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
  • Mutation
  • 2010-2014  (29)
  • 2000-2004
  • 1995-1999  (58)
  • 1955-1959
  • 1950-1954
  • 2011  (29)
  • 1998  (36)
  • 1997  (22)
  • 1
    facet.materialart.
    Unknown
    Chronic mucocutaneous candidiasis in humans with inborn errors of interleukin-17 immunity (2011)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2011-02-26
    Description: Chronic mucocutaneous candidiasis disease (CMCD) is characterized by recurrent or persistent infections of the skin, nails, and oral and genital mucosae caused by Candida albicans and, to a lesser extent, Staphylococcus aureus, in patients with no other infectious or autoimmune manifestations. We report two genetic etiologies of CMCD: autosomal recessive deficiency in the cytokine receptor, interleukin-17 receptor A (IL-17RA), and autosomal dominant deficiency of the cytokine interleukin-17F (IL-17F). IL-17RA deficiency is complete, abolishing cellular responses to IL-17A and IL-17F homo- and heterodimers. By contrast, IL-17F deficiency is partial, with mutant IL-17F-containing homo- and heterodimers displaying impaired, but not abolished, activity. These experiments of nature indicate that human IL-17A and IL-17F are essential for mucocutaneous immunity against C. albicans, but otherwise largely redundant.〈br /〉〈br /〉〈a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3070042/" 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/PMC3070042/" target="_blank"〉This paper as free author manuscript - peer-reviewed and accepted for publication〈/a〉〈br /〉〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Puel, Anne -- Cypowyj, Sophie -- Bustamante, Jacinta -- Wright, Jill F -- Liu, Luyan -- Lim, Hye Kyung -- Migaud, Melanie -- Israel, Laura -- Chrabieh, Maya -- Audry, Magali -- Gumbleton, Matthew -- Toulon, Antoine -- Bodemer, Christine -- El-Baghdadi, Jamila -- Whitters, Matthew -- Paradis, Theresa -- Brooks, Jonathan -- Collins, Mary -- Wolfman, Neil M -- Al-Muhsen, Saleh -- Galicchio, Miguel -- Abel, Laurent -- Picard, Capucine -- Casanova, Jean-Laurent -- 5UL1RR024143-04/RR/NCRR NIH HHS/ -- UL1 RR024143/RR/NCRR NIH HHS/ -- UL1 RR024143-04/RR/NCRR NIH HHS/ -- New York, N.Y. -- Science. 2011 Apr 1;332(6025):65-8. doi: 10.1126/science.1200439. Epub 2011 Feb 24.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Laboratory of Human Genetics of Infectious Diseases, Necker Branch, Institut National de la Sante et de la Recherche Medicale, U980, and University Paris Descartes, Necker Medical School, 75015 Paris, France. anne.puel@inserm.fr〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/21350122" target="_blank"〉PubMed〈/a〉
    Keywords: Candida albicans ; Candidiasis, Chronic Mucocutaneous/*genetics/*immunology ; Child ; Child, Preschool ; Female ; Genes, Dominant ; Genes, Recessive ; Humans ; Interleukin-17/*immunology ; Male ; Molecular Sequence Data ; Mutation ; Pedigree ; Receptors, Interleukin-17/genetics ; Signal Transduction/genetics ; Th17 Cells/immunology
    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
    Positional cloning of the gene for multiple endocrine neoplasia-type 1 (1997)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1997-04-18
    Description: Multiple endocrine neoplasia-type 1 (MEN1) is an autosomal dominant familial cancer syndrome characterized by tumors in parathyroids, enteropancreatic endocrine tissues, and the anterior pituitary. DNA sequencing from a previously identified minimal interval on chromosome 11q13 identified several candidate genes, one of which contained 12 different frameshift, nonsense, missense, and in-frame deletion mutations in 14 probands from 15 families. The MEN1 gene contains 10 exons and encodes a ubiquitously expressed 2.8-kilobase transcript. The predicted 610-amino acid protein product, termed menin, exhibits no apparent similarities to any previously known proteins. The identification of MEN1 will enable improved understanding of the mechanism of endocrine tumorigenesis and should facilitate early diagnosis.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Chandrasekharappa, S C -- Guru, S C -- Manickam, P -- Olufemi, S E -- Collins, F S -- Emmert-Buck, M R -- Debelenko, L V -- Zhuang, Z -- Lubensky, I A -- Liotta, L A -- Crabtree, J S -- Wang, Y -- Roe, B A -- Weisemann, J -- Boguski, M S -- Agarwal, S K -- Kester, M B -- Kim, Y S -- Heppner, C -- Dong, Q -- Spiegel, A M -- Burns, A L -- Marx, S J -- New York, N.Y. -- Science. 1997 Apr 18;276(5311):404-7.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Laboratory of Gene Transfer, National Human Genome Research Institute (NHGRI), National Institutes of Health (NIH), Bethesda, MD 20892, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/9103196" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Chromosome Mapping ; Chromosomes, Human, Pair 11 ; *Cloning, Molecular ; DNA, Complementary/genetics ; Exons ; Frameshift Mutation ; *Genes, Tumor Suppressor ; Humans ; Molecular Sequence Data ; Multiple Endocrine Neoplasia Type 1/*genetics ; Mutation ; Neoplasm Proteins/chemistry/*genetics ; *Proto-Oncogene Proteins
    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
    Structural basis of type II topoisomerase inhibition by the anticancer drug etoposide (2011)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2011-07-23
    Description: Type II topoisomerases (TOP2s) resolve the topological problems of DNA by transiently cleaving both strands of a DNA duplex to form a cleavage complex through which another DNA segment can be transported. Several widely prescribed anticancer drugs increase the population of TOP2 cleavage complex, which leads to TOP2-mediated chromosome DNA breakage and death of cancer cells. We present the crystal structure of a large fragment of human TOP2beta complexed to DNA and to the anticancer drug etoposide to reveal structural details of drug-induced stabilization of a cleavage complex. The interplay between the protein, the DNA, and the drug explains the structure-activity relations of etoposide derivatives and the molecular basis of drug-resistant mutations. The analysis of protein-drug interactions provides information applicable for developing an isoform-specific TOP2-targeting strategy.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Wu, Chyuan-Chuan -- Li, Tsai-Kun -- Farh, Lynn -- Lin, Li-Ying -- Lin, Te-Sheng -- Yu, Yu-Jen -- Yen, Tien-Jui -- Chiang, Chia-Wang -- Chan, Nei-Li -- New York, N.Y. -- Science. 2011 Jul 22;333(6041):459-62. doi: 10.1126/science.1204117.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Institute of Biochemistry and Molecular Biology, College of Medicine, National Taiwan University, Taipei City 100, Taiwan.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/21778401" target="_blank"〉PubMed〈/a〉
    Keywords: Base Pairing ; Catalytic Domain ; Crystallography, X-Ray ; DNA/*chemistry/metabolism ; DNA Topoisomerases, Type II/*chemistry/genetics/metabolism ; DNA-Binding Proteins/*chemistry/genetics/metabolism ; Drug Resistance, Neoplasm ; Etoposide/analogs & derivatives/*chemistry/metabolism/*pharmacology ; Humans ; Models, Molecular ; Mutant Proteins/chemistry/metabolism ; Mutation ; Protein Multimerization ; Protein Structure, Quaternary ; Protein Structure, Tertiary ; Structure-Activity Relationship ; Topoisomerase II Inhibitors/*chemistry/metabolism/*pharmacology
    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
    Budding yeast Cdc20: a target of the spindle checkpoint (1998)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1998-03-07
    Description: The spindle checkpoint regulates the cell division cycle by keeping cells with defective spindles from leaving mitosis. In the two-hybrid system, three proteins that are components of the checkpoint, Mad1, Mad2, and Mad3, were shown to interact with Cdc20, a protein required for exit from mitosis. Mad2 and Mad3 coprecipitated with Cdc20 at all stages of the cell cycle. The binding of Mad2 depended on Mad1 and that of Mad3 on Mad1 and Mad2. Overexpression of Cdc20 allowed cells with a depolymerized spindle or damaged DNA to leave mitosis but did not overcome the arrest caused by unreplicated DNA. Mutants in Cdc20 that were resistant to the spindle checkpoint no longer bound Mad proteins, suggesting that Cdc20 is the target of the spindle checkpoint.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Hwang, L H -- Lau, L F -- Smith, D L -- Mistrot, C A -- Hardwick, K G -- Hwang, E S -- Amon, A -- Murray, A W -- New York, N.Y. -- Science. 1998 Feb 13;279(5353):1041-4.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Physiology, University of California at San Francisco, San Francisco, CA 94143-0444, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/9461437" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Anaphase ; Anaphase-Promoting Complex-Cyclosome ; Cadherins ; Calcium-Binding Proteins/metabolism ; *Carrier Proteins ; Cdc20 Proteins ; Cdh1 Proteins ; Cell Cycle Proteins/chemistry/genetics/*metabolism ; DNA Damage ; DNA Replication ; Fungal Proteins/chemistry/*metabolism ; Ligases/metabolism ; Mad2 Proteins ; *Mitosis ; Molecular Sequence Data ; Mutation ; Nuclear Proteins/metabolism ; Phosphoproteins/metabolism ; *Repressor Proteins ; Saccharomyces cerevisiae/*cytology/*metabolism ; *Saccharomyces cerevisiae Proteins ; Spindle Apparatus/*metabolism ; *Ubiquitin-Protein Ligase Complexes ; Ubiquitin-Protein Ligases
    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
    DCC constrains tumour progression via its dependence receptor activity (2011)
    Nature Publishing Group (NPG)
    Details
    Publication Date: 2011-12-14
    Description: The role of deleted in colorectal carcinoma (DCC) as a tumour suppressor has been a matter of debate for the past 15 years. DCC gene expression is lost or markedly reduced in the majority of advanced colorectal cancers and, by functioning as a dependence receptor, DCC has been shown to induce apoptosis unless engaged by its ligand, netrin-1 (ref. 2). However, so far no animal model has supported the view that the DCC loss-of-function is causally implicated as predisposing to aggressive cancer development. To investigate the role of DCC-induced apoptosis in the control of tumour progression, here we created a mouse model in which the pro-apoptotic activity of DCC is genetically silenced. Although the loss of DCC-induced apoptosis in this mouse model is not associated with a major disorganization of the intestines, it leads to spontaneous intestinal neoplasia at a relatively low frequency. Loss of DCC-induced apoptosis is also associated with an increase in the number and aggressiveness of intestinal tumours in a predisposing APC mutant context, resulting in the development of highly invasive adenocarcinomas. These results demonstrate that DCC functions as a tumour suppressor via its ability to trigger tumour cell apoptosis.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Castets, Marie -- Broutier, Laura -- Molin, Yann -- Brevet, Marie -- Chazot, Guillaume -- Gadot, Nicolas -- Paquet, Armelle -- Mazelin, Laetitia -- Jarrosson-Wuilleme, Loraine -- Scoazec, Jean-Yves -- Bernet, Agnes -- Mehlen, Patrick -- England -- Nature. 2011 Dec 11;482(7386):534-7. doi: 10.1038/nature10708.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Apoptosis, Cancer and Development Laboratory - Equipe labellisee La Ligue, LabEx DEVweCAN, Centre de Cancerologie de Lyon, INSERM U1052-CNRS UMR5286, Universite de Lyon, Centre Leon Berard, 69008 Lyon, France.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/22158121" target="_blank"〉PubMed〈/a〉
    Keywords: Adenocarcinoma/genetics/pathology ; Animals ; Apoptosis/genetics ; Caspases/metabolism ; Cells, Cultured ; Disease Models, Animal ; *Disease Progression ; Fibroblasts ; Gene Silencing ; Genes, APC ; HEK293 Cells ; Humans ; Intestinal Neoplasms/*genetics/metabolism/*pathology ; Mice ; Mutant Proteins/genetics/metabolism ; Mutation ; Nerve Growth Factors/deficiency/genetics ; Receptors, Cell Surface/deficiency/genetics/*metabolism ; Tumor Suppressor Proteins/deficiency/genetics/*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)
    Location Call Number Expected Availability
    BibTip Others were also interested in ...
    PAPER CURRENT
  • 6
    facet.materialart.
    Unknown
    Evolution of a new enzyme for carbon disulphide conversion by an acidothermophilic archaeon (2011)
    Nature Publishing Group (NPG)
    Details
    Publication Date: 2011-10-21
    Description: Extremophilic organisms require specialized enzymes for their exotic metabolisms. Acid-loving thermophilic Archaea that live in the mudpots of volcanic solfataras obtain their energy from reduced sulphur compounds such as hydrogen sulphide (H(2)S) and carbon disulphide (CS(2)). The oxidation of these compounds into sulphuric acid creates the extremely acidic environment that characterizes solfataras. The hyperthermophilic Acidianus strain A1-3, which was isolated from the fumarolic, ancient sauna building at the Solfatara volcano (Naples, Italy), was shown to rapidly convert CS(2) into H(2)S and carbon dioxide (CO(2)), but nothing has been known about the modes of action and the evolution of the enzyme(s) involved. Here we describe the structure, the proposed mechanism and evolution of a CS(2) hydrolase from Acidianus A1-3. The enzyme monomer displays a typical beta-carbonic anhydrase fold and active site, yet CO(2) is not one of its substrates. Owing to large carboxy- and amino-terminal arms, an unusual hexadecameric catenane oligomer has evolved. This structure results in the blocking of the entrance to the active site that is found in canonical beta-carbonic anhydrases and the formation of a single 15-A-long, highly hydrophobic tunnel that functions as a specificity filter. The tunnel determines the enzyme's substrate specificity for CS(2), which is hydrophobic. The transposon sequences that surround the gene encoding this CS(2) hydrolase point to horizontal gene transfer as a mechanism for its acquisition during evolution. Our results show how the ancient beta-carbonic anhydrase, which is central to global carbon metabolism, was transformed by divergent evolution into a crucial enzyme in CS(2) metabolism.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Smeulders, Marjan J -- Barends, Thomas R M -- Pol, Arjan -- Scherer, Anna -- Zandvoort, Marcel H -- Udvarhelyi, Aniko -- Khadem, Ahmad F -- Menzel, Andreas -- Hermans, John -- Shoeman, Robert L -- Wessels, Hans J C T -- van den Heuvel, Lambert P -- Russ, Lina -- Schlichting, Ilme -- Jetten, Mike S M -- Op den Camp, Huub J M -- England -- Nature. 2011 Oct 19;478(7369):412-6. doi: 10.1038/nature10464.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Microbiology, Radboud University Nijmegen, Heyendaalseweg 135, 6525 AJ, Nijmegen, The Netherlands.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/22012399" target="_blank"〉PubMed〈/a〉
    Keywords: Acidianus/classification/*enzymology/genetics ; Carbon Disulfide/*metabolism ; Catalytic Domain ; Crystallography, X-Ray ; *Evolution, Molecular ; Hydrolases/chemistry/*genetics ; Models, Molecular ; Molecular Sequence Data ; Mutation ; Phylogeny ; Protein Structure, Tertiary
    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)
    Location Call Number Expected Availability
    BibTip Others were also interested in ...
    PAPER CURRENT
  • 7
    facet.materialart.
    Unknown
    A highly conserved neutralizing epitope on group 2 influenza A viruses (2011)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2011-07-09
    Description: Current flu vaccines provide only limited coverage against seasonal strains of influenza viruses. The identification of V(H)1-69 antibodies that broadly neutralize almost all influenza A group 1 viruses constituted a breakthrough in the influenza field. Here, we report the isolation and characterization of a human monoclonal antibody CR8020 with broad neutralizing activity against most group 2 viruses, including H3N2 and H7N7, which cause severe human infection. The crystal structure of Fab CR8020 with the 1968 pandemic H3 hemagglutinin (HA) reveals a highly conserved epitope in the HA stalk distinct from the epitope recognized by the V(H)1-69 group 1 antibodies. Thus, a cocktail of two antibodies may be sufficient to neutralize most influenza A subtypes and, hence, enable development of a universal flu vaccine and broad-spectrum antibody therapies.〈br /〉〈br /〉〈a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3210727/" 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/PMC3210727/" target="_blank"〉This paper as free author manuscript - peer-reviewed and accepted for publication〈/a〉〈br /〉〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Ekiert, Damian C -- Friesen, Robert H E -- Bhabha, Gira -- Kwaks, Ted -- Jongeneelen, Mandy -- Yu, Wenli -- Ophorst, Carla -- Cox, Freek -- Korse, Hans J W M -- Brandenburg, Boerries -- Vogels, Ronald -- Brakenhoff, Just P J -- Kompier, Ronald -- Koldijk, Martin H -- Cornelissen, Lisette A H M -- Poon, Leo L M -- Peiris, Malik -- Koudstaal, Wouter -- Wilson, Ian A -- Goudsmit, Jaap -- GM080209/GM/NIGMS NIH HHS/ -- HHSN272200900060C/PHS HHS/ -- T32 GM080209/GM/NIGMS NIH HHS/ -- T32 GM080209-03/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 2011 Aug 12;333(6044):843-50. doi: 10.1126/science.1204839. Epub 2011 Jul 7.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Molecular Biology, 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/21737702" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Antibodies, Monoclonal/*immunology/isolation & purification ; Antibodies, Neutralizing/*immunology/isolation & purification ; Antibodies, Viral/*immunology/isolation & purification ; Antibody Specificity ; Antigens, Viral/chemistry/genetics/*immunology ; Binding Sites, Antibody ; Conserved Sequence ; Crystallography, X-Ray ; Epitopes/immunology ; Hemagglutinin Glycoproteins, Influenza Virus/chemistry/genetics/*immunology ; Humans ; Influenza A Virus, H3N2 Subtype/immunology ; Influenza A Virus, H7N7 Subtype/genetics/immunology ; Influenza A virus/*immunology ; Influenza Vaccines/immunology ; Influenza, Human/immunology/prevention & control/therapy ; Mice ; Models, Molecular ; Molecular Sequence Data ; Mutation ; Neutralization Tests ; Orthomyxoviridae Infections/immunology/prevention & control ; Protein Conformation
    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
    Structural basis of plasticity in T cell receptor recognition of a self peptide-MHC antigen (1998)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1998-03-21
    Description: The T cell receptor (TCR) inherently has dual specificity. T cells must recognize self-antigens in the thymus during maturation and then discriminate between foreign pathogens in the periphery. A molecular basis for this cross-reactivity is elucidated by the crystal structure of the alloreactive 2C TCR bound to self peptide-major histocompatibility complex (pMHC) antigen H-2Kb-dEV8 refined against anisotropic 3.0 angstrom resolution x-ray data. The interface between peptide and TCR exhibits extremely poor shape complementarity, and the TCR beta chain complementarity-determining region 3 (CDR3) has minimal interaction with the dEV8 peptide. Large conformational changes in three of the TCR CDR loops are induced upon binding, providing a mechanism of structural plasticity to accommodate a variety of different peptide antigens. Extensive TCR interaction with the pMHC alpha helices suggests a generalized orientation that is mediated by the Valpha domain of the TCR and rationalizes how TCRs can effectively "scan" different peptides bound within a large, low-affinity MHC structural framework for those that provide the slight additional kinetic stabilization required for signaling.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Garcia, K C -- Degano, M -- Pease, L R -- Huang, M -- Peterson, P A -- Teyton, L -- Wilson, I A -- AI42266/AI/NIAID NIH HHS/ -- AI42267/AI/NIAID NIH HHS/ -- R01 CA58896/CA/NCI NIH HHS/ -- New York, N.Y. -- Science. 1998 Feb 20;279(5354):1166-72.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Molecular Biology 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/9469799" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Crystallization ; Crystallography, X-Ray ; H-2 Antigens/*chemistry/*immunology/metabolism ; Ligands ; Mice ; Mice, Transgenic ; Models, Molecular ; Mutation ; Oligopeptides/*chemistry/immunology/metabolism ; Protein Conformation ; Protein Structure, Secondary ; Receptors, Antigen, T-Cell, alpha-beta/*chemistry/*immunology/metabolism ; Recombinant Proteins
    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
    An essential role for ectodomain shedding in mammalian development (1998)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1998-11-13
    Description: The ectodomains of numerous proteins are released from cells by proteolysis to yield soluble intercellular regulators. The responsible protease, tumor necrosis factor-alpha converting enzyme (TACE), has been identified only in the case when tumor necrosis factor-alpha (TNFalpha) is released. Analyses of cells lacking this metalloproteinase-disintegrin revealed an expanded role for TACE in the processing of other cell surface proteins, including a TNF receptor, the L-selectin adhesion molecule, and transforming growth factor-alpha (TGFalpha). The phenotype of mice lacking TACE suggests an essential role for soluble TGFalpha in normal development and emphasizes the importance of protein ectodomain shedding in vivo.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Peschon, J J -- Slack, J L -- Reddy, P -- Stocking, K L -- Sunnarborg, S W -- Lee, D C -- Russell, W E -- Castner, B J -- Johnson, R S -- Fitzner, J N -- Boyce, R W -- Nelson, N -- Kozlosky, C J -- Wolfson, M F -- Rauch, C T -- Cerretti, D P -- Paxton, R J -- March, C J -- Black, R A -- CA43793/CA/NCI NIH HHS/ -- DK53804/DK/NIDDK NIH HHS/ -- New York, N.Y. -- Science. 1998 Nov 13;282(5392):1281-4.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Immunex Corporation, Seattle, WA 98101, USA. peschon@immunex.com〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/9812885" target="_blank"〉PubMed〈/a〉
    Keywords: ADAM Proteins ; Amino Acid Sequence ; Animals ; Catalytic Domain ; Cell Membrane/*metabolism ; Cells, Cultured ; Crosses, Genetic ; *Embryonic and Fetal Development ; L-Selectin/metabolism ; Ligands ; Membrane Proteins/*metabolism ; Metalloendopeptidases/chemistry/genetics/*metabolism ; Mice ; Mice, Inbred C57BL ; Molecular Sequence Data ; Mutation ; Phenotype ; Protein Processing, Post-Translational ; Receptors, Tumor Necrosis Factor/metabolism ; Transforming Growth Factor alpha/metabolism ; Tumor Necrosis Factor-alpha/*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
  • 10
    facet.materialart.
    Unknown
    Regulation of meiotic S phase by Ime2 and a Clb5,6-associated kinase in Saccharomyces cerevisiae (1998)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1998-09-22
    Description: Cyclin-dependent kinase (Cdk) mutations that prevent entry into the mitotic cell cycle of budding yeast fail to block meiotic DNA replication, suggesting there may be fundamental differences between these pathways. However, S phase in meiosis was found to depend on the same B-type cyclins (Clb5 and Clb6) as it does in mitosis. Meiosis differs instead in the mechanism that controls removal of the Cdk inhibitor Sic1. Destruction of Sic1 and activation of a Clb5-dependent kinase in meiotic cells required the action of the meiosis-specific protein kinase Ime2, thereby coupling early meiotic gene expression to control of DNA replication for meiosis.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Dirick, L -- Goetsch, L -- Ammerer, G -- Byers, B -- GM 18541/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 1998 Sep 18;281(5384):1854-7.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Genetics, Box 357360, University of Washington, Seattle, WA 98195-7360, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/9743499" target="_blank"〉PubMed〈/a〉
    Keywords: CDC28 Protein Kinase, S cerevisiae/metabolism ; *Cell Cycle Proteins ; *Cyclin B ; Cyclin-Dependent Kinase Inhibitor Proteins ; Cyclin-Dependent Kinases/*metabolism ; Cyclins/genetics/*metabolism ; DNA Replication ; Enzyme Inhibitors/metabolism ; Fungal Proteins/genetics/*metabolism ; Genes, Fungal ; Intracellular Signaling Peptides and Proteins ; *Meiosis ; Mutation ; Protein Kinases/genetics/*metabolism ; Protein-Serine-Threonine Kinases ; *S Phase ; Saccharomyces cerevisiae/*cytology/genetics/metabolism ; *Saccharomyces cerevisiae Proteins
    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...