ALBERT

All Library Books, journals and Electronic Records Telegrafenberg

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
  • Protein Structure, Tertiary  (129)
  • American Association for the Advancement of Science (AAAS)  (129)
  • 2005-2009  (129)
  • 1955-1959
Collection
Publisher
Years
Year
  • 1
    Publication Date: 2006-09-16
    Description: We report the draft genome of the black cottonwood tree, Populus trichocarpa. Integration of shotgun sequence assembly with genetic mapping enabled chromosome-scale reconstruction of the genome. More than 45,000 putative protein-coding genes were identified. Analysis of the assembled genome revealed a whole-genome duplication event; about 8000 pairs of duplicated genes from that event survived in the Populus genome. A second, older duplication event is indistinguishably coincident with the divergence of the Populus and Arabidopsis lineages. Nucleotide substitution, tandem gene duplication, and gross chromosomal rearrangement appear to proceed substantially more slowly in Populus than in Arabidopsis. Populus has more protein-coding genes than Arabidopsis, ranging on average from 1.4 to 1.6 putative Populus homologs for each Arabidopsis gene. However, the relative frequency of protein domains in the two genomes is similar. Overrepresented exceptions in Populus include genes associated with lignocellulosic wall biosynthesis, meristem development, disease resistance, and metabolite transport.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Tuskan, G A -- Difazio, S -- Jansson, S -- Bohlmann, J -- Grigoriev, I -- Hellsten, U -- Putnam, N -- Ralph, S -- Rombauts, S -- Salamov, A -- Schein, J -- Sterck, L -- Aerts, A -- Bhalerao, R R -- Bhalerao, R P -- Blaudez, D -- Boerjan, W -- Brun, A -- Brunner, A -- Busov, V -- Campbell, M -- Carlson, J -- Chalot, M -- Chapman, J -- Chen, G-L -- Cooper, D -- Coutinho, P M -- Couturier, J -- Covert, S -- Cronk, Q -- Cunningham, R -- Davis, J -- Degroeve, S -- Dejardin, A -- Depamphilis, C -- Detter, J -- Dirks, B -- Dubchak, I -- Duplessis, S -- Ehlting, J -- Ellis, B -- Gendler, K -- Goodstein, D -- Gribskov, M -- Grimwood, J -- Groover, A -- Gunter, L -- Hamberger, B -- Heinze, B -- Helariutta, Y -- Henrissat, B -- Holligan, D -- Holt, R -- Huang, W -- Islam-Faridi, N -- Jones, S -- Jones-Rhoades, M -- Jorgensen, R -- Joshi, C -- Kangasjarvi, J -- Karlsson, J -- Kelleher, C -- Kirkpatrick, R -- Kirst, M -- Kohler, A -- Kalluri, U -- Larimer, F -- Leebens-Mack, J -- Leple, J-C -- Locascio, P -- Lou, Y -- Lucas, S -- Martin, F -- Montanini, B -- Napoli, C -- Nelson, D R -- Nelson, C -- Nieminen, K -- Nilsson, O -- Pereda, V -- Peter, G -- Philippe, R -- Pilate, G -- Poliakov, A -- Razumovskaya, J -- Richardson, P -- Rinaldi, C -- Ritland, K -- Rouze, P -- Ryaboy, D -- Schmutz, J -- Schrader, J -- Segerman, B -- Shin, H -- Siddiqui, A -- Sterky, F -- Terry, A -- Tsai, C-J -- Uberbacher, E -- Unneberg, P -- Vahala, J -- Wall, K -- Wessler, S -- Yang, G -- Yin, T -- Douglas, C -- Marra, M -- Sandberg, G -- Van de Peer, Y -- Rokhsar, D -- New York, N.Y. -- Science. 2006 Sep 15;313(5793):1596-604.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Environmental Sciences Division, Oak Ridge National Laboratory, Oak Ridge, TN 37831, USA. gtk@ornl.gov〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/16973872" target="_blank"〉PubMed〈/a〉
    Keywords: Arabidopsis/genetics ; Chromosome Mapping ; Computational Biology ; Evolution, Molecular ; Expressed Sequence Tags ; *Gene Duplication ; Gene Expression ; Genes, Plant ; *Genome, Plant ; Oligonucleotide Array Sequence Analysis ; Phylogeny ; Plant Proteins/chemistry/genetics ; Polymorphism, Single Nucleotide ; Populus/*genetics/growth & development/metabolism ; Protein Structure, Tertiary ; RNA, Plant/analysis ; RNA, Untranslated/analysis ; *Sequence Analysis, DNA
    Print ISSN: 0036-8075
    Electronic ISSN: 1095-9203
    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
    Location Call Number Expected Availability
    BibTip Others were also interested in ...
  • 2
    Publication Date: 2005-07-05
    Description: We report the genome sequence of Theileria parva, an apicomplexan pathogen causing economic losses to smallholder farmers in Africa. The parasite chromosomes exhibit limited conservation of gene synteny with Plasmodium falciparum, and its plastid-like genome represents the first example where all apicoplast genes are encoded on one DNA strand. We tentatively identify proteins that facilitate parasite segregation during host cell cytokinesis and contribute to persistent infection of transformed host cells. Several biosynthetic pathways are incomplete or absent, suggesting substantial metabolic dependence on the host cell. One protein family that may generate parasite antigenic diversity is not telomere-associated.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Gardner, Malcolm J -- Bishop, Richard -- Shah, Trushar -- de Villiers, Etienne P -- Carlton, Jane M -- Hall, Neil -- Ren, Qinghu -- Paulsen, Ian T -- Pain, Arnab -- Berriman, Matthew -- Wilson, Robert J M -- Sato, Shigeharu -- Ralph, Stuart A -- Mann, David J -- Xiong, Zikai -- Shallom, Shamira J -- Weidman, Janice -- Jiang, Lingxia -- Lynn, Jeffery -- Weaver, Bruce -- Shoaibi, Azadeh -- Domingo, Alexander R -- Wasawo, Delia -- Crabtree, Jonathan -- Wortman, Jennifer R -- Haas, Brian -- Angiuoli, Samuel V -- Creasy, Todd H -- Lu, Charles -- Suh, Bernard -- Silva, Joana C -- Utterback, Teresa R -- Feldblyum, Tamara V -- Pertea, Mihaela -- Allen, Jonathan -- Nierman, William C -- Taracha, Evans L N -- Salzberg, Steven L -- White, Owen R -- Fitzhugh, Henry A -- Morzaria, Subhash -- Venter, J Craig -- Fraser, Claire M -- Nene, Vishvanath -- New York, N.Y. -- Science. 2005 Jul 1;309(5731):134-7.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Institute for Genomic Research (TIGR), 9712 Medical Center Drive, Rockville, MD 20850, USA. gardner@tigr.org〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/15994558" target="_blank"〉PubMed〈/a〉
    Keywords: Algorithms ; Animals ; Antigens, Protozoan/genetics ; Cattle ; Cell Proliferation ; Chromosomes/genetics ; Conserved Sequence ; Enzymes/genetics/metabolism ; Genes, Protozoan ; *Genome, Protozoan ; Lymphocytes/cytology/*parasitology ; Mitochondria/metabolism ; Molecular Sequence Data ; Organelles/genetics/physiology ; Plasmodium falciparum/genetics ; Protein Structure, Tertiary ; Protozoan Proteins/chemistry/*genetics/metabolism ; Sequence Analysis, DNA ; Synteny ; Telomere/genetics ; Theileria parva/*genetics/growth & development/pathogenicity/physiology
    Print ISSN: 0036-8075
    Electronic ISSN: 1095-9203
    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
    Location Call Number Expected Availability
    BibTip Others were also interested in ...
  • 3
    Publication Date: 2005-07-05
    Description: Theileria annulata and T. parva are closely related protozoan parasites that cause lymphoproliferative diseases of cattle. We sequenced the genome of T. annulata and compared it with that of T. parva to understand the mechanisms underlying transformation and tropism. Despite high conservation of gene sequences and synteny, the analysis reveals unequally expanded gene families and species-specific genes. We also identify divergent families of putative secreted polypeptides that may reduce immune recognition, candidate regulators of host-cell transformation, and a Theileria-specific protein domain [frequently associated in Theileria (FAINT)] present in a large number of secreted proteins.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Pain, Arnab -- Renauld, Hubert -- Berriman, Matthew -- Murphy, Lee -- Yeats, Corin A -- Weir, William -- Kerhornou, Arnaud -- Aslett, Martin -- Bishop, Richard -- Bouchier, Christiane -- Cochet, Madeleine -- Coulson, Richard M R -- Cronin, Ann -- de Villiers, Etienne P -- Fraser, Audrey -- Fosker, Nigel -- Gardner, Malcolm -- Goble, Arlette -- Griffiths-Jones, Sam -- Harris, David E -- Katzer, Frank -- Larke, Natasha -- Lord, Angela -- Maser, Pascal -- McKellar, Sue -- Mooney, Paul -- Morton, Fraser -- Nene, Vishvanath -- O'Neil, Susan -- Price, Claire -- Quail, Michael A -- Rabbinowitsch, Ester -- Rawlings, Neil D -- Rutter, Simon -- Saunders, David -- Seeger, Kathy -- Shah, Trushar -- Squares, Robert -- Squares, Steven -- Tivey, Adrian -- Walker, Alan R -- Woodward, John -- Dobbelaere, Dirk A E -- Langsley, Gordon -- Rajandream, Marie-Adele -- McKeever, Declan -- Shiels, Brian -- Tait, Andrew -- Barrell, Bart -- Hall, Neil -- Wellcome Trust/United Kingdom -- New York, N.Y. -- Science. 2005 Jul 1;309(5731):131-3.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Wellcome Trust Sanger Institute, Wellcome Trust Genome Campus, Hinxton, Cambridge CB10 1SA, UK. ap2@sanger.ac.uk〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/15994557" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Motifs ; Animals ; Cattle ; Cell Proliferation ; Chromosome Mapping ; Chromosomes/genetics ; Conserved Sequence ; Genes, Protozoan ; *Genome, Protozoan ; Life Cycle Stages ; Lipid Metabolism ; Lymphocytes/cytology/parasitology ; Molecular Sequence Data ; Multigene Family ; Phylogeny ; Protein Sorting Signals/genetics ; Protein Structure, Tertiary ; Proteome ; Protozoan Proteins/chemistry/*genetics/physiology ; Sequence Analysis, DNA ; Species Specificity ; Synteny ; Telomere/genetics ; Theileria annulata/*genetics/growth & development/immunology/pathogenicity ; Theileria parva/*genetics/growth & development/immunology/pathogenicity
    Print ISSN: 0036-8075
    Electronic ISSN: 1095-9203
    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
    Location Call Number Expected Availability
    BibTip Others were also interested in ...
  • 4
    Publication Date: 2007-12-22
    Description: The guanine nucleotide exchange factor p63RhoGEF is an effector of the heterotrimeric guanine nucleotide-binding protein (G protein) Galphaq and thereby links Galphaq-coupled receptors (GPCRs) to the activation of the small-molecular-weight G protein RhoA. We determined the crystal structure of the Galphaq-p63RhoGEF-RhoA complex, detailing the interactions of Galphaq with the Dbl and pleckstrin homology (DH and PH) domains of p63RhoGEF. These interactions involve the effector-binding site and the C-terminal region of Galphaq and appear to relieve autoinhibition of the catalytic DH domain by the PH domain. Trio, Duet, and p63RhoGEF are shown to constitute a family of Galphaq effectors that appear to activate RhoA both in vitro and in intact cells. We propose that this structure represents the crux of an ancient signal transduction pathway that is expected to be important in an array of physiological processes.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Lutz, Susanne -- Shankaranarayanan, Aruna -- Coco, Cassandra -- Ridilla, Marc -- Nance, Mark R -- Vettel, Christiane -- Baltus, Doris -- Evelyn, Chris R -- Neubig, Richard R -- Wieland, Thomas -- Tesmer, John J G -- HL071818/HL/NHLBI NIH HHS/ -- HL086865/HL/NHLBI NIH HHS/ -- Y1-CO-1020/CO/NCI NIH HHS/ -- Y1-GM-1104/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 2007 Dec 21;318(5858):1923-7.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Institute of Experimental and Clinical Pharmacology and Toxicology, Medical Faculty Mannheim, University of Heidelberg, Maybachstrasse 14, D-68169 Mannheim, Germany.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/18096806" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Binding Sites ; Cell Line ; Crystallography, X-Ray ; GTP-Binding Protein alpha Subunits, Gq-G11/*chemistry/metabolism ; Guanine Nucleotide Exchange Factors/*chemistry/metabolism ; Humans ; Models, Molecular ; Molecular Sequence Data ; Mutagenesis, Site-Directed ; Protein Conformation ; Protein Structure, Secondary ; Protein Structure, Tertiary ; Rho Guanine Nucleotide Exchange Factors ; Signal Transduction ; rhoA GTP-Binding Protein/*chemistry/metabolism
    Print ISSN: 0036-8075
    Electronic ISSN: 1095-9203
    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
    Location Call Number Expected Availability
    BibTip Others were also interested in ...
  • 5
    Publication Date: 2008-12-17
    Description: Dynein motors move various cargos along microtubules within the cytoplasm and power the beating of cilia and flagella. An unusual feature of dynein is that its microtubule-binding domain (MTBD) is separated from its ring-shaped AAA+ adenosine triphosphatase (ATPase) domain by a 15-nanometer coiled-coil stalk. We report the crystal structure of the mouse cytoplasmic dynein MTBD and a portion of the coiled coil, which supports a mechanism by which the ATPase domain and MTBD may communicate through a shift in the heptad registry of the coiled coil. Surprisingly, functional data suggest that the MTBD, and not the ATPase domain, is the main determinant of the direction of dynein motility.〈br /〉〈br /〉〈a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2663340/" 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/PMC2663340/" target="_blank"〉This paper as free author manuscript - peer-reviewed and accepted for publication〈/a〉〈br /〉〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Carter, Andrew P -- Garbarino, Joan E -- Wilson-Kubalek, Elizabeth M -- Shipley, Wesley E -- Cho, Carol -- Milligan, Ronald A -- Vale, Ronald D -- Gibbons, I R -- GM30401-29/GM/NIGMS NIH HHS/ -- GM52468/GM/NIGMS NIH HHS/ -- P01 AR042895/AR/NIAMS NIH HHS/ -- P01 AR042895-15/AR/NIAMS NIH HHS/ -- P01-AR42895/AR/NIAMS NIH HHS/ -- P41 RR-17573/RR/NCRR NIH HHS/ -- R01 GM097312/GM/NIGMS NIH HHS/ -- Howard Hughes Medical Institute/ -- New York, N.Y. -- Science. 2008 Dec 12;322(5908):1691-5. doi: 10.1126/science.1164424.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Howard Hughes Medical Institute and Department of Cellular and Molecular Pharmacology, University of California, San Francisco, CA 94158, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/19074350" target="_blank"〉PubMed〈/a〉
    Keywords: Adenosine Triphosphate/metabolism ; Amino Acid Sequence ; Animals ; Binding Sites ; Crystallization ; Crystallography, X-Ray ; Dimerization ; Dyneins/*chemistry/*metabolism ; Hydrophobic and Hydrophilic Interactions ; Image Processing, Computer-Assisted ; Mice ; Microscopy, Electron ; Microtubules/*metabolism/ultrastructure ; Models, Molecular ; Molecular Sequence Data ; Movement ; Protein Structure, Secondary ; Protein Structure, Tertiary ; Recombinant Fusion Proteins/chemistry/metabolism
    Print ISSN: 0036-8075
    Electronic ISSN: 1095-9203
    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
    Location Call Number Expected Availability
    BibTip Others were also interested in ...
  • 6
    Publication Date: 2008-03-08
    Description: Diffuse large B cell lymphoma (DLBCL) is the most common form of non-Hodgkin's lymphoma. In the least curable (ABC) subtype of DLBCL, survival of the malignant cells is dependent on constitutive activation of the nuclear factor-kappaB (NF-kappaB) signaling pathway. In normal B cells, antigen receptor-induced NF-kappaB activation requires CARD11, a cytoplasmic scaffolding protein. To determine whether CARD11 contributes to tumorigenesis, we sequenced the CARD11 gene in human DLBCL tumors. We detected missense mutations in 7 of 73 ABC DLBCL biopsies (9.6%), all within exons encoding the coiled-coil domain. Experimental introduction of CARD11 coiled-coil domain mutants into lymphoma cell lines resulted in constitutive NF-kappaB activation and enhanced NF-kappaB activity upon antigen receptor stimulation. These results demonstrate that CARD11 is a bona fide oncogenein DLBCL, providing a genetic rationale for the development of pharmacological inhibitors of the CARD11 pathway for DLBCL therapy.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Lenz, Georg -- Davis, R Eric -- Ngo, Vu N -- Lam, Lloyd -- George, Thaddeus C -- Wright, George W -- Dave, Sandeep S -- Zhao, Hong -- Xu, Weihong -- Rosenwald, Andreas -- Ott, German -- Muller-Hermelink, Hans Konrad -- Gascoyne, Randy D -- Connors, Joseph M -- Rimsza, Lisa M -- Campo, Elias -- Jaffe, Elaine S -- Delabie, Jan -- Smeland, Erlend B -- Fisher, Richard I -- Chan, Wing C -- Staudt, Louis M -- UO1-CA84967/CA/NCI NIH HHS/ -- Intramural NIH HHS/ -- New York, N.Y. -- Science. 2008 Mar 21;319(5870):1676-9. doi: 10.1126/science.1153629. Epub 2008 Mar 6.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Metabolism Branch, Division of Cancer Treatment and Diagnosis, Center for Cancer Research, National Cancer Institute, Bethesda, MD 20892, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/18323416" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Apoptosis Regulatory Proteins/chemistry/*genetics/metabolism ; CARD Signaling Adaptor Proteins/chemistry/*genetics/metabolism ; Cell Line, Tumor ; Cytoplasm/metabolism ; Guanylate Cyclase/chemistry/*genetics/metabolism ; Humans ; I-kappa B Kinase/metabolism ; Jurkat Cells ; Lymphoma, Large B-Cell, Diffuse/*genetics ; Molecular Sequence Data ; *Mutation, Missense ; NF-kappa B ; *Oncogenes ; Protein Structure, Tertiary ; Receptors, Antigen, B-Cell/physiology ; Sequence Analysis, DNA
    Print ISSN: 0036-8075
    Electronic ISSN: 1095-9203
    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
    Location Call Number Expected Availability
    BibTip Others were also interested in ...
  • 7
    facet.materialart.
    Unknown
    American Association for the Advancement of Science (AAAS)
    Publication Date: 2009-05-16
    Description: Integrins are transmembrane cell-adhesion molecules that carry signals from the outside to the inside of the cell and vice versa. Like other cell surface receptors, integrins signal in response to ligand binding; however, events within the cell can also regulate the affinity of integrins for ligands. This feature is important in physiological situations such as those in blood, in which cells are always in close proximity to their ligands, yet cell-ligand interactions occur only after integrin activation in response to specific external cues. This review focuses on the mechanisms whereby two key proteins, talin and the kindlins, regulate integrin activation by binding the tails of integrin-beta subunits.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Moser, Markus -- Legate, Kyle R -- Zent, Roy -- Fassler, Reinhard -- DK 69921/DK/NIDDK NIH HHS/ -- DK075594/DK/NIDDK NIH HHS/ -- DK65138/DK/NIDDK NIH HHS/ -- New York, N.Y. -- Science. 2009 May 15;324(5929):895-9. doi: 10.1126/science.1163865.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Max Planck Institute of Biochemistry, 82152 Martinsried, Germany.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/19443776" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; *Cell Adhesion ; Humans ; Integrins/chemistry/*metabolism ; Ligands ; Membrane Proteins/chemistry/*metabolism ; Protein Binding ; Protein Conformation ; Protein Structure, Tertiary ; Signal Transduction ; Talin/chemistry/*metabolism
    Print ISSN: 0036-8075
    Electronic ISSN: 1095-9203
    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
    Location Call Number Expected Availability
    BibTip Others were also interested in ...
  • 8
    Publication Date: 2006-06-17
    Description: Negative-strand RNA viruses condense their genome into a helical nucleoprotein-RNA complex, the nucleocapsid, which is packed into virions and serves as a template for the RNA-dependent RNA polymerase complex. The crystal structure of a recombinant rabies virus nucleoprotein-RNA complex, organized in an undecameric ring, has been determined at 3.5 angstrom resolution. Polymerization of the nucleoprotein is achieved by domain exchange between protomers, with flexible hinges allowing nucleocapsid formation. The two core domains of the nucleoprotein clamp around the RNA at their interface and shield it from the environment. RNA sequestering by nucleoproteins is likely a common mechanism used by negative-strand RNA viruses to protect their genomes from the innate immune response directed against viral RNA in human host cells at certain stages of an infectious cycle.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Albertini, Aurelie A V -- Wernimont, Amy K -- Muziol, Tadeusz -- Ravelli, Raimond B G -- Clapier, Cedric R -- Schoehn, Guy -- Weissenhorn, Winfried -- Ruigrok, Rob W H -- New York, N.Y. -- Science. 2006 Jul 21;313(5785):360-3. Epub 2006 Jun 15.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Institut de Virologie Moleculaire et Structurale, FRE 2854 Universite Joseph Fourier-CNRS, Boite Postale 181, 38042 Grenoble, France.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/16778023" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Crystallography, X-Ray ; DNA-Directed RNA Polymerases/metabolism ; Genome, Viral ; Models, Molecular ; Molecular Sequence Data ; Nucleic Acid Conformation ; Nucleocapsid Proteins/*chemistry/metabolism ; Phosphoproteins/metabolism ; Phosphorylation ; Protein Conformation ; Protein Folding ; Protein Structure, Quaternary ; Protein Structure, Secondary ; Protein Structure, Tertiary ; Protein Subunits/chemistry ; RNA, Viral/*chemistry/genetics/metabolism ; Rabies virus/*chemistry/genetics ; Recombinant Proteins/chemistry ; Ribonucleoproteins/*chemistry
    Print ISSN: 0036-8075
    Electronic ISSN: 1095-9203
    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
    Location Call Number Expected Availability
    BibTip Others were also interested in ...
  • 9
    Publication Date: 2007-08-25
    Description: Proteins containing membrane attack complex/perforin (MACPF) domains play important roles in vertebrate immunity, embryonic development, and neural-cell migration. In vertebrates, the ninth component of complement and perforin form oligomeric pores that lyse bacteria and kill virus-infected cells, respectively. However, the mechanism of MACPF function is unknown. We determined the crystal structure of a bacterial MACPF protein, Plu-MACPF from Photorhabdus luminescens, to 2.0 angstrom resolution. The MACPF domain reveals structural similarity with poreforming cholesterol-dependent cytolysins (CDCs) from Gram-positive bacteria. This suggests that lytic MACPF proteins may use a CDC-like mechanism to form pores and disrupt cell membranes. Sequence similarity between bacterial and vertebrate MACPF domains suggests that the fold of the CDCs, a family of proteins important for bacterial pathogenesis, is probably used by vertebrates for defense against infection.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Rosado, Carlos J -- Buckle, Ashley M -- Law, Ruby H P -- Butcher, Rebecca E -- Kan, Wan-Ting -- Bird, Catherina H -- Ung, Kheng -- Browne, Kylie A -- Baran, Katherine -- Bashtannyk-Puhalovich, Tanya A -- Faux, Noel G -- Wong, Wilson -- Porter, Corrine J -- Pike, Robert N -- Ellisdon, Andrew M -- Pearce, Mary C -- Bottomley, Stephen P -- Emsley, Jonas -- Smith, A Ian -- Rossjohn, Jamie -- Hartland, Elizabeth L -- Voskoboinik, Ilia -- Trapani, Joseph A -- Bird, Phillip I -- Dunstone, Michelle A -- Whisstock, James C -- New York, N.Y. -- Science. 2007 Sep 14;317(5844):1548-51. Epub 2007 Aug 23.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Biochemistry and Molecular Biology, Monash University, Clayton, VIC 3800, Australia.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/17717151" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Motifs ; Amino Acid Sequence ; Animals ; Bacterial Proteins/*chemistry/metabolism ; Complement Membrane Attack Complex/chemistry/metabolism ; Crystallography, X-Ray ; Cytotoxins/chemistry ; Membrane Glycoproteins/chemistry/genetics/metabolism ; Molecular Sequence Data ; Perforin ; Photorhabdus/*chemistry ; Pore Forming Cytotoxic Proteins/chemistry/genetics/metabolism ; *Protein Conformation ; *Protein Folding ; Protein Structure, Secondary ; Protein Structure, Tertiary ; Vertebrates
    Print ISSN: 0036-8075
    Electronic ISSN: 1095-9203
    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
    Location Call Number Expected Availability
    BibTip Others were also interested in ...
  • 10
    Publication Date: 2007-10-20
    Description: Nonhomologous end joining (NHEJ) is a critical DNA double-strand break (DSB) repair pathway required to maintain genome stability. Many prokaryotes possess a minimalist NHEJ apparatus required to repair DSBs during stationary phase, composed of two conserved core proteins, Ku and ligase D (LigD). The crystal structure of Mycobacterium tuberculosis polymerase domain of LigD mediating the synapsis of two noncomplementary DNA ends revealed a variety of interactions, including microhomology base pairing, mismatched and flipped-out bases, and 3' termini forming hairpin-like ends. Biochemical and biophysical studies confirmed that polymerase-induced end synapsis also occurs in solution. We propose that this DNA synaptic structure reflects an intermediate bridging stage of the NHEJ process, before end processing and ligation, with both the polymerase and the DNA sequence playing pivotal roles in determining the sequential order of synapsis and remodeling before end joining.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Brissett, Nigel C -- Pitcher, Robert S -- Juarez, Raquel -- Picher, Angel J -- Green, Andrew J -- Dafforn, Timothy R -- Fox, Gavin C -- Blanco, Luis -- Doherty, Aidan J -- BB/D522746/1/Biotechnology and Biological Sciences Research Council/United Kingdom -- G120/738/Medical Research Council/United Kingdom -- New York, N.Y. -- Science. 2007 Oct 19;318(5849):456-9.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Genome Damage and Stability Centre, University of Sussex, Brighton BN1 9RQ, UK.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/17947582" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Base Sequence ; Crystallography, X-Ray ; DNA Ligases/*chemistry/genetics/metabolism ; *DNA Repair ; DNA, Bacterial/*chemistry/metabolism ; Dimerization ; Models, Molecular ; Molecular Sequence Data ; Mutation ; Mycobacterium tuberculosis/*chemistry/enzymology/genetics/metabolism ; Protein Conformation ; Protein Structure, Tertiary
    Print ISSN: 0036-8075
    Electronic ISSN: 1095-9203
    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
    Location Call Number Expected Availability
    BibTip Others were also interested in ...
Close ⊗
This website uses cookies and the analysis tool Matomo. More information can be found here...