uncultured archaeal lineages. However, the assembly and biochemistry of MCRs from uncultured archaea remain largely unknown. Here we present an approach to study MCRs from uncultured archaea by heterologous expression in a methanogen, Methanococcus maripaludis. Promoter, operon structure, and temperature were important determinants for MCR production. Both recombinant methanococcal and ANME-2 MCR assembled with the host MCR forming hybrid complexes, whereas tested ANME-1 MCR and ethyl-coenzyme M reductase only formed homogenous complexes. Together with structural modeling, this suggests that ANME-2 and methanogen MCRs are structurally similar and their reaction directions are likely regulated by thermodynamics rather than intrinsic structural differences.
    Mesh-Begriff(e) Archaea/genetics ; Archaea/metabolism ; Mesna/metabolism ; Oxidoreductases/metabolism ; Methane/metabolism
    Chemische Substanzen methyl coenzyme M reductase (EC 2.8.4.1) ; Mesna (NR7O1405Q9) ; Oxidoreductases (EC 1.-) ; Methane (OP0UW79H66)
    Sprache Englisch
    Erscheinungsdatum 2022-10-20
    Erscheinungsland England
    Dokumenttyp Journal Article ; Research Support, U.S. Gov't, Non-P.H.S. ; Research Support, N.I.H., Extramural
    ISSN 2399-3642
    ISSN (online) 2399-3642
    DOI 10.1038/s42003-022-04057-6
    Datenquelle MEDical Literature Analysis and Retrieval System OnLINE

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  5. Artikel ; Online: Posttranslational Methylation of Arginine in Methyl Coenzyme M Reductase Has a Profound Impact on both Methanogenesis and Growth of Methanococcus maripaludis.

    Lyu, Zhe / Shao, Nana / Chou, Chau-Wen / Shi, Hao / Patel, Ricky / Duin, Evert C / Whitman, William B

    Journal of bacteriology

    2020  Band 202, Heft 3

    Abstract: Catalyzing the key step for anaerobic production and/or oxidation of methane and likely other short-chain alkanes, methyl coenzyme M reductase (Mcr) and its homologs play a key role in the global carbon cycle. The McrA subunit possesses up to five ... ...

    Abstract Catalyzing the key step for anaerobic production and/or oxidation of methane and likely other short-chain alkanes, methyl coenzyme M reductase (Mcr) and its homologs play a key role in the global carbon cycle. The McrA subunit possesses up to five conserved posttranslational modifications (PTMs) at its active site. It was previously suggested that methanogenesis marker protein 10 (Mmp10) could play an important role in methanogenesis. To systematically examine its physiological role,
    Mesh-Begriff(e) Arginine/metabolism ; Binding Sites ; Blotting, Western ; Catalytic Domain ; Computational Biology ; Mass Spectrometry ; Methanococcus/pathogenicity ; Methylation ; Oxidoreductases/chemistry ; Oxidoreductases/genetics ; Oxidoreductases/metabolism ; Protein Processing, Post-Translational ; Substrate Specificity
    Chemische Substanzen Arginine (94ZLA3W45F) ; Oxidoreductases (EC 1.-) ; methyl coenzyme M reductase (EC 2.8.4.1)
    Sprache Englisch
    Erscheinungsdatum 2020-01-15
    Erscheinungsland United States
    Dokumenttyp Journal Article ; Research Support, U.S. Gov't, Non-P.H.S.
    ZDB-ID 2968-3
    ISSN 1098-5530 ; 0021-9193
    ISSN (online) 1098-5530
    ISSN 0021-9193
    DOI 10.1128/JB.00654-19
    Datenquelle MEDical Literature Analysis and Retrieval System OnLINE

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  6. Artikel: Burkholderia thailandensis outer membrane vesicles exert antimicrobial activity against drug-resistant and competitor microbial species

    Wang, Yihui / Hoffmann, Joseph P / Chou, Chau-Wen / Höner zu Bentrup, Kerstin / Fuselier, Joseph A / Bitoun, Jacob P / Wimley, William C / Morici, Lisa A

    journal of microbiology. 2020 July, v. 58, no. 7

    2020  

    Abstract: Gram-negative bacteria secrete outer membrane vesicles (OMVs) that play critical roles in intraspecies, interspecies, and bacteria-environment interactions. Some OMVs, such as those produced by Pseudomonas aeruginosa, have previously been shown to ... ...

    Abstract Gram-negative bacteria secrete outer membrane vesicles (OMVs) that play critical roles in intraspecies, interspecies, and bacteria-environment interactions. Some OMVs, such as those produced by Pseudomonas aeruginosa, have previously been shown to possess antimicrobial activity against competitor species. In the current study, we demonstrate that OMVs from Burkholderia thailandensis inhibit the growth of drug-sensitive and drug-resistant bacteria and fungi. We show that a number of antimicrobial compounds, including peptidoglycan hydrolases, 4-hydroxy-3-methyl-2-(2-non-enyl)-quinoline (HMNQ) and long-chain rhamnolipid are present in or tightly associate with B. thailandensis OMVs. Furthermore, we demonstrate that HMNQ and rhamnolipid possess antimicrobial and antibiofilm properties against methicillin-resistant Staphylococcus aureus (MRSA). These findings indicate that B. thailandensis secretes antimicrobial OMVs that may impart a survival advantage by eliminating competition. In addition, bacterial OMVs may represent an untapped resource of novel therapeutics effective against bio-film-forming and multidrug-resistant organisms.
    Schlagwörter Burkholderia thailandensis ; Pseudomonas aeruginosa ; antimicrobial properties ; hydrolases ; methicillin-resistant Staphylococcus aureus ; multiple drug resistance ; peptidoglycans ; rhamnolipids ; therapeutics
    Sprache Englisch
    Erscheinungsverlauf 2020-07
    Umfang p. 550-562.
    Erscheinungsort The Microbiological Society of Korea
    Dokumenttyp Artikel
    Anmerkung NAL-AP-2-clean
    ZDB-ID 2012399-1
    ISSN 1225-8873
    ISSN 1225-8873
    DOI 10.1007/s12275-020-0028-1
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  7. Artikel ; Online: Profiling Cellular Substrates of Lysine Acetyltransferases GCN5 and p300 with Orthogonal Labeling and Click Chemistry.

    Han, Zhen / Chou, Chau-Wen / Yang, Xiangkun / Bartlett, Michael G / Zheng, Y George

    ACS chemical biology

    2017  Band 12, Heft 6, Seite(n) 1547–1555

    Abstract: p300 and GCN5 are two representative lysine acetyltransferases (KATs) in mammalian cells. It was recently reported that they possess multiple acyltransferase activities including acetylation, propionylation, and butyrylation of the ε-amino group of ... ...

    Abstract p300 and GCN5 are two representative lysine acetyltransferases (KATs) in mammalian cells. It was recently reported that they possess multiple acyltransferase activities including acetylation, propionylation, and butyrylation of the ε-amino group of lysine residues of histones and non-histone protein substrates. Although thousands of acetylated substrates and acetylation sites have been identified by mass spectrometry-based proteomic screening, our knowledge about the causative connections between individual KAT members and their corresponding sub-acylomes remain very limited. Herein, we applied 3-azidopropionyl CoA (3AZ-CoA) as a bioorthogonal surrogate of acetyl-, propionyl- and butyryl-CoA for KAT substrate identification. We successfully attached the azide as a chemical warhead to cellular substrates of wild-type p300 and engineered GCN5. The substrates were subsequently labeled with biotin tag through the copper-catalyzed azide-alkyne cycloaddition (CuAAC). Following protein enrichment on streptavidin-coated resin, we conducted LC-MS/MS studies from which more than four hundred proteins were identified as GCN5 or p300 substrate candidates. These proteins are either p300- or GCN5-unique or shared by the two KATs and are extensively involved in various biological events including gene expression, cell cycle, and cellular metabolism. We also experimentally validated two novel substrates of GCN5, that is, IQGAP1 and SMC1. These results demonstrate extensive engagement of GCN5 and p300 in cellular pathways and provide new insights into understanding their functions in specific biological processes.
    Mesh-Begriff(e) Animals ; Bacterial Proteins ; Biotin/analogs & derivatives ; Chromatography, Liquid ; Click Chemistry ; E1A-Associated p300 Protein/metabolism ; Humans ; Ligands ; Lysine Acetyltransferases/metabolism ; Tandem Mass Spectrometry ; p300-CBP Transcription Factors/metabolism
    Chemische Substanzen Bacterial Proteins ; Ligands ; biotin-streptavidin complex ; Biotin (6SO6U10H04) ; Lysine Acetyltransferases (EC 2.3.1.32) ; E1A-Associated p300 Protein (EC 2.3.1.48) ; EP300 protein, human (EC 2.3.1.48) ; p300-CBP Transcription Factors (EC 2.3.1.48) ; p300-CBP-associated factor (EC 2.3.1.48)
    Sprache Englisch
    Erscheinungsdatum 2017-06-16
    Erscheinungsland United States
    Dokumenttyp Journal Article
    ISSN 1554-8937
    ISSN (online) 1554-8937
    DOI 10.1021/acschembio.7b00114
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  8. Artikel ; Online: Assembly of Methyl Coenzyme M Reductase in the Methanogenic Archaeon Methanococcus maripaludis.

    Lyu, Zhe / Chou, Chau-Wen / Shi, Hao / Wang, Liangliang / Ghebreab, Robel / Phillips, Dennis / Yan, Yajun / Duin, Evert C / Whitman, William B

    Journal of bacteriology

    2018  Band 200, Heft 7

    Abstract: Methyl coenzyme M reductase (MCR) is a complex enzyme that catalyzes the final step in biological methanogenesis. To better understand its assembly, the recombinant MCR from the ... ...

    Abstract Methyl coenzyme M reductase (MCR) is a complex enzyme that catalyzes the final step in biological methanogenesis. To better understand its assembly, the recombinant MCR from the thermophile
    Mesh-Begriff(e) Binding Sites ; Catalysis ; Metalloporphyrins/chemistry ; Methane/metabolism ; Methanococcus/enzymology ; Methanococcus/metabolism ; Oxidation-Reduction ; Oxidoreductases/chemistry ; Oxidoreductases/genetics ; Oxidoreductases/metabolism ; Protein Processing, Post-Translational/genetics
    Chemische Substanzen Metalloporphyrins ; factor F430 (73145-13-8) ; Oxidoreductases (EC 1.-) ; methyl coenzyme M reductase (EC 2.8.4.1) ; Methane (OP0UW79H66)
    Sprache Englisch
    Erscheinungsdatum 2018-03-12
    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.
    ZDB-ID 2968-3
    ISSN 1098-5530 ; 0021-9193
    ISSN (online) 1098-5530
    ISSN 0021-9193
    DOI 10.1128/JB.00746-17
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  9. Artikel ; Online: Burkholderia thailandensis outer membrane vesicles exert antimicrobial activity against drug-resistant and competitor microbial species.

    Wang, Yihui / Hoffmann, Joseph P / Chou, Chau-Wen / Höner Zu Bentrup, Kerstin / Fuselier, Joseph A / Bitoun, Jacob P / Wimley, William C / Morici, Lisa A

    Journal of microbiology (Seoul, Korea)

    2020  Band 58, Heft 7, Seite(n) 550–562

    Abstract: Gram-negative bacteria secrete outer membrane vesicles (OMVs) that play critical roles in intraspecies, interspecies, and bacteria-environment interactions. Some OMVs, such as those produced by Pseudomonas aeruginosa, have previously been shown to ... ...

    Abstract Gram-negative bacteria secrete outer membrane vesicles (OMVs) that play critical roles in intraspecies, interspecies, and bacteria-environment interactions. Some OMVs, such as those produced by Pseudomonas aeruginosa, have previously been shown to possess antimicrobial activity against competitor species. In the current study, we demonstrate that OMVs from Burkholderia thailandensis inhibit the growth of drug-sensitive and drug-resistant bacteria and fungi. We show that a number of antimicrobial compounds, including peptidoglycan hydrolases, 4-hydroxy-3-methyl-2-(2-non-enyl)-quinoline (HMNQ) and long-chain rhamnolipid are present in or tightly associate with B. thailandensis OMVs. Furthermore, we demonstrate that HMNQ and rhamnolipid possess antimicrobial and antibiofilm properties against methicillin-resistant Staphylococcus aureus (MRSA). These findings indicate that B. thailandensis secretes antimicrobial OMVs that may impart a survival advantage by eliminating competition. In addition, bacterial OMVs may represent an untapped resource of novel therapeutics effective against bio-film-forming and multidrug-resistant organisms.
    Mesh-Begriff(e) Anti-Bacterial Agents/metabolism ; Anti-Bacterial Agents/pharmacology ; Antibiosis/physiology ; Bacterial Outer Membrane/metabolism ; Biofilms/growth & development ; Burkholderia/metabolism ; Extracellular Vesicles/metabolism ; Glycolipids/metabolism ; Methicillin-Resistant Staphylococcus aureus/drug effects ; Methicillin-Resistant Staphylococcus aureus/growth & development ; Microbial Sensitivity Tests ; N-Acetylmuramoyl-L-alanine Amidase/metabolism ; Quinolines/metabolism
    Chemische Substanzen Anti-Bacterial Agents ; Glycolipids ; Quinolines ; rhamnolipid ; N-Acetylmuramoyl-L-alanine Amidase (EC 3.5.1.28)
    Sprache Englisch
    Erscheinungsdatum 2020-04-11
    Erscheinungsland Korea (South)
    Dokumenttyp Journal Article
    ZDB-ID 2012399-1
    ISSN 1976-3794 ; 1225-8873
    ISSN (online) 1976-3794
    ISSN 1225-8873
    DOI 10.1007/s12275-020-0028-1
    Datenquelle MEDical Literature Analysis and Retrieval System OnLINE

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  10. Artikel ; Online: The roles of phosphorylation and SHAGGY-like protein kinases in geminivirus C4 protein induced hyperplasia.

    Mills-Lujan, Katherine / Andrews, David L / Chou, Chau-Wen / Deom, C Michael

    PloS one

    2015  Band 10, Heft 3, Seite(n) e0122356

    Abstract: Even though plant cells are highly plastic, plants only develop hyperplasia under very specific abiotic and biotic stresses, such as when exposed to pathogens like Beet curly top virus (BCTV). The C4 protein of BCTV is sufficient to induce hyperplasia ... ...

    Abstract Even though plant cells are highly plastic, plants only develop hyperplasia under very specific abiotic and biotic stresses, such as when exposed to pathogens like Beet curly top virus (BCTV). The C4 protein of BCTV is sufficient to induce hyperplasia and alter Arabidopsis development. It was previously shown that C4 interacts with two Arabidopsis Shaggy-like protein kinases, AtSK21 and 23, which are negative regulators of brassinosteroid (BR) hormone signaling. Here we show that the C4 protein interacts with five additional AtSK family members. Bikinin, a competitive inhibitor of the seven AtSK family members that interact with C4, induced hyperplasia similar to that induced by the C4 protein. The Ser49 residue of C4 was found to be critical for C4 function, since: 1) mutagenesis of Ser49 to Ala abolished the C4-induced phenotype, abolished C4/AtSK interactions, and resulted in a mutant protein that failed to induce changes in the BR signaling pathway; 2) Ser49 is phosphorylated in planta; and 3) plant-encoded AtSKs must be catalytically active to interact with C4. A C4 N-myristoylation site mutant that does not localize to the plasma membrane and does not induce a phenotype, retained the ability to bind AtSKs. Taken together, these results suggest that plasma membrane associated C4 interacts with and co-opts multiple AtSKs to promote its own phosphorylation and activation to subsequently compromise cell cycle control.
    Mesh-Begriff(e) Aminopyridines/metabolism ; Arabidopsis/genetics ; Arabidopsis/growth & development ; Arabidopsis/virology ; Geminiviridae/metabolism ; Geminiviridae/pathogenicity ; Gene Expression Regulation, Plant ; Hyperplasia/genetics ; Hyperplasia/virology ; Mutagenesis ; Phosphorylation ; Plants, Genetically Modified ; Protein Interaction Mapping ; Protein Kinases/metabolism ; Seedlings/genetics ; Seedlings/metabolism ; Seedlings/virology ; Signal Transduction/genetics ; Succinates/metabolism ; Viral Proteins/genetics ; Viral Proteins/metabolism
    Chemische Substanzen Aminopyridines ; Succinates ; Viral Proteins ; bikinin ; Protein Kinases (EC 2.7.-)
    Sprache Englisch
    Erscheinungsdatum 2015
    Erscheinungsland United States
    Dokumenttyp Journal Article ; Research Support, Non-U.S. Gov't
    ISSN 1932-6203
    ISSN (online) 1932-6203
    DOI 10.1371/journal.pone.0122356
    Datenquelle MEDical Literature Analysis and Retrieval System OnLINE

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