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  • 1
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    Structural basis for leucine-rich nuclear export signal recognition by CRM1 (2009)
    Nature Publishing Group (NPG)
    Details
    Publication Date: 2009-04-03
    Description: CRM1 (also known as XPO1 and exportin 1) mediates nuclear export of hundreds of proteins through the recognition of the leucine-rich nuclear export signal (LR-NES). Here we present the 2.9 A structure of CRM1 bound to snurportin 1 (SNUPN). Snurportin 1 binds CRM1 in a bipartite manner by means of an amino-terminal LR-NES and its nucleotide-binding domain. The LR-NES is a combined alpha-helical-extended structure that occupies a hydrophobic groove between two CRM1 outer helices. The LR-NES interface explains the consensus hydrophobic pattern, preference for intervening electronegative residues and inhibition by leptomycin B. The second nuclear export signal epitope is a basic surface on the snurportin 1 nucleotide-binding domain, which binds an acidic patch on CRM1 adjacent to the LR-NES site. Multipartite recognition of individually weak nuclear export signal epitopes may be common to CRM1 substrates, enhancing CRM1 binding beyond the generally low affinity LR-NES. Similar energetic construction is also used in multipartite nuclear localization signals to provide broad substrate specificity and rapid evolution in nuclear transport.〈br /〉〈br /〉〈a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3437623/" 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/PMC3437623/" target="_blank"〉This paper as free author manuscript - peer-reviewed and accepted for publication〈/a〉〈br /〉〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Dong, Xiuhua -- Biswas, Anindita -- Suel, Katherine E -- Jackson, Laurie K -- Martinez, Rita -- Gu, Hongmei -- Chook, Yuh Min -- 5-T32-GM008297/GM/NIGMS NIH HHS/ -- R01 GM069909/GM/NIGMS NIH HHS/ -- R01GM069909/GM/NIGMS NIH HHS/ -- R01GM069909-03S1/GM/NIGMS NIH HHS/ -- England -- Nature. 2009 Apr 30;458(7242):1136-41. doi: 10.1038/nature07975. Epub 2009 Apr 1.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Pharmacology, University of Texas Southwestern Medical Center at Dallas, 6001 Forest Park, Dallas, Texas 75390-9041, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/19339969" target="_blank"〉PubMed〈/a〉
    Keywords: Active Transport, Cell Nucleus ; Crystallography, X-Ray ; Epitopes ; Fatty Acids, Unsaturated/pharmacology ; Humans ; Hydrophobic and Hydrophilic Interactions ; Karyopherins/*chemistry/*metabolism ; Leucine/*metabolism ; Models, Molecular ; Nuclear Export Signals/*physiology ; Protein Binding/drug effects ; Protein Conformation ; Receptors, Cytoplasmic and Nuclear/*chemistry/*metabolism ; Structure-Activity Relationship ; Substrate Specificity ; snRNP Core Proteins/chemistry/metabolism
    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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    Crystal structure of a divalent metal ion transporter CorA at 2.9 angstrom resolution (2006)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2006-07-22
    Description: CorA family members are ubiquitously distributed transporters of divalent metal cations and are considered to be the primary Mg2+ transporter of Bacteria and Archaea. We have determined a 2.9 angstrom resolution structure of CorA from Thermotoga maritima that reveals a pentameric cone-shaped protein. Two potential regulatory metal binding sites are found in the N-terminal domain that bind both Mg2+ and Co2+. The structure of CorA supports an efflux system involving dehydration and rehydration of divalent metal ions potentially mediated by a ring of conserved aspartate residues at the cytoplasmic entrance and a carbonyl funnel at the periplasmic side of the pore.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Eshaghi, Said -- Niegowski, Damian -- Kohl, Andreas -- Martinez Molina, Daniel -- Lesley, Scott A -- Nordlund, Par -- New York, N.Y. -- Science. 2006 Jul 21;313(5785):354-7.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Division of Biophysics, Department of Medical Biochemistry and Biophysics, Karolinska Institute, SE-171 77 Stockholm, Sweden. Said.Eshaghi@ki.se〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/16857941" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Bacterial Proteins/*chemistry/metabolism ; Binding Sites ; Cation Transport Proteins/*chemistry/metabolism ; Chlorides/analysis/metabolism ; Cobalt/chemistry/*metabolism ; Crystallography, X-Ray ; Hydrophobic and Hydrophilic Interactions ; Magnesium/chemistry/*metabolism ; Models, Molecular ; Molecular Sequence Data ; Protein Conformation ; Protein Folding ; Protein Structure, Quaternary ; Protein Structure, Secondary ; Protein Structure, Tertiary ; Sequence Alignment ; Thermotoga maritima/*chemistry ; Water/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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  • 3
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    Crystal structure of the malaria vaccine candidate apical membrane antigen 1 (2005)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2005-02-26
    Description: Apical membrane antigen 1 from Plasmodium is a leading malaria vaccine candidate. The protein is essential for host-cell invasion, but its molecular function is unknown. The crystal structure of the three domains comprising the ectoplasmic region of the antigen from P. vivax, solved at 1.8 angstrom resolution, shows that domains I and II belong to the PAN motif, which defines a superfamily of protein folds implicated in receptor binding. We also mapped the epitope of an invasion-inhibitory monoclonal antibody specific for the P. falciparum ortholog and modeled this to the structure. The location of the epitope and current knowledge on structure-function correlations for PAN domains together suggest a receptor-binding role during invasion in which domain II plays a critical part. These results are likely to aid vaccine and drug design.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Pizarro, Juan Carlos -- Vulliez-Le Normand, Brigitte -- Chesne-Seck, Marie-Laure -- Collins, Christine R -- Withers-Martinez, Chrislaine -- Hackett, Fiona -- Blackman, Michael J -- Faber, Bart W -- Remarque, Edmond J -- Kocken, Clemens H M -- Thomas, Alan W -- Bentley, Graham A -- MC_U117532063/Medical Research Council/United Kingdom -- New York, N.Y. -- Science. 2005 Apr 15;308(5720):408-11. Epub 2005 Feb 24.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Unite d'Immunologie Structurale, Centre National de la Recherche Scientifique, URA 2185, Institut Pasteur, 25 rue du Docteur Roux, 75724 Paris, France.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/15731407" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Motifs ; Amino Acid Sequence ; Animals ; Antibodies, Monoclonal/immunology ; Antigens, Protozoan/*chemistry/immunology ; Binding Sites ; Crystallization ; Crystallography, X-Ray ; Epitope Mapping ; Epitopes ; Heparin/metabolism ; Malaria Vaccines ; Membrane Proteins/*chemistry/immunology ; Models, Molecular ; Molecular Sequence Data ; Plasmodium falciparum/chemistry/immunology ; Plasmodium vivax/chemistry/*immunology ; Protein Conformation ; Protein Folding ; Protein Structure, Secondary ; Protein Structure, Tertiary ; Protozoan Proteins/*chemistry/immunology ; Recombinant Proteins/chemistry ; Sequence Alignment
    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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    Los recursos de peces demersales de la Plataforma Continental del Ecuador. Parte uno. Distribución, abundancia y variaciones (2009)
    INP (Ecuador)
    Details
    Publication Date: 2021-05-19
    Description: A survey of demersal fish resources of the Continental Shelf of Ecuador was carried out between October 1980 an July 1985 by the National Fisheries Institute of Ecuador, with British Technical Cooperation. This report deals with the stock assessment part of the work. In the course of seven cruises, 366 valid diurnal hauls were made with a high-opening bottom trawl. The demersal fish resources were estimated by swept area methods and the results are presented. The overall average standing stock of demersal fish was 78 000 t of which 22 000 t was good fish, but 36 000 t were gurnards (Triglidae) and 3 000 t of unusable fish. The main stocks were gurnards, grunts and croakers, sharks and corvinas Cynoscion spp. The southern areas especially the Gulf of Guayaquil had the highest densities of fish (9,6 t.Km-2 or 4,0 t.Km-2 excluding gurnards). There was a massive abundance of the gurnard, Prionotus stephanophys in 1984 and 1985. There was a general decrease and other changes in the demersal stocks due to the effects of the ”El Niño” in 1983.
    Description: Published
    Keywords: Demersal fisheries ; Geographical distribution ; Biomass ; Demersal fisheries ; Geographical distribution ; Abundance ; Biomass
    Repository Name: AquaDocs
    Type: Journal Contribution
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  • 5
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    Los recursos demersales de la Plataforma Continental del Ecuador. Parte dos. Producción potencial y recomendaciones para la utilización del recurso de pesca blanca en el Ecuador (2009)
    INP (Ecuador)
    Details
    Publication Date: 2021-05-19
    Description: The stock estimates obtained during the demersal fish resources survey in 1980-1985 were used to estimate the potential yields of demersal stocks of the Ecuadorian Continental Shelf. The difficulties of predicting yields for multispecies fisheries are discussed and modified version of the Gulland model was adopted. The potential realizable yields for multispecies fisheries are discussed and a modified version of the Gulland model was adopted. The potential realizable yield was calculated to be between 15,000 t and 20,000 t per year, of which 2,000 t is good quality fish, 5,000 t per year of small and medium fish and 8,000 t of gurnards. The majority of these resources are at present being fished at around their optimum levels and any further developments that would increase the fishing effort on demersal resources which are at present being exploited should be approached with caution. The national fisheries, especially the artisanal sector play a valuable role in the country and care should be taken to see that these are not adversely affected.
    Description: Published
    Keywords: Demersal fisheries ; Continental shelves ; Demersal fisheries ; Continental shelves ; Yield predictions ; Exploitation
    Repository Name: AquaDocs
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  • 6
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    Estudios sobre la edad y crecimiento de la Palma Calamus brachysomus (Lockington) (Pisces: Sparidae) en aguas ecuatorianas (2009)
    INP (Ecuador)
    Details
    Publication Date: 2021-05-19
    Description: 342 specimens of sparid Calamus brachysomus ”Palma”, collected during a demersal trawl survey by the R. V. Tohallí in April and May1983, were examined. The different techniques used to prepare scales and otoliths for ageing are described and analysed. The otoliths were determined to be the most reliable for ageing studies; 87% of otoliths were readable. The rings observed were assumed to be annual. The mean lengths at age were used to determine the parameters of the Von Bertalanffy growth formula, giving: Lt=50.13(1-e-0.1473(t+2.0704)). The growth curve obtained must be considered provisional due to possible biases in the interpretation of the otoliths, and also due to those arising from the selectivity of the fishing gear.
    Description: Published
    Keywords: Demersal fisheries ; Growth ; Otoliths ; Age ; Demersal fisheries ; Age ; Growth ; Growth curves ; Otoliths ; Otolith reading
    Repository Name: AquaDocs
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