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  • 1
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    Ktu/PF13 is required for cytoplasmic pre-assembly of axonemal dyneins (2008)
    Nature Publishing Group (NPG)
    Details
    Publication Date: 2008-12-05
    Description: Cilia and flagella are highly conserved organelles that have diverse roles in cell motility and sensing extracellular signals. Motility defects in cilia and flagella often result in primary ciliary dyskinesia. However, the mechanisms underlying cilia formation and function, and in particular the cytoplasmic assembly of dyneins that power ciliary motility, are only poorly understood. Here we report a new gene, kintoun (ktu), involved in this cytoplasmic process. This gene was first identified in a medaka mutant, and found to be mutated in primary ciliary dyskinesia patients from two affected families as well as in the pf13 mutant of Chlamydomonas. In the absence of Ktu/PF13, both outer and inner dynein arms are missing or defective in the axoneme, leading to a loss of motility. Biochemical and immunohistochemical studies show that Ktu/PF13 is one of the long-sought proteins involved in pre-assembly of dynein arm complexes in the cytoplasm before intraflagellar transport loads them for the ciliary compartment.〈br /〉〈br /〉〈a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3279746/" target="_blank"〉〈img src="https://static.pubmed.gov/portal/portal3rc.fcgi/4089621/img/3977009" border="0"〉〈/a〉   〈a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3279746/" target="_blank"〉This paper as free author manuscript - peer-reviewed and accepted for publication〈/a〉〈br /〉〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Omran, Heymut -- Kobayashi, Daisuke -- Olbrich, Heike -- Tsukahara, Tatsuya -- Loges, Niki T -- Hagiwara, Haruo -- Zhang, Qi -- Leblond, Gerard -- O'Toole, Eileen -- Hara, Chikako -- Mizuno, Hideaki -- Kawano, Hiroyuki -- Fliegauf, Manfred -- Yagi, Toshiki -- Koshida, Sumito -- Miyawaki, Atsushi -- Zentgraf, Hanswalter -- Seithe, Horst -- Reinhardt, Richard -- Watanabe, Yoshinori -- Kamiya, Ritsu -- Mitchell, David R -- Takeda, Hiroyuki -- GM44228/GM/NIGMS NIH HHS/ -- R01 GM044228/GM/NIGMS NIH HHS/ -- R01 GM044228-17/GM/NIGMS NIH HHS/ -- England -- Nature. 2008 Dec 4;456(7222):611-6. doi: 10.1038/nature07471.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Pediatrics and Adolescent Medicine, University Hospital Freiburg Mathildenstrasse 1, D-79106 Freiburg, Germany. heymut.omran@uniklinik-freiburg.de〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/19052621" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Axoneme/chemistry/genetics/*metabolism/pathology ; Chlamydomonas/genetics/metabolism ; Cilia/chemistry/genetics/*metabolism/pathology ; Cloning, Molecular ; Dyneins/*metabolism ; Epithelial Cells/cytology ; Fish Proteins/genetics/*metabolism ; Genes, Recessive/genetics ; HSP70 Heat-Shock Proteins/metabolism ; Humans ; Kartagener Syndrome/genetics/pathology ; Male ; Mice ; Molecular Sequence Data ; Mutation/genetics ; *Oryzias/embryology/genetics/metabolism ; Protein Binding ; Proteins/genetics/*metabolism ; Sequence Homology, Amino Acid ; Sperm Motility ; Testis/cytology
    Print ISSN: 0028-0836
    Electronic ISSN: 1476-4687
    Topics: Biology , Chemistry and Pharmacology , Medicine , Natural Sciences in General , Physics
    Published by Nature Publishing Group (NPG)
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  • 2
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    A beta 3 integrin mutation abolishes ligand binding and alters divalent cation-dependent conformation (1990)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1990-08-24
    Description: The ligand-binding function of integrin adhesion receptors depends on divalent cations. A mutant alpha IIb beta 3 integrin (platelet gpIIb/IIIa) that lacks ligand recognition shows immunologic evidence of a perturbed interaction with divalent cations. This was found to be caused by a G----T mutation that resulted in an Asp119----Tyr119 substitution in the beta 3 subunit. This residue is proximal to bound ligand and is in a conserved region among integrins that are enriched in oxygenated residues. The spacing of these residues aligns with the calcium-binding residues in EF hand proteins, suggesting interaction with receptor-bound divalent cation as a mechanism of ligand binding common to all integrins.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Loftus, J C -- O'Toole, T E -- Plow, E F -- Glass, A -- Frelinger, A L 3rd -- Ginsberg, M H -- AR 27214/AR/NIAMS NIH HHS/ -- HL 28235/HL/NHLBI NIH HHS/ -- HL 42977/HL/NHLBI NIH HHS/ -- etc. -- New York, N.Y. -- Science. 1990 Aug 24;249(4971):915-8.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Committee on Vascular Biology, Research Institute of Scripps Clinic, La Jolla, CA 92037.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/2392682" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Aspartic Acid ; Base Sequence ; Binding Sites ; Cell Line ; Integrins/*genetics/metabolism ; Ligands ; Macromolecular Substances ; Molecular Sequence Data ; *Mutation ; Oligonucleotide Probes ; Platelet Membrane Glycoproteins/*genetics/metabolism ; Polymerase Chain Reaction ; Protein Conformation ; Sequence Homology, Nucleic Acid ; Tyrosine
    Print ISSN: 0036-8075
    Electronic ISSN: 1095-9203
    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
    Published by American Association for the Advancement of Science (AAAS)
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  • 3
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    Modulation of the affinity of integrin alpha IIb beta 3 (GPIIb-IIIa) by the cytoplasmic domain of alpha IIb (1991)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1991-11-08
    Description: Intracellular signaling alters integrin adhesive functions in inflammation, immune responses, hemostasis, thrombosis, and retinal development. By truncating the cytoplasmic domain of alpha IIb, the affinity of integrin alpha IIb beta 3 for ligand was increased. Reconstitution with the cytoplasmic domain from integrin alpha 5 did not reverse the increased affinity. Thus, the cytoplasmic domain of the alpha subunit of GPIIb-IIIa controls ligand binding affinity, which suggests mechanisms for inside-out transmembrane signaling through integrins. These findings imply the existence of hitherto unappreciated hereditary and acquired thrombotic disorders in humans.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉O'Toole, T E -- Mandelman, D -- Forsyth, J -- Shattil, S J -- Plow, E F -- Ginsberg, M H -- HL 39150/HL/NHLBI NIH HHS/ -- HL16411/HL/NHLBI NIH HHS/ -- HL28235/HL/NHLBI NIH HHS/ -- etc. -- New York, N.Y. -- Science. 1991 Nov 8;254(5033):845-7.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Committee on Vascular Biology, Scripps Research Institute, La Jolla, CA 92037.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1948065" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; CHO Cells ; Cell Aggregation ; Cricetinae ; Cytoplasm/metabolism ; Fibrinogen/metabolism ; Kinetics ; Macromolecular Substances ; Molecular Sequence Data ; Mutagenesis, Site-Directed ; Platelet Membrane Glycoproteins/genetics/*physiology ; Transfection
    Print ISSN: 0036-8075
    Electronic ISSN: 1095-9203
    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
    Published by American Association for the Advancement of Science (AAAS)
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  • 4
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    A selective activity-dependent requirement for dynamin 1 in synaptic vesicle endocytosis (2007)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2007-04-28
    Description: Dynamin 1 is a neuron-specific guanosine triphosphatase thought to be critically required for the fission reaction of synaptic vesicle endocytosis. Unexpectedly, mice lacking dynamin 1 were able to form functional synapses, even though their postnatal viability was limited. However, during spontaneous network activity, branched, tubular plasma membrane invaginations accumulated, capped by clathrin-coated pits, in synapses of dynamin 1-knockout mice. Synaptic vesicle endocytosis was severely impaired during strong exogenous stimulation but resumed efficiently when the stimulus was terminated. Thus, dynamin 1-independent mechanisms can support limited synaptic vesicle endocytosis, but dynamin 1 is needed during high levels of neuronal activity.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Ferguson, Shawn M -- Brasnjo, Gabor -- Hayashi, Mitsuko -- Wolfel, Markus -- Collesi, Chiara -- Giovedi, Silvia -- Raimondi, Andrea -- Gong, Liang-Wei -- Ariel, Pablo -- Paradise, Summer -- O'toole, Eileen -- Flavell, Richard -- Cremona, Ottavio -- Miesenbock, Gero -- Ryan, Timothy A -- De Camilli, Pietro -- CA46128/CA/NCI NIH HHS/ -- D.061/Telethon/Italy -- DA018343/DA/NIDA NIH HHS/ -- DA17297/DA/NIDA NIH HHS/ -- DK45735/DK/NIDDK NIH HHS/ -- NS036942/NS/NINDS NIH HHS/ -- NS36251/NS/NINDS NIH HHS/ -- P30 DA018343/DA/NIDA NIH HHS/ -- R01 NS036942/NS/NINDS NIH HHS/ -- RR-000592/RR/NCRR NIH HHS/ -- New York, N.Y. -- Science. 2007 Apr 27;316(5824):570-4.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Howard Hughes Medical Institute, Kavli Institute for Neuroscience, Yale University School of Medicine, New Haven, CT 06510, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/17463283" target="_blank"〉PubMed〈/a〉
    Keywords: Action Potentials ; Animals ; Cell Membrane/ultrastructure ; Clathrin-Coated Vesicles/metabolism/ultrastructure ; Dynamin I/genetics/*physiology ; Dynamin II ; Dynamin III/physiology ; Electric Stimulation ; *Endocytosis ; Excitatory Postsynaptic Potentials ; Exocytosis ; Inhibitory Postsynaptic Potentials ; Mice ; Mice, Knockout ; Microscopy, Electron ; Neurons/*physiology/ultrastructure ; Patch-Clamp Techniques ; Presynaptic Terminals/physiology/ultrastructure ; Synapses/*physiology/ultrastructure ; Synaptic Transmission ; Synaptic Vesicles/*physiology/ultrastructure
    Print ISSN: 0036-8075
    Electronic ISSN: 1095-9203
    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
    Published by American Association for the Advancement of Science (AAAS)
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  • 5
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    iRHOM2-dependent regulation of ADAM17 in cutaneous disease and epidermal barrier function (2014)
    Oxford University Press
    Details
    Publication Date: 2014-07-05
    Description: iRHOM2 is a highly conserved, catalytically inactive member of the Rhomboid family, which has recently been shown to regulate the maturation of the multi-substrate ectodomain sheddase enzyme ADAM17 (TACE) in macrophages. Dominant iRHOM2 mutations are the cause of the inherited cutaneous and oesophageal cancer-susceptibility syndrome tylosis with oesophageal cancer (TOC), suggesting a role for this protein in epithelial cells. Here, using tissues derived from TOC patients, we demonstrate that TOC-associated mutations in iRHOM2 cause an increase in the maturation and activity of ADAM17 in epidermal keratinocytes, resulting in significantly upregulated shedding of ADAM17 substrates, including EGF-family growth factors and pro-inflammatory cytokines. This activity is accompanied by increased EGFR activity, increased desmosome processing and the presence of immature epidermal desmosomes, upregulated epidermal transglutaminase activity and heightened resistance to Staphylococcal infection in TOC keratinocytes. Many of these features are consistent with the presence of a constitutive wound-healing-like phenotype in TOC epidermis, which may shed light on a novel pathway in skin repair, regeneration and inflammation.
    Print ISSN: 0964-6906
    Electronic ISSN: 1460-2083
    Topics: Biology , Medicine
    Published by Oxford University Press
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  • 6
    Electronic Resource
    Electronic Resource
    High Voltage Cryomicroscopy of Human Blood Platelets
    Amsterdam : Elsevier
    Journal of Structural Biology 110 (1993), S. 55-66 
    Details
    ISSN: 1047-8477
    Source: Elsevier Journal Backfiles on ScienceDirect 1907 - 2002
    Topics: Biology
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1006/jsbi.1993.1004
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    Paper (German National Licenses)
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  • 7
    Electronic Resource
    Electronic Resource
    Characterization of carbon nitride films grown using an inductively-coupled plasma with adamantane as the source hydrocarbon†Paper presented at the Fifth International Conference on Adhesion and Surface Analysis, Loughborough, UK 31 March-2 April 1998. (1998)
    Chichester [u.a.] : Wiley-Blackwell
    Surface and Interface Analysis 26 (1998), S. 896-902 
    Details
    ISSN: 0142-2421
    Keywords: carbon nitride films ; inductively-coupled plasma deposition ; adamantane ; Chemistry ; Polymer and Materials Science
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Physics
    Notes: The films addressed here were grown using adamantane (C10H16) vapour in flowing argon/nitrogen mixtures in an inductively-coupled plasma processing (ICP) vacuum rig. The films were characterized by XPS, AES, infrared spectroscopy (Fourier transform infrared (FTIR) in transmission) and atomic force microscopy. The x-ray photoelectron data showed typically high nitrogen contents, and deconvolution of the observed C 1s band confirmed the presence of the chemical states identified by FTIR. Further XPS-quantified data established the changes observed in the relative carbon and nitrogen concentrations as a function of deposition regime.Evidence of a structural transformation in the films over time was established from the FTIR spectra, which exhibited significant changes in the relative intensities of the C≡N, C=N/C=C, NH and CH bands identified attendant on the deposition parameters.Analysis by AES revealed additionally an increasing carbon/nitrogen ratio, suggesting the transformation of sp3 to sp3 carbon was taking place in the film, with some nitrogen lost from the films during data acquisition. These data indicated clearly that the electron beam-stimulating production of the Auger spectra contributed to the transformation of the chemical states present initially.Finally, atomic force microscopy of the surfaces showed that the surface morphology of the film changes during Auger analysis. © 1998 John Wiley & Sons, Ltd.
    Additional Material: 6 Ill.
    Type of Medium: Electronic Resource
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