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
Filter
  • Articles  (83)
  • Kinetics  (83)
  • American Association for the Advancement of Science (AAAS)  (83)
  • American Geophysical Union
  • American Meteorological Society
  • American Physical Society (APS)
  • Public Library of Science
  • Springer
  • Springer Nature
  • Wiley
  • 2010-2014
  • 2000-2004  (29)
  • 1985-1989
  • 1980-1984  (54)
  • 1970-1974
  • 1960-1964
  • 1955-1959
  • 1935-1939
  • 1930-1934
  • 2003  (29)
  • 1984  (20)
  • 1981  (34)
  • Natural Sciences in General  (83)
  • Information Science and Librarianship
  • Philosophy
  • Geosciences
Collection
  • Articles  (83)
Source
Keywords
Publisher
  • American Association for the Advancement of Science (AAAS)  (83)
  • American Geophysical Union
  • American Meteorological Society
  • American Physical Society (APS)
  • Public Library of Science
    • +
Years
  • 2010-2014
  • 2000-2004  (29)
  • 1985-1989
  • 1980-1984  (54)
  • 1970-1974
    • +
Year
Journal
Topic
  • 1
    facet.materialart.
    Unknown
    Development and use of fluorescent protein markers in living cells (2003)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2003-04-05
    Description: The ability to visualize, track, and quantify molecules and events in living cells with high spatial and temporal resolution is essential for understanding biological systems. Only recently has it become feasible to carry out these tasks due to the advent of fluorescent protein technology. Here, we trace the development of highly visible and minimally perturbing fluorescent proteins that, together with updated fluorescent imaging techniques, are providing unprecedented insights into the movement of proteins and their interactions with cellular components in living cells.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Lippincott-Schwartz, Jennifer -- Patterson, George H -- New York, N.Y. -- Science. 2003 Apr 4;300(5616):87-91.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Cell Biology and Metabolism Branch, National Institute of Child Health and Human Development, National Institutes of Health, Bethesda, MD 20892, USA. jlippin@helix.nih.gov〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/12677058" target="_blank"〉PubMed〈/a〉
    Keywords: *Cell Physiological Phenomena ; Diagnostic Imaging/*methods ; Fluorescence ; Fluorescence Recovery After Photobleaching/methods ; Fluorometry/methods ; Green Fluorescent Proteins ; Kinetics ; Light ; *Luminescent Proteins/chemistry/genetics/metabolism ; Microscopy/*methods ; Microscopy, Fluorescence/*methods ; Mutagenesis ; Protein Engineering ; Proteins/*metabolism ; Recombinant Fusion Proteins ; Spectrometry, Fluorescence
    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
    Role of EDEM in the release of misfolded glycoproteins from the calnexin cycle (2003)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2003-03-01
    Description: The mechanisms that determine how folding attempts are interrupted to target folding-incompetent proteins for endoplasmic reticulum-associated degradation (ERAD) are poorly defined. Here the alpha-mannosidase I-like protein EDEM was shown to extract misfolded glycoproteins, but not glycoproteins undergoing productive folding, from the calnexin cycle. EDEM overexpression resulted in faster release of folding-incompetent proteins from the calnexin cycle and earlier onset of degradation, whereas EDEM down-regulation prolonged folding attempts and delayed ERAD. Up-regulation of EDEM during ER stress may promote cell recovery by clearing the calnexin cycle and by accelerating ERAD of terminally misfolded polypeptides.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Molinari, Maurizio -- Calanca, Verena -- Galli, Carmela -- Lucca, Paola -- Paganetti, Paolo -- New York, N.Y. -- Science. 2003 Feb 28;299(5611):1397-400.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Institute for Research in Biomedicine, CH-6500 Bellinzona, Switzerland. Maurizio.molinari@irb.unisi.ch〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/12610306" target="_blank"〉PubMed〈/a〉
    Keywords: Aspartic Acid Endopeptidases/chemistry/*metabolism ; Calnexin/*metabolism ; Cell Line ; Down-Regulation ; Electrophoresis, Polyacrylamide Gel ; Endoplasmic Reticulum/*metabolism ; Glycoproteins/chemistry/*metabolism ; Glycosylation ; Humans ; Kinetics ; Membrane Proteins/*metabolism ; Molecular Weight ; Polysaccharides/metabolism ; Protein Conformation ; Protein Folding ; RNA Interference ; Transfection ; Up-Regulation
    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
    Biophysics. Myosin motors walk the walk (2003)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2003-06-28
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Molloy, Justin E -- Veigel, Claudia -- New York, N.Y. -- Science. 2003 Jun 27;300(5628):2045-6.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Division of Physical Biochemistry, National Institute for Medical Research, The Ridgeway, Mill Hill, London NW7 1AA, UK. jmolloy@nimr.mrc.ac.uk〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/12829773" target="_blank"〉PubMed〈/a〉
    Keywords: Actin Cytoskeleton/*metabolism/ultrastructure ; Actins/metabolism ; Adenosine Triphosphate/metabolism ; Binding Sites ; Fluorescent Dyes/metabolism ; Hydrolysis ; Kinetics ; Microscopy, Fluorescence ; Models, Biological ; Molecular Motor Proteins/chemistry/*metabolism ; Myosin Light Chains/chemistry/metabolism ; Myosin Type V/chemistry/*metabolism ; Protein Structure, Tertiary
    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
    Prevention of transthyretin amyloid disease by changing protein misfolding energetics (2003)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2003-02-01
    Description: Genetic evidence suggests that inhibition of amyloid fibril formation by small molecules should be effective against amyloid diseases. Known amyloid inhibitors appear to function by shifting the aggregation equilibrium away from the amyloid state. Here, we describe a series of transthyretin amyloidosis inhibitors that functioned by increasing the kinetic barrier associated with misfolding, preventing amyloidogenesis by stabilizing the native state. The trans-suppressor mutation, threonine 119 --〉 methionine 119, which is known to ameliorate familial amyloid disease, also functioned through kinetic stabilization, implying that this small-molecule strategy should be effective in treating amyloid diseases.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Hammarstrom, Per -- Wiseman, R Luke -- Powers, Evan T -- Kelly, Jeffery W -- DK 46335/DK/NIDDK NIH HHS/ -- New York, N.Y. -- Science. 2003 Jan 31;299(5607):713-6.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Chemistry and The Skaggs Institute of Chemical Biology, The Scripps Research Institute, 10550 North Torrey Pines Road, La Jolla, CA 92037, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/12560553" target="_blank"〉PubMed〈/a〉
    Keywords: Amyloidosis/metabolism/*prevention & control ; Humans ; Hydrogen-Ion Concentration ; Kinetics ; Prealbumin/*antagonists & inhibitors/*chemistry/genetics/metabolism ; Protein Denaturation ; *Protein Folding ; Protein Structure, Quaternary ; Protein Subunits ; Suppression, Genetic ; Thermodynamics
    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
  • 5
    facet.materialart.
    Unknown
    Selective charging of tRNA isoacceptors explains patterns of codon usage (2003)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2003-06-14
    Description: We modeled how the charged levels of different transfer RNAs (tRNAs) that carry the same amino acid (isoacceptors) respond when this amino acid becomes growth-limiting. The charged levels will approach zero for some isoacceptors (such as tRNA2Leu) and remain high for others (such as tRNA4Leu), as determined by the concentrations of isoacceptors and how often their codons occur in protein synthesis. The theory accounts for (synonymous) codons for the same amino acid that are used in ribosome-mediated transcriptional attenuation, the choices of synonymous codons in trans-translating transfermessenger RNA, and the overrepresentation of rare codons in messenger RNAs for amino acid biosynthetic enzymes.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Elf, Johan -- Nilsson, Daniel -- Tenson, Tanel -- Ehrenberg, Mans -- New York, N.Y. -- Science. 2003 Jun 13;300(5626):1718-22.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Cell and Molecular Biology, Uppsala University, Biomedical Center, Box 596, 751 24 Uppsala, Sweden.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/12805541" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acids/*metabolism ; Amino Acyl-tRNA Synthetases/metabolism ; *Codon ; Escherichia coli/*genetics/growth & development/metabolism ; Escherichia coli Proteins/biosynthesis/genetics ; Frameshifting, Ribosomal ; Gene Expression Regulation, Bacterial ; Kinetics ; Mathematics ; Models, Genetic ; Operon ; *Protein Biosynthesis ; Pyrophosphatases/genetics/metabolism ; RNA, Bacterial/genetics/metabolism ; RNA, Messenger/genetics/metabolism ; RNA, Transfer/genetics/metabolism ; RNA, Transfer, Amino Acyl/genetics/*metabolism ; Ribosomes/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
  • 6
    facet.materialart.
    Unknown
    Phosphadioxirane: a peroxide from an ortho-substituted arylphosphine and singlet dioxygen (2003)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2003-10-11
    Description: We prepared the primary adduct for the reaction of singlet dioxygen (1O2) with an arylphosphine by using the sterically hindered arylphosphine tris(o-methoxyphenyl)phosphine. The resulting phosphadioxirane has a dioxygen molecule triangularly bound to the phosphorus atom. Olefin trapping experiments show that the phosphadioxirane can undergo nonradical oxygen atom-transfer reactions. Under protic conditions, two different intermediates are formed during the reaction of singlet dioxygen with tris(o-methoxyphenyl)phosphine, namely, the corresponding hydroperoxy arylphosphine and a hydroxy phosphorane. Experiments with other arylphosphines possessing different electronic and steric properties demonstrate that the relative stability of the tris(o-methoxyphenyl)phosphadioxirane is due to both steric and electronic effects.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Ho, David G -- Gao, Ruomei -- Celaje, Jeff -- Chung, Ha-Yong -- Selke, Matthias -- GM 08101/GM/NIGMS NIH HHS/ -- GM 64104/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 2003 Oct 10;302(5643):259-62.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Chemistry and Biochemistry, California State University, Los Angeles, Los Angeles, CA 90032, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/14551430" target="_blank"〉PubMed〈/a〉
    Keywords: Chemistry, Physical ; Epoxy Compounds/*chemistry ; Heterocyclic Compounds, 1-Ring/*chemistry ; Kinetics ; Magnetic Resonance Spectroscopy ; Molecular Structure ; Organophosphorus Compounds/*chemistry ; Oxidation-Reduction ; Oxygen/chemistry ; Peroxides/*chemistry ; Phosphines/chemistry ; Phosphorus ; Physicochemical Phenomena ; Singlet Oxygen/chemistry ; Temperature
    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
  • 7
    facet.materialart.
    Unknown
    Myosin V walks hand-over-hand: single fluorophore imaging with 1.5-nm localization (2003)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2003-06-07
    Description: Myosin V is a dimeric molecular motor that moves processively on actin, with the center of mass moving approximately 37 nanometers for each adenosine triphosphate hydrolyzed. We have labeled myosin V with a single fluorophore at different positions in the light-chain domain and measured the step size with a standard deviation of 〈1.5 nanometers, with 0.5-second temporal resolution, and observation times of minutes. The step size alternates between 37 + 2x nm and 37 - 2x, where x is the distance along the direction of motion between the dye and the midpoint between the two heads. These results strongly support a hand-over-hand model of motility, not an inchworm model.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Yildiz, Ahmet -- Forkey, Joseph N -- McKinney, Sean A -- Ha, Taekjip -- Goldman, Yale E -- Selvin, Paul R -- AR26846/AR/NIAMS NIH HHS/ -- AR44420/AR/NIAMS NIH HHS/ -- GM65367/GM/NIGMS NIH HHS/ -- PHS 5 T32 GM08276/PH/PHPPO CDC HHS/ -- R01 GM065367/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 2003 Jun 27;300(5628):2061-5. Epub 2003 Jun 5.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Center for Biophysics and Computational Biology, University of Illinois, Urbana-Champaign, IL 61801, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/12791999" target="_blank"〉PubMed〈/a〉
    Keywords: Actin Cytoskeleton/*metabolism/ultrastructure ; Actins/metabolism ; Adenosine Triphosphate/metabolism ; Binding Sites ; Calmodulin ; Carbocyanines/metabolism ; Catalytic Domain ; Dna ; Fluorescence ; Fluorescent Dyes/metabolism ; Kinetics ; Mathematics ; Microscopy, Fluorescence ; *Models, Biological ; Molecular Motor Proteins/chemistry/*metabolism ; Myosin Light Chains/chemistry/metabolism ; Myosin Type V/chemistry/*metabolism ; Protein Structure, Tertiary ; Rhodamines/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
  • 8
    facet.materialart.
    Unknown
    Comment on "Global biodiversity, biochemical kinetics, and the energetic-equivalence rule" (2003)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2003-01-18
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Storch, David -- New York, N.Y. -- Science. 2003 Jan 17;299(5605):346; author reply 346.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Biodiversity and Macroecology Group, Department of Animal and Plant Sciences, University of Sheffield, Sheffield S10 2TN, UK, and Center for Theoretical Study, Charles University, Jilska 1, 110 00 Prague, Czech Republic. storch@cts.cuni.cz〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/12531999" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Body Constitution ; *Ecosystem ; Kinetics ; *Models, Biological ; Population Density ; Temperature ; Thermodynamics
    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
  • 9
    facet.materialart.
    Unknown
    Crystal structure of the carboxyltransferase domain of acetyl-coenzyme A carboxylase (2003)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2003-03-29
    Description: Acetyl-coenzyme A carboxylases (ACCs) are required for the biosynthesis and oxidation of long-chain fatty acids. They are targets for therapeutics against obesity and diabetes, and several herbicides function by inhibiting their carboxyltransferase (CT) domain. We determined the crystal structure of the free enzyme and the coenzyme A complex of yeast CT at 2.7 angstrom resolution and found that it comprises two domains, both belonging to the crotonase/ClpP superfamily. The active site is at the interface of a dimer. Mutagenesis and kinetic studies reveal the functional roles of conserved residues here. The herbicides target the active site of CT, providing a lead for inhibitor development against human ACCs.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Zhang, Hailong -- Yang, Zhiru -- Shen, Yang -- Tong, Liang -- New York, N.Y. -- Science. 2003 Mar 28;299(5615):2064-7.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Biological Sciences, Columbia University, New York, NY 10027, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/12663926" target="_blank"〉PubMed〈/a〉
    Keywords: Acetyl-CoA Carboxylase/antagonists & inhibitors/*chemistry/genetics/metabolism ; Amino Acid Sequence ; Binding Sites ; Biotin/chemistry/metabolism ; Catalysis ; Coenzyme A/chemistry/metabolism ; Crystallography, X-Ray ; Dimerization ; Enzyme Inhibitors/metabolism/pharmacology ; Hydrogen Bonding ; Kinetics ; Molecular Sequence Data ; Mutagenesis ; Protein Conformation ; Protein Folding ; Protein Structure, Secondary ; Protein Structure, Tertiary ; Pyridines/metabolism/pharmacology ; Saccharomyces cerevisiae/*enzymology
    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
  • 10
    facet.materialart.
    Unknown
    Maintenance of stable heterochromatin domains by dynamic HP1 binding (2003)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2003-02-01
    Description: One function of heterochromatin is the epigenetic silencing by sequestration of genes into transcriptionally repressed nuclear neighborhoods. Heterochromatin protein 1 (HP1) is a major component of heterochromatin and thus is a candidate for establishing and maintaining the transcriptionally repressive heterochromatin structure. Here we demonstrate that maintenance of stable heterochromatin domains in living cells involves the transient binding and dynamic exchange of HP1 from chromatin. HP1 exchange kinetics correlate with the condensation level of chromatin and are dependent on the histone methyltransferase Suv39h. The chromodomain and the chromoshadow domain of HP1 are both required for binding to native chromatin in vivo, but they contribute differentially to binding in euchromatin and heterochromatin. These data argue against HP1 repression of transcription by formation of static, higher order oligomeric networks but support a dynamic competition model, and they demonstrate that heterochromatin is accessible to regulatory factors.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Cheutin, Thierry -- McNairn, Adrian J -- Jenuwein, Thomas -- Gilbert, David M -- Singh, Prim B -- Misteli, Tom -- New York, N.Y. -- Science. 2003 Jan 31;299(5607):721-5.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉National Cancer Institute, National Institutes of Health, Bethesda, MD 20892, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/12560555" target="_blank"〉PubMed〈/a〉
    Keywords: Amanitins/pharmacology ; Animals ; Binding Sites ; CHO Cells ; Cell Nucleus/metabolism ; Cells, Cultured ; Chromosomal Proteins, Non-Histone/*chemistry/genetics/*metabolism ; Cricetinae ; Dimerization ; Euchromatin/metabolism ; Fluorescence Recovery After Photobleaching ; HeLa Cells ; Heterochromatin/*chemistry/*metabolism ; Histones/metabolism ; Humans ; Hydroxamic Acids/pharmacology ; Kinetics ; Methyltransferases/metabolism ; Mice ; Mice, Knockout ; Protein Structure, Tertiary ; Recombinant Fusion Proteins/metabolism ; 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)
    Location Call Number Expected Availability
    BibTip Others were also interested in ...
    PAPER CURRENT
Close ⊗
This website uses cookies and the analysis tool Matomo. More information can be found here...