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  1. Article ; Online: The draft genome of the C

    Studer, Anthony J / Schnable, James C / Weissmann, Sarit / Kolbe, Allison R / McKain, Michael R / Shao, Ying / Cousins, Asaph B / Kellogg, Elizabeth A / Brutnell, Thomas P

    Genome biology

    2016  Volume 17, Issue 1, Page(s) 223

    Abstract: Background: Comparisons between C: Results: We report the assembly of the nuclear and ... anatomical characterizations verified that D. oligosanthes utilizes the C: Conclusions: The phylogenetic ... location of D. oligosanthes makes it an ideal C ...

    Abstract Background: Comparisons between C
    Results: We report the assembly of the nuclear and chloroplast genomes of D. oligosanthes, from high-throughput short read sequencing data and a comparative transcriptomics analysis of the developing leaf of D. oligosanthes, S. viridis, and S. bicolor. Physiological and anatomical characterizations verified that D. oligosanthes utilizes the C
    Conclusions: The phylogenetic location of D. oligosanthes makes it an ideal C
    MeSH term(s) Evolution, Molecular ; Genome, Plant/genetics ; High-Throughput Nucleotide Sequencing ; Molecular Sequence Annotation ; Oryza ; Photosynthesis/genetics ; Phylogeny ; Poaceae/genetics ; Sorghum/genetics ; Zea mays/genetics
    Language English
    Publishing date 2016-10-28
    Publishing country England
    Document type Journal Article ; Research Support, U.S. Gov't, Non-P.H.S. ; Research Support, Non-U.S. Gov't
    ZDB-ID 2040529-7
    ISSN 1474-760X ; 1474-760X
    ISSN (online) 1474-760X
    ISSN 1474-760X
    DOI 10.1186/s13059-016-1080-3
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  2. Article ; Online: Ubiquitin chain-elongating enzyme UBE2S activates the RING E3 ligase APC/C for substrate priming.

    Martinez-Chacin, Raquel C / Bodrug, Tatyana / Bolhuis, Derek L / Kedziora, Katarzyna M / Bonacci, Thomas / Ordureau, Alban / Gibbs, Morgan E / Weissmann, Florian / Qiao, Renping / Grant, Gavin D / Cook, Jeanette G / Peters, Jan-Michael / Wade Harper, J / Emanuele, Michael J / Brown, Nicholas G

    Nature structural & molecular biology

    2020  Volume 27, Issue 6, Page(s) 550–560

    Abstract: ... for polyubiquitination. For example, the cell cycle regulatory E3, human anaphase-promoting complex/cyclosome (APC/C ... to describe a case where the chain-elongating E2 UBE2S feeds back and directly stimulates the E3 APC/C ...

    Abstract The interplay between E2 and E3 enzymes regulates the polyubiquitination of substrates in eukaryotes. Among the several RING-domain E3 ligases in humans, many utilize two distinct E2s for polyubiquitination. For example, the cell cycle regulatory E3, human anaphase-promoting complex/cyclosome (APC/C), relies on UBE2C to prime substrates with ubiquitin (Ub) and on UBE2S to extend polyubiquitin chains. However, the potential coordination between these steps in ubiquitin chain formation remains undefined. While numerous studies have unveiled how RING E3s stimulate individual E2s for Ub transfer, here we change perspective to describe a case where the chain-elongating E2 UBE2S feeds back and directly stimulates the E3 APC/C to promote substrate priming and subsequent multiubiquitination by UBE2C. Our work reveals an unexpected model for the mechanisms of RING E3-dependent ubiquitination and for the diverse and complex interrelationship between components of the ubiquitination cascade.
    MeSH term(s) Anaphase-Promoting Complex-Cyclosome/chemistry ; Anaphase-Promoting Complex-Cyclosome/genetics ; Anaphase-Promoting Complex-Cyclosome/metabolism ; Apc4 Subunit, Anaphase-Promoting Complex-Cyclosome/chemistry ; Apc4 Subunit, Anaphase-Promoting Complex-Cyclosome/genetics ; Apc4 Subunit, Anaphase-Promoting Complex-Cyclosome/metabolism ; Cytidine Triphosphate/metabolism ; Cytoskeletal Proteins/chemistry ; Cytoskeletal Proteins/genetics ; Cytoskeletal Proteins/metabolism ; HeLa Cells ; Humans ; Polyubiquitin/metabolism ; Ubiquitin/metabolism ; Ubiquitin-Conjugating Enzymes/genetics ; Ubiquitin-Conjugating Enzymes/metabolism ; Ubiquitin-Protein Ligases/chemistry ; Ubiquitin-Protein Ligases/metabolism ; Ubiquitination
    Chemical Substances ANAPC4 protein, human ; APC2 protein, human ; Apc4 Subunit, Anaphase-Promoting Complex-Cyclosome ; Cytoskeletal Proteins ; Ubiquitin ; Polyubiquitin (120904-94-1) ; Cytidine Triphosphate (65-47-4) ; UBE2C protein, human (EC 2.3.2.23) ; Ube2S protein, human (EC 2.3.2.23) ; Ubiquitin-Conjugating Enzymes (EC 2.3.2.23) ; Anaphase-Promoting Complex-Cyclosome (EC 2.3.2.27) ; Ubiquitin-Protein Ligases (EC 2.3.2.27)
    Language English
    Publishing date 2020-05-11
    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 2126708-X
    ISSN 1545-9985 ; 1545-9993
    ISSN (online) 1545-9985
    ISSN 1545-9993
    DOI 10.1038/s41594-020-0424-6
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  3. Article ; Online: BubR1 Promotes Bub3-Dependent APC/C Inhibition during Spindle Assembly Checkpoint Signaling.

    Overlack, Katharina / Bange, Tanja / Weissmann, Florian / Faesen, Alex C / Maffini, Stefano / Primorac, Ivana / Müller, Franziska / Peters, Jan-Michael / Musacchio, Andrea

    Current biology : CB

    2017  Volume 27, Issue 19, Page(s) 2915–2927.e7

    Abstract: ... ability to inhibit the MCC target anaphase-promoting complex (APC/C), suggesting that BubR1:Bub3 ... recognition and inhibition of APC/C requires phosphorylation. Thus, small sequence differences in Bub1 and ...

    Abstract The spindle assembly checkpoint (SAC) prevents premature sister chromatid separation during mitosis. Phosphorylation of unattached kinetochores by the Mps1 kinase promotes recruitment of SAC machinery that catalyzes assembly of the SAC effector mitotic checkpoint complex (MCC). The SAC protein Bub3 is a phospho-amino acid adaptor that forms structurally related stable complexes with functionally distinct paralogs named Bub1 and BubR1. A short motif ("loop") of Bub1, but not the equivalent loop of BubR1, enhances binding of Bub3 to kinetochore phospho-targets. Here, we asked whether the BubR1 loop directs Bub3 to different phospho-targets. The BubR1 loop is essential for SAC function and cannot be removed or replaced with the Bub1 loop. BubR1 loop mutants bind Bub3 and are normally incorporated in MCC in vitro but have reduced ability to inhibit the MCC target anaphase-promoting complex (APC/C), suggesting that BubR1:Bub3 recognition and inhibition of APC/C requires phosphorylation. Thus, small sequence differences in Bub1 and BubR1 direct Bub3 to different phosphorylated targets in the SAC signaling cascade.
    MeSH term(s) Anaphase-Promoting Complex-Cyclosome/antagonists & inhibitors ; Cell Cycle Proteins/genetics ; Cell Cycle Proteins/metabolism ; Humans ; M Phase Cell Cycle Checkpoints/physiology ; Phosphorylation ; Poly-ADP-Ribose Binding Proteins/genetics ; Poly-ADP-Ribose Binding Proteins/metabolism ; Protein-Serine-Threonine Kinases/genetics ; Protein-Serine-Threonine Kinases/metabolism ; Signal Transduction ; Spindle Apparatus/metabolism
    Chemical Substances BUB3 protein, human ; Cell Cycle Proteins ; Poly-ADP-Ribose Binding Proteins ; Anaphase-Promoting Complex-Cyclosome (EC 2.3.2.27) ; BUB1 protein, human (EC 2.7.11.1) ; Protein-Serine-Threonine Kinases (EC 2.7.11.1)
    Language English
    Publishing date 2017-10-09
    Publishing country England
    Document type Journal Article
    ZDB-ID 1071731-6
    ISSN 1879-0445 ; 0960-9822
    ISSN (online) 1879-0445
    ISSN 0960-9822
    DOI 10.1016/j.cub.2017.08.033
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  4. Article ; Online: Comparative analyses of C₄ and C₃ photosynthesis in developing leaves of maize and rice.

    Wang, Lin / Czedik-Eysenberg, Angelika / Mertz, Rachel A / Si, Yaqing / Tohge, Takayuki / Nunes-Nesi, Adriano / Arrivault, Stephanie / Dedow, Lauren K / Bryant, Douglas W / Zhou, Wen / Xu, Jiajia / Weissmann, Sarit / Studer, Anthony / Li, Pinghua / Zhang, Cankui / LaRue, Therese / Shao, Ying / Ding, Zehong / Sun, Qi /
    Patel, Rohan V / Turgeon, Robert / Zhu, Xinguang / Provart, Nicholas J / Mockler, Todd C / Fernie, Alisdair R / Stitt, Mark / Liu, Peng / Brutnell, Thomas P

    Nature biotechnology

    2014  Volume 32, Issue 11, Page(s) 1158–1165

    Abstract: C₄ and C₃ photosynthesis differ in the efficiency with which they consume water and nitrogen ... Engineering traits of the more efficient C₄ photosynthesis into C₃ crops could substantially increase crop ... yields in hot, arid conditions. To identify differences between C₄ and C₃ photosynthetic mechanisms ...

    Abstract C₄ and C₃ photosynthesis differ in the efficiency with which they consume water and nitrogen. Engineering traits of the more efficient C₄ photosynthesis into C₃ crops could substantially increase crop yields in hot, arid conditions. To identify differences between C₄ and C₃ photosynthetic mechanisms, we profiled metabolites and gene expression in the developing leaves of Zea mays (maize), a C₄ plant, and Oryza sativa (rice), a C₃ plant, using a statistical method named the unified developmental model (UDM). Candidate cis-regulatory elements and transcription factors that might regulate photosynthesis were identified, together with differences between C₄ and C₃ nitrogen and carbon metabolism. The UDM algorithms could be applied to analyze and compare development in other species. These data sets together with community viewers to access and mine them provide a resource for photosynthetic research that will inform efforts to engineer improvements in carbon fixation in economically valuable grass crops.
    MeSH term(s) Gene Expression Regulation, Plant ; Nitrogen/metabolism ; Oryza/physiology ; Photosynthesis ; Plant Leaves/metabolism ; Plant Leaves/physiology ; Water/metabolism ; Zea mays/physiology
    Chemical Substances Water (059QF0KO0R) ; Nitrogen (N762921K75)
    Language English
    Publishing date 2014-10-12
    Publishing country United States
    Document type Comparative Study ; Journal Article ; Research Support, Non-U.S. Gov't ; Research Support, U.S. Gov't, Non-P.H.S.
    ZDB-ID 1311932-1
    ISSN 1546-1696 ; 1087-0156
    ISSN (online) 1546-1696
    ISSN 1087-0156
    DOI 10.1038/nbt.3019
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  5. Article ; Conference proceedings: The role of cytochrome c oxidase subunit 4 isoform 2 (Cox4i2) in chronic hypoxia induced pulmonary hypertension

    Jonas, F / Veith-Berger, C / Kraut, S / Quanz, K / Gierhardt, M / Seeger, W / Grossman, L / Hüttemann, M / Weissmann, N / Sommer, N

    Pneumologie

    2016  

    Abstract: ... specific and hypoxia-regulated mitochondrial protein cytochrome c oxidase subunit 4 isoform 2 ( Cox4i2 ...

    Event/congress 57. Kongress der Deutschen Gesellschaft für Pneumologie und Beatmungsmedizin e.V., Leipzig, 2016
    Abstract Rationale: Exposure of the pulmonary vasculature to chronic hypoxia results in pulmonary vascular remodeling and development of pulmonary hypertension (PH) ultimately leading to right heart failure and death. Mitochondria have been suggested to be involved in proliferation of pulmonary arterial smooth muscle cells (PASMC) underlying pulmonary vascular remodeling. We thus aimed to investigate the role of the lung-specific and hypoxia-regulated mitochondrial protein cytochrome c oxidase subunit 4 isoform 2 ( Cox4i2 ) in chronic hypoxia-induced PH.
    Methods and Results: PASMC were isolated from wild-type (WT) mice and incubated for 36h in normoxia (21% O 2 ) or different degree of hypoxia (1 – 6% O 2 ). The maximum of Cox4i2 protein and mRNA expression, as well as hypoxia-inducible factor (HIF)-1α stabilization was detected at 1% O 2. However, chronic hypoxia-induced HIF-1α stabilization was preserved in PASMC isolated from Cox4i2 knockout mice. In vivo studies in Cox4i2 knockout or respective WT mice, which were exposed to normoxia (21% O 2 ) or chronic hypoxia (10% O 2 ) for 28 days, revealed that both strains developed PH to a similar degree as determined by hemodynamic measurements and echocardiography. The degree of muscularization of small pulmonary vessels (20 – 70 µm) trended to be reduced in Cox4i2 knockout mice compared to WT. However, there was no difference in hypoxia-induced proliferation of WT and Cox4i2 knockout PASMCs.
    Conclusion: This study demonstrates the prominent hypoxia-dependent regulation of Cox4i2 in isolated primary murine PASMCs. However, global knockout of Cox4i2 showed only slightly reduced pulmonary vascular remodeling. The role of Cox4i2 in PASMC under chronic hypoxia needs to be further evaluated.
    Language English
    Publishing date 2016-02-09
    Publishing place Stuttgart ; New York
    Document type Article ; Conference proceedings
    ZDB-ID 607630-0
    ISSN 1438-8790 ; 0934-8387
    ISSN (online) 1438-8790
    ISSN 0934-8387
    DOI 10.1055/s-0036-1572296
    Database Thieme publisher's database

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  6. Article ; Online: Cellular infiltrates and NFκB subunit c-Rel signaling in kidney allografts of patients with clinical operational tolerance.

    Becker, Luis E / de Oliveira Biazotto, Fúvia / Conrad, Heike / Schaier, Matthias / Kihm, Lars P / Gross-Weissmann, Marie-Luise / Waldherr, Rüdiger / Bierhaus, Angelika / Nawroth, Peter P / Zeier, Martin / Morath, Christian

    Transplantation

    2012  Volume 94, Issue 7, Page(s) 729–737

    Abstract: ... onset and resolution of inflammation and regulatory T cell differentiation through subunit c-Rel ... We characterized cellular infiltrates and expression of NFκB1, c-Rel and its upstream regulators ... 78% of infiltrating cells; P=0.02). c-Rel expression in cellular infiltrates was significantly ...

    Abstract Background: Nuclear factor kappa B (NFκB) plays a potential role in tolerance by orchestrating onset and resolution of inflammation and regulatory T cell differentiation through subunit c-Rel. We characterized cellular infiltrates and expression of NFκB1, c-Rel and its upstream regulators phosphatidylinositol 3-kinase/RAC-alpha serine/threonine kinase, in allograft biopsies from patients with spontaneous clinical operational tolerance (COT).
    Methods: Paraffin-fixed kidney allograft biopsies from 40 patients with COT (n=4), interstitial rejection (IR; n=12), borderline changes (BC; n=12), and long-term allograft function without rejection (NR; n=12) were used in the study. Cellular infiltrates and immunohistochemical expression of key proteins of the NFκB pathway were evaluated in the cortical tubulointerstitium and in cellular infiltrates using digital image analysis software. Results were given as mean±SEM.
    Results: Biopsies from patients with COT exhibited a comparable amount of cellular infiltrate to IR, BC, and NR (COT, 191±81; IR, 291±62; BC, 178±45; and NR, 210±42 cells/mm) but a significantly higher proportion of forkhead box P3-positive cells (COT, 11%±1.7%; IR, 3.5%±0.70%; BC, 3.4%±0.57%; and NR, 3.7%±0.78% of infiltrating cells; P=0.02). c-Rel expression in cellular infiltrates was significantly elevated in IR, BC, and NR when analyzing the number of positive cells per mm (P=0.02) and positive cells per infiltrating cells (P=0.04). In contrast, tubular PI3K and c-Rel expression were significantly higher in IR and BC but not in NR compared with COT (P=0.03 and P=0.006, respectively). With RAC-alpha serine-threonine kinase, similar tendencies were observed (P=0.2).
    Conclusions: Allografts from COT patients show significant cellular infiltrates but a distinct expression of proteins involved in the NFκB pathway and a higher proportion of forkhead box P3-positive cells.
    MeSH term(s) Adult ; Biopsy ; Chi-Square Distribution ; Female ; Forkhead Transcription Factors/analysis ; Graft Rejection/immunology ; Graft Rejection/metabolism ; Graft Rejection/pathology ; Graft Survival ; HLA-DR Antigens/analysis ; Humans ; Immunohistochemistry ; Immunosuppressive Agents/therapeutic use ; Kidney/chemistry ; Kidney/drug effects ; Kidney/immunology ; Kidney/pathology ; Kidney Transplantation/immunology ; Male ; Middle Aged ; NF-kappa B p50 Subunit/analysis ; Phosphatidylinositol 3-Kinase/analysis ; Proto-Oncogene Proteins c-akt/analysis ; Proto-Oncogene Proteins c-rel/analysis ; Signal Transduction/drug effects ; Time Factors ; Transplantation Tolerance/drug effects
    Chemical Substances FOXP3 protein, human ; Forkhead Transcription Factors ; HLA-DR Antigens ; Immunosuppressive Agents ; NF-kappa B p50 Subunit ; NFKB1 protein, human ; Proto-Oncogene Proteins c-rel ; Phosphatidylinositol 3-Kinase (EC 2.7.1.137) ; Proto-Oncogene Proteins c-akt (EC 2.7.11.1)
    Language English
    Publishing date 2012-10-15
    Publishing country United States
    Document type Comparative Study ; Journal Article ; Research Support, Non-U.S. Gov't
    ZDB-ID 208424-7
    ISSN 1534-6080 ; 0041-1337
    ISSN (online) 1534-6080
    ISSN 0041-1337
    DOI 10.1097/TP.0b013e31826032be
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  7. Article ; Online: Cryo-EM of Mitotic Checkpoint Complex-Bound APC/C Reveals Reciprocal and Conformational Regulation of Ubiquitin Ligation.

    Yamaguchi, Masaya / VanderLinden, Ryan / Weissmann, Florian / Qiao, Renping / Dube, Prakash / Brown, Nicholas G / Haselbach, David / Zhang, Wei / Sidhu, Sachdev S / Peters, Jan-Michael / Stark, Holger / Schulman, Brenda A

    Molecular cell

    2016  Volume 63, Issue 4, Page(s) 593–607

    Abstract: ... with ubiquitination activities of CDC20-activated anaphase-promoting complex/cyclosome (APC/C(CDC20)). APC/C(CDC20 ... molecule of CDC20, blocks APC/C(CDC20)-UBE2C-dependent ubiquitination of Securin and Cyclins ... activation, and checkpoint termination. Here electron microscopy reveals conformational variation of APC/C ...

    Abstract The mitotic checkpoint complex (MCC) coordinates proper chromosome biorientation on the spindle with ubiquitination activities of CDC20-activated anaphase-promoting complex/cyclosome (APC/C(CDC20)). APC/C(CDC20) and two E2s, UBE2C and UBE2S, catalyze ubiquitination through distinct architectures for linking ubiquitin (UB) to substrates and elongating polyUB chains, respectively. MCC, which contains a second molecule of CDC20, blocks APC/C(CDC20)-UBE2C-dependent ubiquitination of Securin and Cyclins, while differentially determining or inhibiting CDC20 ubiquitination to regulate spindle surveillance, checkpoint activation, and checkpoint termination. Here electron microscopy reveals conformational variation of APC/C(CDC20)-MCC underlying this multifaceted regulation. MCC binds APC/C-bound CDC20 to inhibit substrate access. However, rotation about the CDC20-MCC assembly and conformational variability of APC/C modulate UBE2C-catalyzed ubiquitination of MCC's CDC20 molecule. Access of UBE2C is limiting for subsequent polyubiquitination by UBE2S. We propose that conformational dynamics of APC/C(CDC20)-MCC modulate E2 activation and determine distinctive ubiquitination activities as part of a response mechanism ensuring accurate sister chromatid segregation.
    MeSH term(s) Anaphase-Promoting Complex-Cyclosome/metabolism ; Anaphase-Promoting Complex-Cyclosome/ultrastructure ; Binding Sites ; Cdc20 Proteins/metabolism ; Cdc20 Proteins/ultrastructure ; Chromosome Segregation ; Cryoelectron Microscopy ; Humans ; M Phase Cell Cycle Checkpoints ; Models, Molecular ; Protein Binding ; Protein Conformation ; Spindle Apparatus/metabolism ; Spindle Apparatus/ultrastructure ; Structure-Activity Relationship ; Ubiquitin/metabolism ; Ubiquitin-Activating Enzymes/metabolism ; Ubiquitin-Activating Enzymes/ultrastructure ; Ubiquitin-Conjugating Enzymes/metabolism ; Ubiquitin-Conjugating Enzymes/ultrastructure ; Ubiquitination
    Chemical Substances Cdc20 Proteins ; UBA1 protein, human ; Ubiquitin ; CDC20 protein, human (156288-95-8) ; UBE2C protein, human (EC 2.3.2.23) ; Ube2S protein, human (EC 2.3.2.23) ; Ubiquitin-Conjugating Enzymes (EC 2.3.2.23) ; Anaphase-Promoting Complex-Cyclosome (EC 2.3.2.27) ; Ubiquitin-Activating Enzymes (EC 6.2.1.45)
    Language English
    Publishing date 2016-08-10
    Publishing country United States
    Document type Journal Article ; Video-Audio Media
    ZDB-ID 1415236-8
    ISSN 1097-4164 ; 1097-2765
    ISSN (online) 1097-4164
    ISSN 1097-2765
    DOI 10.1016/j.molcel.2016.07.003
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  8. Article ; Online: Dual RING E3 Architectures Regulate Multiubiquitination and Ubiquitin Chain Elongation by APC/C.

    Brown, Nicholas G / VanderLinden, Ryan / Watson, Edmond R / Weissmann, Florian / Ordureau, Alban / Wu, Kuen-Phon / Zhang, Wei / Yu, Shanshan / Mercredi, Peter Y / Harrison, Joseph S / Davidson, Iain F / Qiao, Renping / Lu, Ying / Dube, Prakash / Brunner, Michael R / Grace, Christy R R / Miller, Darcie J / Haselbach, David / Jarvis, Marc A /
    Yamaguchi, Masaya / Yanishevski, David / Petzold, Georg / Sidhu, Sachdev S / Kuhlman, Brian / Kirschner, Marc W / Harper, J Wade / Peters, Jan-Michael / Stark, Holger / Schulman, Brenda A

    Cell

    2016  Volume 165, Issue 6, Page(s) 1440–1453

    Abstract: ... and biochemistry show that the human E3 anaphase-promoting complex/cyclosome (APC/C) and its two ... distinct forms of polyubiquitination. The APC/C RING constrains UBE2C proximal to a substrate and ... of APC/C regulation, and establish principles by which specialized E3-E2-substrate-UB architectures ...

    Abstract Protein ubiquitination involves E1, E2, and E3 trienzyme cascades. E2 and RING E3 enzymes often collaborate to first prime a substrate with a single ubiquitin (UB) and then achieve different forms of polyubiquitination: multiubiquitination of several sites and elongation of linkage-specific UB chains. Here, cryo-EM and biochemistry show that the human E3 anaphase-promoting complex/cyclosome (APC/C) and its two partner E2s, UBE2C (aka UBCH10) and UBE2S, adopt specialized catalytic architectures for these two distinct forms of polyubiquitination. The APC/C RING constrains UBE2C proximal to a substrate and simultaneously binds a substrate-linked UB to drive processive multiubiquitination. Alternatively, during UB chain elongation, the RING does not bind UBE2S but rather lures an evolving substrate-linked UB to UBE2S positioned through a cullin interaction to generate a Lys11-linked chain. Our findings define mechanisms of APC/C regulation, and establish principles by which specialized E3-E2-substrate-UB architectures control different forms of polyubiquitination.
    MeSH term(s) Amino Acid Sequence ; Anaphase-Promoting Complex-Cyclosome/chemistry ; Anaphase-Promoting Complex-Cyclosome/metabolism ; Biocatalysis ; Cryoelectron Microscopy ; Humans ; Models, Molecular ; Saccharomyces cerevisiae Proteins/chemistry ; Structure-Activity Relationship ; Ubiquitin/metabolism ; Ubiquitin-Conjugating Enzymes/metabolism ; Ubiquitination
    Chemical Substances Saccharomyces cerevisiae Proteins ; Ubiquitin ; UBE2C protein, human (EC 2.3.2.23) ; Ubiquitin-Conjugating Enzymes (EC 2.3.2.23) ; Anaphase-Promoting Complex-Cyclosome (EC 2.3.2.27)
    Language English
    Publishing date 2016-06-02
    Publishing country United States
    Document type Journal Article ; Research Support, N.I.H., Extramural ; Research Support, Non-U.S. Gov't
    ZDB-ID 187009-9
    ISSN 1097-4172 ; 0092-8674
    ISSN (online) 1097-4172
    ISSN 0092-8674
    DOI 10.1016/j.cell.2016.05.037
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  9. Article: Antioxidant vitamin C improves endothelial function in obstructive sleep apnea.

    Grebe, Mathias / Eisele, Hans Joachim / Weissmann, Norbert / Schaefer, Christian / Tillmanns, Harald / Seeger, Werner / Schulz, Richard

    American journal of respiratory and critical care medicine

    2006  Volume 173, Issue 8, Page(s) 897–901

    Abstract: ... before and after intravenous injection of the antioxidant vitamin C. The investigator performing the FMD ... vitamin C, vasoreactivity remained unchanged in the control subjects. In the patients with OSA, ascorbate ... by the free radical scavenger vitamin C. These results are in favor of oxidative stress being responsible for the endothelial ...

    Abstract Rationale: Obstructive sleep apnea (OSA) is associated with oxidative stress, endothelial dysfunction, and increased cardiovascular morbidity and mortality.
    Objective: We tested the hypothesis that endothelial dysfunction in patients with OSA is linked to oxidative stress.
    Methods: In the present study, we measured flow-mediated dilation (FMD) of the brachial artery by ultrasound in 10 otherwise healthy, untreated patients with OSA and 10 age-and sex-matched control subjects without sleep-disordered breathing before and after intravenous injection of the antioxidant vitamin C. The investigator performing the FMD measurements was blinded to the status of the patients.
    Results: When compared with control subjects, baseline FMD was significantly reduced in the patients with OSA. After intravenous injection of 0.5 g vitamin C, vasoreactivity remained unchanged in the control subjects. In the patients with OSA, ascorbate led to an increase in FMD to a level comparable to that observed in the control group.
    Conclusion: The reduced endothelial-dependent vasodilation in untreated patients with OSA acutely improves by the free radical scavenger vitamin C. These results are in favor of oxidative stress being responsible for the endothelial dysfunction in OSA. Antioxidant strategies should be explored for the treatment of OSA-related cardiovascular disease.
    MeSH term(s) Administration, Sublingual ; Antioxidants/administration & dosage ; Antioxidants/therapeutic use ; Ascorbic Acid/administration & dosage ; Ascorbic Acid/therapeutic use ; Brachial Artery/diagnostic imaging ; Brachial Artery/drug effects ; Brachial Artery/physiopathology ; Endothelium, Vascular/drug effects ; Endothelium, Vascular/physiopathology ; Female ; Humans ; Injections, Intravenous ; Male ; Middle Aged ; Nitroglycerin/administration & dosage ; Polysomnography ; Sleep Apnea, Obstructive/drug therapy ; Sleep Apnea, Obstructive/physiopathology ; Treatment Outcome ; Ultrasonography ; Vasodilation/drug effects ; Vasodilation/physiology ; Vasodilator Agents/administration & dosage
    Chemical Substances Antioxidants ; Vasodilator Agents ; Nitroglycerin (G59M7S0WS3) ; Ascorbic Acid (PQ6CK8PD0R)
    Language English
    Publishing date 2006-04-15
    Publishing country United States
    Document type Comparative Study ; Journal Article
    ZDB-ID 1180953-x
    ISSN 1535-4970 ; 1073-449X ; 0003-0805
    ISSN (online) 1535-4970
    ISSN 1073-449X ; 0003-0805
    DOI 10.1164/rccm.200508-1223OC
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  10. Article ; Online: c-ANCA-induced neutrophil-mediated lung injury: a model of acute Wegener's granulomatosis.

    Hattar, K / Oppermann, S / Ankele, C / Weissmann, N / Schermuly, R T / Bohle, R M / Moritz, R / Krögel, B / Seeger, W / Grimminger, F / Sibelius, U / Grandel, U

    The European respiratory journal

    2010  Volume 36, Issue 1, Page(s) 187–195

    Abstract: Anti-neutrophil cytoplasmic antibodies (c-ANCA) targeting proteinase 3 (PR3) are implicated ... PMNs. The c-ANCA-induced oedema formation was paralleled by an increase in the capillary filtration ... oxidase inhibitor, c-ANCA-induced lung oedema could be prevented. Inhibition of neutrophil elastase was ...

    Abstract Anti-neutrophil cytoplasmic antibodies (c-ANCA) targeting proteinase 3 (PR3) are implicated in the pathogenesis of Wegener's granulomatosis (WG). Fulminant disease can present as acute lung injury (ALI). In this study, a model of ALI in WG was developed using isolated rat lungs. Isolated human polymorphonuclear leukocytes (PMNs) were primed with tumour necrosis factor (TNF) to induce surface expression of PR3. Co-perfusion of TNF-primed neutrophils and monoclonal anti-PR3 antibodies induced a massive weight gain in isolated lungs. This effect was not observed when control immunoglobulin G was co-perfused with TNF-primed PMNs. The c-ANCA-induced oedema formation was paralleled by an increase in the capillary filtration coefficient as a marker of increased pulmonary endothelial permeability. In contrast, pulmonary artery pressure was not affected. In the presence of the oxygen radical scavenger superoxide dismutase and a NADPH oxidase inhibitor, c-ANCA-induced lung oedema could be prevented. Inhibition of neutrophil elastase was equally effective in preventing c-ANCA-induced lung injury. In conclusion, anti-PR3 antibodies induced neutrophil mediated, elastase- and oxygen radical-dependent ALI in the isolated lung. This experimental model supports the hypothesis of a pathogenic role for c-ANCA in WG and offers the possibility of the development of therapeutic strategies for the treatment of lung injury in fulminant WG.
    MeSH term(s) Acute Lung Injury/drug therapy ; Acute Lung Injury/immunology ; Acute Lung Injury/pathology ; Acute Lung Injury/prevention & control ; Animals ; Antibodies, Antineutrophil Cytoplasmic/immunology ; Antibodies, Antineutrophil Cytoplasmic/pharmacology ; Antibodies, Monoclonal/pharmacology ; Disease Models, Animal ; Enzyme Inhibitors/pharmacology ; Granulomatosis with Polyangiitis/drug therapy ; Granulomatosis with Polyangiitis/immunology ; Granulomatosis with Polyangiitis/prevention & control ; Humans ; Immunoglobulin G/immunology ; Immunoglobulin G/pharmacology ; Leukocyte Elastase/antagonists & inhibitors ; Myeloblastin/immunology ; NADPH Oxidases/antagonists & inhibitors ; Neutrophil Activation/immunology ; Neutrophils/immunology ; Pulmonary Edema/immunology ; Pulmonary Edema/prevention & control ; Rats ; Superoxide Dismutase/analysis ; Tumor Necrosis Factor-alpha/immunology ; Tumor Necrosis Factor-alpha/pharmacology
    Chemical Substances Antibodies, Antineutrophil Cytoplasmic ; Antibodies, Monoclonal ; Enzyme Inhibitors ; Immunoglobulin G ; Tumor Necrosis Factor-alpha ; Superoxide Dismutase (EC 1.15.1.1) ; NADPH Oxidases (EC 1.6.3.-) ; Leukocyte Elastase (EC 3.4.21.37) ; Myeloblastin (EC 3.4.21.76)
    Language English
    Publishing date 2010-07
    Publishing country England
    Document type Journal Article ; Research Support, Non-U.S. Gov't
    ZDB-ID 639359-7
    ISSN 1399-3003 ; 0903-1936
    ISSN (online) 1399-3003
    ISSN 0903-1936
    DOI 10.1183/09031936.00143308
    Database MEDical Literature Analysis and Retrieval System OnLINE

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