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  • 1
    Language: English
    In: Science (New York, N.Y.), 12 October 2018, Vol.362(6411), pp.151-152
    Description: Expanding the functional and structural repertoire of the proteome through protein dimerization is a fundamental concept in biology. Dimerization can occur in a homo- or heterotypic fashion with recurrent modular domains, such as BTB (BR-C, ttk, and bab) domains, leucine zippers, or coiled coils. Dimerization is a key factor in the regulation of enzymes, ion channels, receptors, and transcription factors. Indeed, proteomic studies indicate that a large fraction of mammalian proteins function only as dimers or multimers in cells (1). Thus, correct dimer formation is of fundamental importance for a healthy proteome and consequently for a healthy organism. However, whereas quality control systems for RNA, DNA, and the folding of nascent proteins are well-studied, whether and how correct composition of protein complexes is surveyed by cells has been unknown. On page 198 of this issue, Mena et al. (2) describe a quality control pathway that detects and eliminates nonfunctional dimer complexes. A failing dimerization quality control (DQC) pathway leads to the accumulation of aberrant dimers, which could contribute to the pathology of various diseases.
    Keywords: Dimerization ; Ubiquitination
    ISSN: 00368075
    E-ISSN: 1095-9203
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  • 2
    Language: English
    In: Nature, September 2018, Vol.561(7722), pp.185-186
    Description: [...]an absence of STING prevented the movement defects and neuronal losses that usually occur in old mutator mice that lack parkin. [...]given that impaired mitophagy and inflammation are common features of several neurodegenerative disorders, it is tempting to speculate that STING-dependent inflammation...
    Keywords: Immunology ; Parkinson'S Disease ; Inflammation ; Mitochondria
    ISSN: 00280836
    E-ISSN: 1476-4687
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  • 3
    In: Nature, 2016
    Description: Ubiquitin is a polypeptide of 76 amino acids that, when covalently attached to substrate proteins, results in either modulation of the protein's function or its destruction by the cell's proteasome machinery. Since its discovery in the late 1970s, conjugation of ubiquitin to substrate proteins has been...
    Keywords: Proteins ; Studies ; Cell Division ; Enzymes ; Mass Spectrometry ; Scientific Imaging;
    ISSN: 0028-0836
    E-ISSN: 14764687
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  • 4
    Language: English
    In: Proceedings of the National Academy of Sciences of the United States of America, 22 November 2016, Vol.113(47), pp.13266-13268
    Description: Author contributions: D.H. and I.D. wrote the paper.
    Keywords: Cytoplasm ; Proteasome Endopeptidase Complex
    ISSN: 00278424
    E-ISSN: 1091-6490
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  • 5
    Language: English
    In: Proceedings of the National Academy of Sciences of the United States of America, 29 October 2013, Vol.110(44), pp.17606-7
    Description: Author contributions: M.P. and I.D. wrote the paper.
    Keywords: Parkinson Disease -- Physiopathology ; Polyubiquitin -- Chemistry ; Protein Engineering -- Methods ; Alpha-Synuclein -- Chemistry
    ISSN: 00278424
    E-ISSN: 1091-6490
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  • 6
    Article
    Article
    Language: English
    In: Current Biology, 07 February 2012, Vol.22(3), pp.R76-R77
    Keywords: Biology
    ISSN: 0960-9822
    E-ISSN: 1879-0445
    Source: ScienceDirect Journals (Elsevier)
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  • 7
    Language: English
    In: The Journal of biological chemistry, 13 April 2018, Vol.293(15), pp.5404-5413
    Description: Ubiquitination is a widespread post-translational modification that controls multiple steps in autophagy, a major lysosome-mediated intracellular degradation pathway. A variety of ubiquitin chains are attached as selective labels on protein aggregates and dysfunctional organelles, thus promoting their autophagy-dependent degradation. Moreover, ubiquitin modification of autophagy regulatory components is essential to positively or negatively regulate autophagy flux in both non-selective and selective pathways. We review the current findings that elucidate the components, timing, and kinetics of the multivalent role of ubiquitin signals in control of amplitude and selectivity of autophagy pathways as well as their impact on the development of human diseases.
    Keywords: Protein Aggregates ; Proteolysis ; Ubiquitination ; Lysosomes -- Metabolism ; Ubiquitin -- Metabolism
    E-ISSN: 1083-351X
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  • 8
    Language: English
    In: Cell, 25 February 2016, Vol.164(5), pp.1074-1074.e1
    Description: The Ubiquitin (Ub) system coordinates vital cellular processes by controlling lifetime, signaling, and binding properties of proteins. Ub serves as a multivalent protein tag that is further diversified by post-translational modifications. Specialized Ub receptors then convert the encoded signals into cellular responses. This SnapShot highlights the importance of the rapidly expanding Ub code in biology as well as novel pharmacological approaches to target the Ub system in multiple diseases. To view this SnapShot, open or download the PDF. The Ubiquitin (Ub) system coordinates vital cellular processes by controlling lifetime, signaling, and binding properties of proteins. Ub serves as a multivalent protein tag that is further diversified by post-translational modifications. Specialized Ub receptors then convert the encoded signals into cellular responses. This SnapShot highlights the importance of the rapidly expanding Ub code in biology as well as novel pharmacological approaches to target the Ub system in multiple diseases. To view this SnapShot, open or download the PDF.
    Keywords: Biology
    ISSN: 0092-8674
    E-ISSN: 1097-4172
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  • 9
    Language: English
    In: Cell, 28 March 2013, Vol.153(1), pp.14-16
    Description: Cullin-RING ubiquitin ligase complexes (CRLs) rely on a vast array of adaptor proteins to recognize their substrates. Pierce et al. and related papers from Zemla et al. and Wu et al. in show that Cand1 promotes exchange of adaptor proteins to regulate the CRL repertoire.
    Keywords: Biology
    ISSN: 0092-8674
    E-ISSN: 1097-4172
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  • 10
    Language: English
    In: Science (New York, N.Y.), 08 July 2011, Vol.333(6039), pp.228-33
    Description: Selective autophagy can be mediated via receptor molecules that link specific cargoes to the autophagosomal membranes decorated by ubiquitin-like microtubule-associated protein light chain 3 (LC3) modifiers. Although several autophagy receptors have been identified, little is known about mechanisms controlling their functions in vivo. In this work, we found that phosphorylation of an autophagy receptor, optineurin, promoted selective autophagy of ubiquitin-coated cytosolic Salmonella enterica. The protein kinase TANK binding kinase 1 (TBK1) phosphorylated optineurin on serine-177, enhancing LC3 binding affinity and autophagic clearance of cytosolic Salmonella. Conversely, ubiquitin- or LC3-binding optineurin mutants and silencing of optineurin or TBK1 impaired Salmonella autophagy, resulting in increased intracellular bacterial proliferation. We propose that phosphorylation of autophagy receptors might be a general mechanism for regulation of cargo-selective autophagy.
    Keywords: Autophagy ; Cytosol -- Microbiology ; Salmonella Typhimurium -- Growth & Development ; Transcription Factor Tfiiia -- Metabolism
    ISSN: 00368075
    E-ISSN: 1095-9203
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