ALBERT

All Library Books, journals and Electronic Records Telegrafenberg

X
feed icon rss

Your email was sent successfully. Check your inbox.

An error occurred while sending the email. Please try again.

Proceed reservation?

Export
  • 1
    facet.materialart.
    Unknown
    Microtubule treadmilling in vivo (1997)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1997-01-10
    Description: In vivo, cytoplasmic microtubules are nucleated and anchored by their minus ends at the centrosome and are believed to turn over by a mechanism termed dynamic instability: depolymerization and repolymerization at their plus ends. In cytoplasmic fragments of fish melanophores, microtubules were shown to detach from their nucleation site and depolymerize from their minus ends. Free microtubules moved toward the periphery by treadmilling-growth at one end and shortening from the opposite end. Frequent release from nucleation sites may be a general property of centrosomes and permit a minus-end mechanism of microtubule turnover and treadmilling.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Rodionov, V I -- Borisy, G G -- GM25062/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 1997 Jan 10;275(5297):215-8.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Laboratory of Molecular Biology, University of Wisconsin, Madison, WI 53706, USA. ggborisy@facstaf.wisc.edu〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8985015" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Cell Membrane/metabolism ; Cells, Cultured ; Centrosome/metabolism ; Cytoplasm/metabolism/ultrastructure ; Fishes ; Kinetics ; Melanophores/ultrastructure ; Microtubules/metabolism/*physiology/ultrastructure ; Movement ; Pigments, Biological/metabolism ; Polymers
    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)
    Location Call Number Expected Availability
    BibTip Others were also interested in ...
    PAPER CURRENT
  • 2
    facet.materialart.
    Unknown
    Cell migration: integrating signals from front to back (2003)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2003-12-06
    Description: Cell migration is a highly integrated multistep process that orchestrates embryonic morphogenesis; contributes to tissue repair and regeneration; and drives disease progression in cancer, mental retardation, atherosclerosis, and arthritis. The migrating cell is highly polarized with complex regulatory pathways that spatially and temporally integrate its component processes. This review describes the mechanisms underlying the major steps of migration and the signaling pathways that regulate them, and outlines recent advances investigating the nature of polarity in migrating cells and the pathways that establish it.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Ridley, Anne J -- Schwartz, Martin A -- Burridge, Keith -- Firtel, Richard A -- Ginsberg, Mark H -- Borisy, Gary -- Parsons, J Thomas -- Horwitz, Alan Rick -- New York, N.Y. -- Science. 2003 Dec 5;302(5651):1704-9.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Ludwig Institute for Cancer Research, Royal Free and University College School of Medicine, London W1W 7BS, UK.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/14657486" target="_blank"〉PubMed〈/a〉
    Keywords: Actin Cytoskeleton/physiology ; Animals ; Cell Adhesion ; *Cell Movement ; Cell Polarity ; Humans ; Integrins/physiology ; Models, Biological ; Proteins/metabolism ; Pseudopodia/physiology ; *Signal Transduction
    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)
    Location Call Number Expected Availability
    BibTip Others were also interested in ...
    PAPER CURRENT
  • 3
    facet.materialart.
    Unknown
    Experimental phenylketonuria: replacement of carboxyl terminal tyrosine by phenylalanine in infant rat brain tubulin (1979)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1979-10-26
    Description: In the brains of newborn rats, about half of the tubulin molecules are modified posttranslationally by the addition of an aromatic amino acid at the carboxyl terminus of the alpha chain. Of the added residues, 96 percent are tyrosine and 4 percent are phenylalanine. After induction of hyperphenylalaninemia, the proportion of tubulin molecules containing carboxyl terminal phenylalanine increases up to eightfold and the pool of tyrosine-containing molecules decreases by an equivalent amount.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Rodriguez, J A -- Borisy, G G -- New York, N.Y. -- Science. 1979 Oct 26;206(4417):463-5.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/574315" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Brain/*metabolism ; Cytoplasm/metabolism ; *Disease Models, Animal ; Humans ; Microtubules/metabolism ; Phenylalanine/*metabolism ; Phenylketonurias/*metabolism ; Protein Binding ; Rats ; Tubulin/*metabolism ; Tyrosine/metabolism
    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)
    Location Call Number Expected Availability
    BibTip Others were also interested in ...
    PAPER CURRENT
  • 4
    facet.materialart.
    Unknown
    Spatial organization of a model 15-member human gut microbiota established in gnotobiotic mice [Microbiology] (2017)
    National Academy of Sciences
    Details
    Publication Date: 2017-10-25
    Description: Knowledge of the spatial organization of the gut microbiota is important for understanding the physical and molecular interactions among its members. These interactions are thought to influence microbial succession, community stability, syntrophic relationships, and resiliency in the face of perturbations. The complexity and dynamism of the gut microbiota pose considerable...
    Print ISSN: 0027-8424
    Electronic ISSN: 1091-6490
    Topics: Biology , Medicine , Natural Sciences in General
    Published by National Academy of Sciences
    Location Call Number Expected Availability
    BibTip Others were also interested in ...
    PAPER CURRENT
  • 5
    Electronic Resource
    Electronic Resource
    Characterization of microtubule assembly in porcine brain extracts by viscometry (1973)
    s.l. : American Chemical Society
    Biochemistry 12 (1973), S. 4282-4289 
    Details
    ISSN: 1520-4995
    Source: ACS Legacy Archives
    Topics: Biology , Chemistry and Pharmacology
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1021/bi00745a037
    Location Call Number Expected Availability
    BibTip Others were also interested in ...
    Paper (German National Licenses)
    Fulltext
  • 6
    Electronic Resource
    Electronic Resource
    Ionic and nucleotide requirements for microtubule polymerization in vitro (1975)
    s.l. : American Chemical Society
    Biochemistry 14 (1975), S. 2996-3005 
    Details
    ISSN: 1520-4995
    Source: ACS Legacy Archives
    Topics: Biology , Chemistry and Pharmacology
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1021/bi00684a032
    Location Call Number Expected Availability
    BibTip Others were also interested in ...
    Paper (German National Licenses)
    Fulltext
  • 7
    Electronic Resource
    Electronic Resource
    Microtubules (1973)
    Palo Alto, Calif. : Annual Reviews
    Annual Review of Biochemistry 42 (1973), S. 507-540 
    Details
    ISSN: 0066-4154
    Source: Annual Reviews Electronic Back Volume Collection 1932-2001ff
    Topics: Chemistry and Pharmacology , Biology
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1146/annurev.bi.42.070173.002451
    Location Call Number Expected Availability
    BibTip Others were also interested in ...
    Paper (German National Licenses)
    Fulltext
  • 8
    Electronic Resource
    Electronic Resource
    PURIFICATION OF TUBULIN AND ASSOCIATED HIGH MOLECULAR WEIGHT PROTEINS FROM PORCINE BRAIN AND CHARACTERIZATION OF MICROTUBULE ASSEMBLY IN VITRO (1975)
    Oxford, UK : Blackwell Publishing Ltd
    Annals of the New York Academy of Sciences 253 (1975), 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.1749-6632.1975.tb19196.x
    Location Call Number Expected Availability
    BibTip Others were also interested in ...
    Paper (German National Licenses)
    Fulltext
  • 9
    Electronic Resource
    Electronic Resource
    The Dynamics of Microtubules in Cultured Cells (2000)
    Springer
    Russian journal of developmental biology 31 (2000), S. 354-361 
    Details
    ISSN: 1608-3326
    Keywords: cultured cells ; microtubules ; dynamic instability ; diffusion
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Medicine
    Notes: Abstract The behavior of microtubules in cultured cells in a cooled matrix after the microinjection of fluorescent tubulin was studied using a frame recording with a digital camcorder. In the cell lamella, the positive ends of individual microtubules extend and shorten at random. The histograms of rate distribution have an almost normal distribution with a mode close to 0. The maximum rate of lengthening and shortening reaches 30 and 50 μm/min, respectively. The positive ends of microtubules in PtK cells were in an equilibrium state, while in murine embryonic fibroblasts and Vero cells, they were usually displaced to the cell edge. Free microtubules were present in the cells of all three cultures. In the epithelial cells, they were numerous and relatively stable, while in the fibroblasts, they occurred rarely and were depolymerized at the proximal end. Free microtubules in PtK cells appeared mostly due to spontaneous assembly in the cytoplasm (not in the relationship with the preexisting microtubules) and, more rarely, due to breakage of long microtubules. Separation of microtubules from the centrosome is a very rare event. Unlike positive ends that were characterized by dynamic instability, negative ends were stable and were sometimes depolymerized. When long microtubules were broken, new negative ends were formed that were, as a rule, stable, while in the lamella of fibroblasts (in murine embryonic fibroblasts and Vero cells), new negative ends were immediately depolymerized: free microtubules existed in these cells no more than 1–2 min. A diffusion model has been proposed where the behavior of microtubule ends is considered as unidimensional diffusion. The coefficient of diffusion of positive ends in the epithelial cells is several times less than in the fibroblasts, thus suggesting a higher rate of tubulin metabolism in the fibroblasts as compared to the epithelium. The results obtained indicate that for the exchange of long microtubules, the dynamic instability is not sufficient. In the fibroblasts, their exchange takes place mostly at the expense of depolymerization of the liberating negative ends, which agrees with the previously proposed conveyer hypothesis of microtubule assembly on the centrosome.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1023/A:1026682930669
    Location Call Number Expected Availability
    BibTip Others were also interested in ...
    Paper (German National Licenses)
    Fulltext
  • 10
    Electronic Resource
    Electronic Resource
    Microtubule assembly: Some possible regulatory mechanisms (1974)
    New York, N.Y. : Wiley-Blackwell
    Journal of Supramolecular Structure 2 (1974), S. 429-450 
    Details
    ISSN: 0091-7419
    Keywords: Life Sciences ; Molecular Cell Biology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Chemistry and Pharmacology , Medicine
    Notes: Microtubule polymerization in vitro was examined using material purified from porcine brain tissue by a reversible temperature dependent assembly procedure, and was characterized by electron microscopy, viscometry, and sedimentation. The reaction was endothermic, colchicine sensitive, and occurred at neutral pH and moderate ionic strength. Divalent cations (calcium, magnesium) were inhibitory at millimolar concentrations, but stimulated polymerization at the micromolar level. Nucleoside triphosphates were required for assembly of purified subunits. As determined by quantitative sedimentation analyses, the reaction was an equilibrium process. Below a critical concentration of tubulin no assembly occurred. Analytical ultracentrifugation studies indicated that tubulin species with sO20, w of 6S and 30S were in equilibrium with each other, and that both were incorporated into microtubules. Electron microscopic analyses suggested that disc (or ring) structures might be intermediates in assembly, and that they were primarily utilized early in the polymerization process. Assembly could be seeded by mixing microtubular fragments from brain or flagella with brain microtubule subunits; depending on conditions of temperature and protein concentration, addition of subunits occurred either with unipolar or biased polar directionality. The possible significance of these properties of the polymerization reaction for control of assembly is discussed.
    Additional Material: 12 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/jss.400020230
    Location Call Number Expected Availability
    BibTip Others were also interested in ...
    Paper (German National Licenses)
    Fulltext
Close ⊗
This website uses cookies and the analysis tool Matomo. More information can be found here...