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  • 1
    Electronic Resource
    Electronic Resource
    Intracellular Structure and Elemental Analysis in Rapid-Frozen Neurons (1986)
    Oxford, UK : Blackwell Publishing Ltd
    Annals of the New York Academy of Sciences 483 (1986), S. 0 
    Details
    ISSN: 1749-6632
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Natural Sciences in General
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1749-6632.1986.tb34534.x
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  • 2
    Electronic Resource
    Electronic Resource
    Evidence for the lipidic nature of tight junction strands (1982)
    [s.l.] : Nature Publishing Group
    Nature 296 (1982), S. 464-466 
    Details
    ISSN: 1476-4687
    Source: Nature Archives 1869 - 2009
    Topics: Biology , Chemistry and Pharmacology , Medicine , Natural Sciences in General , Physics
    Notes: [Auszug] Tight junction strands have been assumed to consist of a row of intramembrane particles representing integral membrane proteins which on fixation (glutaraldehyde 1-5%) and cryo-protection (glycerol 20-30%) form the continuous fibrils observed in standard freeze-fracture replicas5'7'12'16. This ...
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1038/296464a0
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  • 3
    Electronic Resource
    Electronic Resource
    Interactions among endoplasmic reticulum, microtubules, and retrograde movements of the cell surface (1994)
    New York, NY : Wiley-Blackwell
    Cell Motility and the Cytoskeleton 29 (1994), S. 291-300 
    Details
    ISSN: 0886-1544
    Keywords: endoplasmic reticulum ; DiOC6(3) ; microtubules ; Life and Medical Sciences ; Cell & Developmental Biology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Medicine
    Notes: Relationships among the endoplasmic reticulum (ER), microtubules, and bead movements on the cell surface were investigated in the thin peripheral region of A6 cells, a frog kidney cell line. ER tubules were often aligned with microtubules, as shown by double-labeling with DiOC6(3) and anti-tubulin in fixed cells. In living cells stained with DiOC6(3) and observed in time lapse, there were frequent extensions, but few retractions, of ER tubules. In addition, there was a steady retrograde (towards the cell center) movement of all of the ER at ∼0.3 μm/min. Since microtubules are often aligned with the ER, microtubules must also be moving retrogradely. By simultaneous imaging, it was found that the ER moves retrogradely at the same rate as aminated latex beads on the cell surface. This indicates that the mechanisms for ER and bead movement are closely related. Cytochalasin B stopped bead and ER movement in most of the cells, providing evidence that actin is involved in both retrograde movements. The ER retracted towards the cell center in nocodazole while both ER and microtubules retracted in taxol. Time lapse observations showed that for both drugs, the retraction of the ER is the result of retrograde movement in the absence of new ER extensions. Presumably, ER extensions do not occur in nocodazole because of the absence of microtubules, and do not occur in taxol because taxol-stabilized microtubules move retrogradely and there is no polymerization of new microtubule tracks for ER elongation. © 1994 Wiley-Liss, Inc.This Article is a US Government work and, as such, is in the public domain in the United States of America.
    Additional Material: 5 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/cm.970290402
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  • 4
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    Persistent accumulation of calcium/calmodulin-dependent protein kinase II in dendritic spines after induction of NMDA receptor-dependent chemical long-term potentiation (2009)
    Society for Neuroscience
    Details
    Publication Date: 2022-05-25
    Description: Author Posting. © Society for Neuroscience, 2004. This article is posted here by permission of Society for Neuroscience for personal use, not for redistribution. The definitive version was published in Journal of Neuroscience 24 (2004): 9324-9331, doi:10.1523/JNEUROSCI.2350-04.2004.
    Description: Calcium/calmodulin-dependent protein kinase II (CaMKII) is a leading candidate for a synaptic memory molecule because it is persistently activated after long-term potentiation (LTP) induction and because mutations that block this persistent activity prevent LTP and learning. Previous work showed that synaptic stimulation causes a rapidly reversible translocation of CaMKII to the synaptic region. We have now measured green fluorescent protein (GFP)-CaMKIIα translocation into synaptic spines during NMDA receptor-dependent chemical LTP (cLTP) and find that under these conditions, translocation is persistent. Using red fluorescent protein as a cell morphology marker, we found that there are two components of the persistent accumulation. cLTP produces a persistent increase in spine volume, and some of the increase in GFP-CaMKIIα is secondary to this volume change. In addition, cLTP results in a dramatic increase in the bound fraction of GFP-CaMKIIα in spines. To further study the bound pool, immunogold electron microscopy was used to measure CaMKIIα in the postsynaptic density (PSD), an important regulator of synaptic function. cLTP produced a persistent increase in the PSD-associated pool of CaMKIIα. These results are consistent with the hypothesis that CaMKIIα accumulation at synapses is a memory trace of past synaptic activity.
    Description: This work was supported by Grant R01 NS-27337 from the National Institutes of Health/National Institute of Neurological Disorders and Stroke.
    Keywords: Protein kinase ; Postsynaptic density ; Imaging ; Synapse ; LTP long-term potentiation ; EM ; Tissue culture ; Fluorescence
    Repository Name: Woods Hole Open Access Server
    Type: Article
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  • 5
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    Distribution of postsynaptic density (PSD)-95 and Ca2+/calmodulin-dependent protein kinase II at the PSD (2009)
    Society for Neuroscience
    Details
    Publication Date: 2022-05-25
    Description: Author Posting. © Society for Neuroscience, 2003. This article is posted here by permission of Society for Neuroscience for personal use, not for redistribution. The definitive version was published in Journal of Neuroscience 23 (2003): 11270-11278.
    Description: Postsynaptic densities (PSDs) contain proteins that regulate synaptic transmission. We determined the positions of calcium/calmodulin-dependent protein kinase II (CaMKII) and PSD-95 within the three-dimensional structure of isolated PSDs using immunogold labeling, rotary shadowing, and electron microscopic tomography. The results show that all PSDs contain a central mesh immediately underlying the postsynaptic membrane. Label for PSD-95 is found on both the cytoplasmic and cleft sides of this mesh, averaging 12 nm from the cleft side. All PSDs label for PSD-95. The properties of CaMKII labeling are quite different. Label is virtually absent on the cleft sides of PSDs, but can be heavy on the cytoplasmic side at a mean distance of 25 nm from the cleft. In tomograms, CaMKII holoenzymes can be visualized directly, appearing as labeled, tower-like structures reflecting the 20 nm diameter of the holoenzyme. These towers protrude from the cytoplasmic side of the central mesh. There appears to be a local organization of CaMKII, as judged by fact that the nearest-neighbor distances are nearly invariant over a wide range of labeling density for CaMKII. The average density of CaMKII holoenzymes is highly variable, ranging from zero to values approaching a tightly packed state. This variability is significantly higher than that for PSD-95 and is consistent with an information storage role for CaMKII.
    Description: This work was supported by National Institute of Neurological Disorders and Stroke Grants RO1 NS-27337 and RO1 NS-35083 (J.L.).
    Keywords: Postsynaptic density ; CaMKII ; PSD ; PSD-95 ; Electron microscopy ; Tomography
    Repository Name: Woods Hole Open Access Server
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  • 6
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    Palmitoylation regulates glutamate receptor distributions in postsynaptic densities through control of PSD95 conformation and orientation (2016)
    Details
    Publication Date: 2022-05-25
    Description: Author Posting. © The Author(s), 2016. This is the author's version of the work. It is posted here by permission of National Academy of Sciences of the United States of America for personal use, not for redistribution. The definitive version was published in Proceedings of the National Academy of Sciences of the United States of America 113 (2016): E8482-E8491, doi: 10.1073/pnas.1612963113.
    Description: PSD95 and SAP97 are homologous scaffold proteins with different N-terminal domains, possessing either a palmitoylation site (PSD95) or an L27 domain (SAP97). Here, we measured PSD95 and SAP97 conformation in vitro and in postsynaptic densities (PSDs) using FRET and electron microscopy, and examined how conformation regulated interactions with AMPA-type and NMDAtype glutamate receptors (AMPARs/NMDARs). Palmitoylation of PSD95 changed its conformation from a compact to an extended configuration. PSD95 associated with AMPARs (via TARP subunits) or NMDARs (via GluN2B subunits) only in its palmitoylated and extended conformation. In contrast, SAP97 in its extended conformation associates with NMDARs but not with AMPARs. Within PSDs, PSD95 and SAP97 were largely in the extended conformation, but had different orientations. PSD95 oriented perpendicular to the PSD membrane, with its palmitoylated, N-terminal domain at the membrane. SAP97 oriented parallel to the PSD membrane, likely as a dimer through interactions of its N-terminal, L27 domain. Changing PSD95 palmitoylation in PSDs altered PSD95 and AMPAR levels but did not affect NMDAR levels. These results indicate that in PSDs, PSD95 palmitoylation, conformation and its interactions are dynamic when associated with AMPARs, and more stable when associated with NMDARs. Altogether, our results are consistent with differential regulation of PSD95 palmitoylation in PSDs resulting from the clustering of palmitoylating and depalmitoylating enzymes into AMPAR nanodomains segregated away from NMDAR nanodomains.
    Description: This work was supported by the U.S. National Institutes of Health under grant numbers NS043782, MH081251 and DA019695 (WNG) and NINDS intramural funds (TSR). This project was also supported by the National Center for Research Resources and the National Center for Advancing Translational Sciences of the National Institutes of Health through Grant Number UL1 RR024999 (O.J.).
    Description: 2017-06-12
    Repository Name: Woods Hole Open Access Server
    Type: Preprint
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  • 7
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    Placozoan fiber cells: mediators of innate immunity and participants in wound healing (2022)
    Nature Research
    Details
    Publication Date: 2022-05-27
    Description: © The Author(s), 2021. This article is distributed under the terms of the Creative Commons Attribution License. The definitive version was published in Mayorova, T. D., Hammar, K., Jung, J. H., Aronova, M. A., Zhang, G., Winters, C. A., Reese, T. S., & Smith, C. L. Placozoan fiber cells: mediators of innate immunity and participants in wound healing. Scientific Reports, 11(1), (2021): 23343, https://doi.org/10.1038/s41598-021-02735-9.
    Description: Placozoa is a phylum of non-bilaterian marine animals. These small, flat organisms adhere to the substrate via their densely ciliated ventral epithelium, which mediates mucociliary locomotion and nutrient uptake. They have only six morphological cell types, including one, fiber cells, for which functional data is lacking. Fiber cells are non-epithelial cells with multiple processes. We used electron and light microscopic approaches to unravel the roles of fiber cells in Trichoplax adhaerens, a representative member of the phylum. Three-dimensional reconstructions of serial sections of Trichoplax showed that each fiber cell is in contact with several other cells. Examination of fiber cells in thin sections and observations of live dissociated fiber cells demonstrated that they phagocytose cell debris and bacteria. In situ hybridization confirmed that fiber cells express genes involved in phagocytic activity. Fiber cells also are involved in wound healing as evidenced from microsurgery experiments. Based on these observations we conclude that fiber cells are multi-purpose macrophage-like cells. Macrophage-like cells have been described in Porifera, Ctenophora, and Cnidaria and are widespread among Bilateria, but our study is the first to show that Placozoa possesses this cell type. The phylogenetic distribution of macrophage-like cells suggests that they appeared early in metazoan evolution.
    Description: Open Access funding provided by the National Institutes of Health (NIH).
    Repository Name: Woods Hole Open Access Server
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  • 8
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    Envelope structure of Synechococcus sp. WH8113, a nonflagellated swimming cyanobacterium (2005)
    BioMed Central
    Details
    Publication Date: 2022-05-26
    Description: © 2001 Samuel et al; licensee BioMed Central Ltd. This is an Open Access article: verbatim copying and redistribution of this article are permitted in all media for any purpose, provided this notice is preserved along with the article's original URL. The definitive version was published in BMC Microbiology 1 (2001): 4, doi:10.1186/1471-2180-1-4.
    Description: Many bacteria swim by rotating helical flagellar filaments. Waterbury et al. discovered an exception, strains of the cyanobacterium Synechococcus that swim without flagella or visible changes in shape. Other species of cyanobacteria glide on surfaces. The hypothesis that Synechococcus might swim using traveling surface waves prompted this investigation. Results Using quick-freeze electron microscopy, we have identified a crystalline surface layer that encloses the outer membrane of the motile strain Synechococcus sp. WH8113, the components of which are arranged in a rhomboid lattice. Spicules emerge in profusion from the layer and extend up to 150 nm into the surrounding fluid. These spicules also send extensions inwards to the inner cell membrane where motility is powered by an ion-motive force. Conclusion The envelope structure of Synechococcus sp. WH8113 provides new constraints on its motile mechanism. The spicules are well positioned to transduce energy at the cell membrane into mechanical work at the cell surface. One model is that an unidentified motor embedded in the cell membrane utilizes the spicules as oars to generate a traveling wave external to the surface layer in the manner of ciliated eukaryotes.
    Description: ADTS was supported by the Rowland Institute for Science and is an Amgen Fellow of the Life Sciences Research Foundation.
    Keywords: Synechococcus sp. ; Motile mechanism
    Repository Name: Woods Hole Open Access Server
    Type: Article
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  • 9
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    Inhibition of phosphatase activity facilitates the formation and maintenance of NMDA-induced calcium/calmodulin-dependent protein kinase ii clusters in hippocampal neurons (2006)
    Details
    Publication Date: 2022-05-26
    Description: Author Posting. © The Authors, 2004. This is the author's version of the work. It is posted here by permission of Elsevier B. V. for personal use, not for redistribution. The definitive version was published in Neuroscience 130 (2005), doi:10.1016/j.neuroscience.2004.10.008.
    Description: The majority of hippocampal neurons in dissociated cultures and in intact brain exhibit clustering of CaMKII into spherical structures with an average diameter of 110 nm when subjected to conditions that mimic ischemia and excitotoxicity (Tao-Cheng et al., 2001). Because clustering of CaMKII would reduce its effective concentration within the neuron, it may represent a cellular strategy to prevent excessive CaMKII-mediated phosphorylation during episodes of Ca2+ overload. Here we employ a relatively mild excitatory stimulus to promote sub-maximal clustering for the purpose of studying the conditions for the formation and disappearance of CaMKII clusters. Treatment with 30 µM NMDA for 2 min produced CaMKII clustering in ~15 percent of dissociated hippocampal neurons in culture, as observed by pre-embedding immunogold electron microscopy. These CaMKII clusters could be labeled with antibodies specific to the phospho form (Thr286) of CaMKII, suggesting that at least some of the CaMKII molecules in clusters are autophosphorylated. To test whether phosphorylation is involved in the formation and maintenance of CaMKII clusters, the phosphatase inhibitors calyculin A (5 nM) or okadaic acid (1 µM) were included in the incubation medium. With inhibitors more neurons exhibited CaMKII clusters in response to 2 min NMDA treatment. Furthermore, 5 min after the removal of NMDA and Ca2+, CaMKII clusters remained and could still be labeled with the phospho-specific antibody. In contrast, in the absence of phosphatase inhibitors, no clusters were detected 5 min after the removal of NMDA and Ca2+ from the medium. These results suggest that phosphatases type 1 and/or 2A regulate the formation and disappearance of CaMKII clusters.
    Description: Supported by NINDS intramural funds and National Science Foundation grant 9817317 to A. D.
    Keywords: Immunogold electron microscopy ; Calyculin A ; Okadaic acid ; Calcium/calmodulin-dependent protein kinase II ; Autophosphorylation
    Repository Name: Woods Hole Open Access Server
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  • 10
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    Isolation and ultrastructural characterization of squid synaptic vesicles (2011)
    Marine Biological Laboratory
    Details
    Publication Date: 2022-05-26
    Description: Author Posting. © Marine Biological Laboratory, 2011. This article is posted here by permission of Marine Biological Laboratory for personal use, not for redistribution. The definitive version was published in Biological Bulletin 220 (2011): 89-96.
    Description: Synaptic vesicles contain a variety of proteins and lipids that mediate fusion with the pre-synaptic membrane. Although the structures of many synaptic vesicle proteins are known, an overall picture of how they are organized at the vesicle surface is lacking. In this paper, we describe a better method for the isolation of squid synaptic vesicles and characterize the results. For highly pure and intact synaptic vesicles from squid optic lobe, glycerol density gradient centrifugation was the key step. Different electron microscopic methods show that vesicle membrane surfaces are largely covered with structures corresponding to surface proteins. Each vesicle contains several stalked globular structures that extend from the vesicle surface and are consistent with the V-ATPase. BLAST search of a library of squid expressed sequence tags identifies 10 V-ATPase subunits, which are expressed in the squid stellate ganglia. Negative-stain tomography demonstrates directly that vesicles flatten during the drying step of negative staining, and furthermore shows details of individual vesicles and other proteins at the vesicle surface.
    Description: JAD is supported by the RI-INBRE program award # P20RR016457-10 from the National Center for Research Resources (NCRR), NIH.
    Repository Name: Woods Hole Open Access Server
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