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  • 1
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    An entirely specific type I A-kinase anchoring protein that can sequester two molecules of protein kinase A at mitochondria [Biochemistry] (2011)
    National Academy of Sciences
    Details
    Publication Date: 2011-11-30
    Description: A-kinase anchoring proteins (AKAPs) tether the cAMP-dependent protein kinase (PKA) to intracellular sites where they preferentially phosphorylate target substrates. Most AKAPs exhibit nanomolar affinity for the regulatory (RII) subunit of the type II PKA holoenzyme, whereas dual-specificity anchoring proteins also bind the type I (RI) regulatory subunit of PKA with 10–100-fold lower affinity. A range of cellular, biochemical, biophysical, and genetic approaches comprehensively establish that sphingosine kinase interacting protein (SKIP) is a truly type I-specific AKAP. Mapping studies located anchoring sites between residues 925–949 and 1,140–1,175 of SKIP that bind RI with dissociation constants of 73 and 774 nM, respectively. Molecular modeling and site-directed mutagenesis approaches identify Phe 929 and Tyr 1,151 as RI-selective binding determinants in each anchoring site. SKIP complexes exist in different states of RI-occupancy as single-molecule pull-down photobleaching experiments show that 41 ± 10% of SKIP sequesters two YFP-RI dimers, whereas 59 ± 10% of the anchoring protein binds a single YFP-RI dimer. Imaging, proteomic analysis, and subcellular fractionation experiments reveal that SKIP is enriched at the inner mitochondrial membrane where it associates with a prominent PKA substrate, the coiled-coil helix protein ChChd3.
    Print ISSN: 0027-8424
    Electronic ISSN: 1091-6490
    Topics: Biology , Medicine , Natural Sciences in General
    Published by National Academy of Sciences
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  • 2
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    Systematic evolution of ligands by exponential enrichment: RNA ligands to bacteriophage T4 DNA polymerase (1990)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1990-08-03
    Description: High-affinity nucleic acid ligands for a protein were isolated by a procedure that depends on alternate cycles of ligand selection from pools of variant sequences and amplification of the bound species. Multiple rounds exponentially enrich the population for the highest affinity species that can be clonally isolated and characterized. In particular one eight-base region of an RNA that interacts with the T4 DNA polymerase was chosen and randomized. Two different sequences were selected by this procedure from the calculated pool of 65,536 species. One is the wild-type sequence found in the bacteriophage mRNA; one is varied from wild type at four positions. The binding constants of these two RNA's to T4 DNA polymerase are equivalent. These protocols with minimal modification can yield high-affinity ligands for any protein that binds nucleic acids as part of its function; high-affinity ligands could conceivably be developed for any target molecule.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Tuerk, C -- Gold, L -- GM 19963/GM/NIGMS NIH HHS/ -- GM 28685/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 1990 Aug 3;249(4968):505-10.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Molecular, Cellular, Developmental Biology, University of Colorado, Boulder 80309.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/2200121" target="_blank"〉PubMed〈/a〉
    Keywords: Base Sequence ; *Biological Evolution ; DNA-Directed DNA Polymerase/*metabolism ; Escherichia coli/*enzymology ; *Genes, Viral ; Genetic Techniques ; Ligands ; *Models, Genetic ; Molecular Sequence Data ; Nucleic Acid Conformation ; Polymerase Chain Reaction ; RNA, Messenger/genetics/*metabolism ; RNA, Viral/genetics/*metabolism ; T-Phages/*enzymology ; Transcription, Genetic
    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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    Crystal structure of the T4 regA translational regulator protein at 1.9 A resolution (1995)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1995-05-26
    Description: The translational regulator protein regA is encoded by the T4 bacteriophage and binds to a region of messenger RNA (mRNA) that includes the initiator codon. RegA is unusual in that it represses the translation of about 35 early T4 mRNAs but does not affect nearly 200 other mRNAs. The crystal structure of regA was determined at 1.9 A resolution; the protein was shown to have an alpha-helical core and two regions with antiparallel beta sheets. One of these beta sheets has four antiparallel strands and has some sequence homology to RNP-1 and RNP-2, which are believed to be RNA-binding motifs and are found in a number of known RNA-binding proteins. Structurally guided mutants may help to uncover the basis for this variety of RNA interaction.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Kang, C -- Chan, R -- Berger, I -- Lockshin, C -- Green, L -- Gold, L -- Rich, A -- New York, N.Y. -- Science. 1995 May 26;268(5214):1170-3.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Biology, Massachusetts Institute of Technology, Cambridge 02139, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/7761833" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Bacteriophage T4/*chemistry ; Crystallography, X-Ray ; Models, Molecular ; Molecular Sequence Data ; Protein Structure, Secondary ; RNA-Binding Proteins/*chemistry ; Structure-Activity Relationship ; Viral Proteins/*chemistry
    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
    Electronic Resource
    Electronic Resource
    A pulsed optical–optical double resonance study of the 1 1Πg state of 7Li2 (1990)
    College Park, Md. : American Institute of Physics (AIP)
    The Journal of Chemical Physics 92 (1990), S. 5822-5825 
    Details
    ISSN: 1089-7690
    Source: AIP Digital Archive
    Topics: Physics , Chemistry and Pharmacology
    Notes: The results of an optical–optical double resonance study of the 1 1Πg state of 7Li2 are presented. This completes the observation and characterization of all singlet states of Li2 correlating with the Li(2s)+Li(2p) dissociation limit. Data spanning the first 31 vibrational levels were used to obtain Dunham molecular constants and a Rydberg–Klein–Rees (RKR) potential corresponding to 96% of the estimated potential well. The 1 1Πg state, which lies at Te=21 998.25 cm−1, can be characterized by a limited set of Dunham coefficients with ωe=93.354 cm−1, ωexe =−1.874 cm−1, Be=0.291 89 cm−1, and a dissociation energy De=1422.5±0.3 cm−1. The results are compared with the predictions of recent theoretical treatments.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1063/1.458402
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  • 5
    Electronic Resource
    Electronic Resource
    Faraday rotation of a A 1∑+u–X 1∑+g transition in 6Li2 (1990)
    College Park, Md. : American Institute of Physics (AIP)
    The Journal of Chemical Physics 93 (1990), S. 2957-2958 
    Details
    ISSN: 1089-7690
    Source: AIP Digital Archive
    Topics: Physics , Chemistry and Pharmacology
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1063/1.458881
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  • 6
    Electronic Resource
    Electronic Resource
    Fine structure and Zeeman effect in the b(1)3Πu state of 6Li2 by Doppler-free polarization spectroscopy (1991)
    College Park, Md. : American Institute of Physics (AIP)
    The Journal of Chemical Physics 94 (1991), S. 928-941 
    Details
    ISSN: 1089-7690
    Source: AIP Digital Archive
    Topics: Physics , Chemistry and Pharmacology
    Notes: The fine structure of the b(1)3Πu state of the lithium dimer was observed for the first time and studied using Doppler-free polarization spectroscopy. The triplet state was accessed by excitation of the A 1Σ+u(v=2,J=33)∼b(1)3Πu (v=9,N=32,F1,e) spin–orbit perturbed levels. The remaining two fine structure levels were excited by using the Zeeman interaction to mix levels of different J. Two polarization geometries, π pump and σ pump, were used to study separately different groups of MJ levels in magnetic fields up to 3 kG. An irreducible tensor derivation of the fine structure and Zeeman Hamiltonian matrix in Hund's case (b) symmetrized basis functions was carried out and used to determine the perturbation parameters and the spin–spin and spin–rotation fine structure constants by a fit to the Zeeman splitting pattern. The spin–orbit contribution to the fine structure is too small in the high J states to be found accurately. The electronic spin–orbit coupling perturbation for the interaction between the singlet and triplet states was also determined to be Hel(A∼b)=0.1172±0.0008 cm−1.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1063/1.459983
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  • 7
    Electronic Resource
    Electronic Resource
    Anomalous nuclear spin effects in the laser induced fluorescence from the A 1Σu+ state of 6Li2 (1992)
    College Park, Md. : American Institute of Physics (AIP)
    The Journal of Chemical Physics 97 (1992), S. 4567-4568 
    Details
    ISSN: 1089-7690
    Source: AIP Digital Archive
    Topics: Physics , Chemistry and Pharmacology
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1063/1.463880
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  • 8
    Electronic Resource
    Electronic Resource
    Near infrared two-photon laser spectroscopy of the 2 1Σ+g state of 7Li2 (1991)
    College Park, Md. : American Institute of Physics (AIP)
    The Journal of Chemical Physics 95 (1991), S. 7947-7951 
    Details
    ISSN: 1089-7690
    Source: AIP Digital Archive
    Topics: Physics , Chemistry and Pharmacology
    Notes: The results of a nonresonant near infrared two-photon laser spectroscopic study of the 2 1Σ+g state of 7Li2 are presented. Over 1000 rotationaly resolved 2 1Σ+g←X 1Σ+g transitions spanning 2300 cm−1 of the 2 1Σ+g potential well have been assigned and analyzed. Data from the v'=1 to v'=21 vibrational levels are used to obtain 2 1Σ+g state Dunham molecular constants as well as band-by-band constants. These data are also used to construct a Rydberg–Klein–Rees (RKR) potential which corresponds to 89% of the potential well depth. The results for the lower v' levels are in agreement with the previously determined molecular constants for v'=0 to v'=16 [J. Mol. Spectrosc. 116, 271 (1986)]. For the higher v' levels they reveal the perturbations from the 1 1Πg state. Comparisons with the results of ab initio calculations are made. In the 2 1Σ+g←X 1Σ+g nonresonant two-photon excitation only Q-branch transitions are observed with plane polarized radiation.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1063/1.461323
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  • 9
    Electronic Resource
    Electronic Resource
    Spectroscopic study of the E 1Σ+g "shelf'' state in 7Li2 (1987)
    College Park, Md. : American Institute of Physics (AIP)
    The Journal of Chemical Physics 87 (1987), S. 861-868 
    Details
    ISSN: 1089-7690
    Source: AIP Digital Archive
    Topics: Physics , Chemistry and Pharmacology
    Notes: The E 1Σ+g "shelf '' state of the 7Li2 molecule was investigated using a pulsed optical optical double resonance technique. The measurements cover the vibrational levels in the range 0≤v≤29 including the shelf region around 13≤v≤15. Molecular constants have been determined. Using an inverted perturbation approach, an effective potential energy curve has been generated within the adiabatic approximation whose quantum mechanical energy eigenvalues reproduce all the measured term values to within 0.113 cm−1 for the range 0≤v≤23 and 0≤J≤47.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1063/1.453293
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  • 10
    Electronic Resource
    Electronic Resource
    Posttranscriptional Regulatory Mechanisms in Escherichia Coli (1988)
    Palo Alto, Calif. : Annual Reviews
    Annual Review of Biochemistry 57 (1988), S. 199-233 
    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.57.070188.001215
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