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  • 1
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    Crystal structure of mouse CD1: An MHC-like fold with a large hydrophobic binding groove (1997)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1997-07-18
    Description: CD1 represents a third lineage of antigen-presenting molecules that are distantly related to major histocompatibility complex (MHC) molecules in the immune system. The crystal structure of mouse CD1d1, corresponding to human CD1d, at 2.8 resolution shows that CD1 adopts an MHC fold that is more closely related to that of MHC class I than to that of MHC class II. The binding groove, although significantly narrower, is substantially larger because of increased depth and it has only two major pockets that are almost completely hydrophobic. The extreme hydrophobicity and shape of the binding site are consistent with observations that human CD1b and CD1c can present mycobacterial cell wall antigens, such as mycolic acid and lipoarabinomannans. However, mouse CD1d1 can present very hydrophobic peptides, but must do so in a very different way from MHC class Ia and class II molecules.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Zeng, Z -- Castano, A R -- Segelke, B W -- Stura, E A -- Peterson, P A -- Wilson, I A -- CA-58896/CA/NCI NIH HHS/ -- New York, N.Y. -- Science. 1997 Jul 18;277(5324):339-45.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Molecular Biology and the Skaggs Institute for Chemical Biology at the Scripps Research Institute, La Jolla, CA 92037, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/9219685" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; *Antigen Presentation ; Antigens, CD1/*chemistry/immunology/metabolism ; Binding Sites ; Crystallization ; Crystallography, X-Ray ; Glycolipids/chemistry/immunology/metabolism ; Histocompatibility Antigens Class I/chemistry ; Histocompatibility Antigens Class II/chemistry ; Humans ; Hydrogen Bonding ; Ligands ; Lipid Metabolism ; Lipids/chemistry/immunology ; Mice ; Models, Molecular ; *Protein Conformation ; *Protein Folding ; Protein Structure, Secondary ; Protein Structure, Tertiary ; T-Lymphocyte Subsets/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)
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  • 2
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    Arthropod diversity in a tropical forest (2012)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2012-12-15
    Description: Most eukaryotic organisms are arthropods. Yet, their diversity in rich terrestrial ecosystems is still unknown. Here we produce tangible estimates of the total species richness of arthropods in a tropical rainforest. Using a comprehensive range of structured protocols, we sampled the phylogenetic breadth of arthropod taxa from the soil to the forest canopy in the San Lorenzo forest, Panama. We collected 6144 arthropod species from 0.48 hectare and extrapolated total species richness to larger areas on the basis of competing models. The whole 6000-hectare forest reserve most likely sustains 25,000 arthropod species. Notably, just 1 hectare of rainforest yields 〉60% of the arthropod biodiversity held in the wider landscape. Models based on plant diversity fitted the accumulated species richness of both herbivore and nonherbivore taxa exceptionally well. This lends credence to global estimates of arthropod biodiversity developed from plant models.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Basset, Yves -- Cizek, Lukas -- Cuenoud, Philippe -- Didham, Raphael K -- Guilhaumon, Francois -- Missa, Olivier -- Novotny, Vojtech -- Odegaard, Frode -- Roslin, Tomas -- Schmidl, Jurgen -- Tishechkin, Alexey K -- Winchester, Neville N -- Roubik, David W -- Aberlenc, Henri-Pierre -- Bail, Johannes -- Barrios, Hector -- Bridle, Jon R -- Castano-Meneses, Gabriela -- Corbara, Bruno -- Curletti, Gianfranco -- Duarte da Rocha, Wesley -- De Bakker, Domir -- Delabie, Jacques H C -- Dejean, Alain -- Fagan, Laura L -- Floren, Andreas -- Kitching, Roger L -- Medianero, Enrique -- Miller, Scott E -- Gama de Oliveira, Evandro -- Orivel, Jerome -- Pollet, Marc -- Rapp, Mathieu -- Ribeiro, Servio P -- Roisin, Yves -- Schmidt, Jesper B -- Sorensen, Line -- Leponce, Maurice -- New York, N.Y. -- Science. 2012 Dec 14;338(6113):1481-4. doi: 10.1126/science.1226727.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Smithsonian Tropical Research Institute, Panama City, Republic of Panama. bassety@si.edu〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/23239740" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Arthropods/*anatomy & histology/*classification ; *Biodiversity ; Herbivory ; Rain ; Trees ; Tropical Climate
    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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    Transforming fusions of FGFR and TACC genes in human glioblastoma (2012)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2012-07-28
    Description: The brain tumor glioblastoma multiforme (GBM) is among the most lethal forms of human cancer. Here, we report that a small subset of GBMs (3.1%; 3 of 97 tumors examined) harbors oncogenic chromosomal translocations that fuse in-frame the tyrosine kinase coding domains of fibroblast growth factor receptor (FGFR) genes (FGFR1 or FGFR3) to the transforming acidic coiled-coil (TACC) coding domains of TACC1 or TACC3, respectively. The FGFR-TACC fusion protein displays oncogenic activity when introduced into astrocytes or stereotactically transduced in the mouse brain. The fusion protein, which localizes to mitotic spindle poles, has constitutive kinase activity and induces mitotic and chromosomal segregation defects and triggers aneuploidy. Inhibition of FGFR kinase corrects the aneuploidy, and oral administration of an FGFR inhibitor prolongs survival of mice harboring intracranial FGFR3-TACC3-initiated glioma. FGFR-TACC fusions could potentially identify a subset of GBM patients who would benefit from targeted FGFR kinase inhibition.〈br /〉〈br /〉〈a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3677224/" 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/PMC3677224/" target="_blank"〉This paper as free author manuscript - peer-reviewed and accepted for publication〈/a〉〈br /〉〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Singh, Devendra -- Chan, Joseph Minhow -- Zoppoli, Pietro -- Niola, Francesco -- Sullivan, Ryan -- Castano, Angelica -- Liu, Eric Minwei -- Reichel, Jonathan -- Porrati, Paola -- Pellegatta, Serena -- Qiu, Kunlong -- Gao, Zhibo -- Ceccarelli, Michele -- Riccardi, Riccardo -- Brat, Daniel J -- Guha, Abhijit -- Aldape, Ken -- Golfinos, John G -- Zagzag, David -- Mikkelsen, Tom -- Finocchiaro, Gaetano -- Lasorella, Anna -- Rabadan, Raul -- Iavarone, Antonio -- 1R01LM010140-01/LM/NLM NIH HHS/ -- R01 CA085628/CA/NCI NIH HHS/ -- R01 CA101644/CA/NCI NIH HHS/ -- R01 CA127643/CA/NCI NIH HHS/ -- R01 CA131126/CA/NCI NIH HHS/ -- R01 LM010140/LM/NLM NIH HHS/ -- R01 NS061776/NS/NINDS NIH HHS/ -- R01CA085628/CA/NCI NIH HHS/ -- R01CA101644/CA/NCI NIH HHS/ -- R01CA127643/CA/NCI NIH HHS/ -- R01CA131126/CA/NCI NIH HHS/ -- R01NS061776/NS/NINDS NIH HHS/ -- U54 CA121852/CA/NCI NIH HHS/ -- U54 CA121852-05/CA/NCI NIH HHS/ -- New York, N.Y. -- Science. 2012 Sep 7;337(6099):1231-5. doi: 10.1126/science.1220834. Epub 2012 Jul 26.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Institute for Cancer Genetics, Columbia University Medical Center, New York, NY, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/22837387" target="_blank"〉PubMed〈/a〉
    Keywords: Aneuploidy ; Animals ; Antineoplastic Agents/pharmacology ; Benzamides/pharmacology ; Brain Neoplasms/genetics/metabolism ; *Cell Transformation, Neoplastic ; Chromosomal Instability ; Enzyme Inhibitors/pharmacology ; Fetal Proteins/chemistry/*genetics/metabolism ; Glioblastoma/*genetics/metabolism ; Humans ; Mice ; Microtubule-Associated Proteins/chemistry/*genetics/metabolism ; Mitosis ; Neoplasm Transplantation ; Nuclear Proteins/chemistry/*genetics/metabolism ; Oncogene Fusion ; Oncogene Proteins, Fusion/chemistry/genetics/*metabolism ; Piperazines/pharmacology ; Protein Structure, Tertiary ; Pyrazoles/pharmacology ; Pyrimidines/pharmacology ; Receptor, Fibroblast Growth Factor, Type 1/antagonists & ; inhibitors/chemistry/*genetics/metabolism ; Receptor, Fibroblast Growth Factor, Type 3/antagonists & ; inhibitors/chemistry/*genetics/metabolism ; Spindle Apparatus/metabolism ; Translocation, Genetic ; Xenograft Model Antitumor Assays
    Print ISSN: 0036-8075
    Electronic ISSN: 1095-9203
    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 4
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    Nicotinic acid limitation regulates silencing of Candida adhesins during UTI (2005)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2005-03-19
    Description: The adherence of Candida glabrata to host cells is mediated, at least in part, by the EPA genes, a family of adhesins encoded at subtelomeric loci, where they are subject to transcriptional silencing. We show that normally silent EPA genes are expressed during murine urinary tract infection (UTI) and that the inducing signal is the limitation of nicotinic acid (NA), a precursor of nicotinamide adenine dinucleotide (NAD+). C. glabrata is an NA auxotroph, and NA-induced EPA expression is likely the result of a reduction in NAD+ availability for the NAD+-dependent histone deacetylase Sir2p. The adaptation of C. glabrata to the host, therefore, involves a loss of metabolic capacity and exploitation of the resulting auxotrophy to signal a particular host environment.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Domergue, Renee -- Castano, Irene -- De Las Penas, Alejandro -- Zupancic, Margaret -- Lockatell, Virginia -- Hebel, J Richard -- Johnson, David -- Cormack, Brendan P -- 2PO1DK49720/DK/NIDDK NIH HHS/ -- R01AI46223/AI/NIAID NIH HHS/ -- New York, N.Y. -- Science. 2005 May 6;308(5723):866-70. Epub 2005 Mar 17.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Molecular Biology and Genetics, Johns Hopkins University School of Medicine, Baltimore, MD 21205, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/15774723" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Candida glabrata/*genetics/growth & development/*pathogenicity/physiology ; Candidiasis/*microbiology ; Cell Adhesion ; Culture Media ; Female ; Gene Expression Regulation, Fungal ; *Gene Silencing ; Genes, Fungal ; Histone Deacetylases/genetics/metabolism ; Lectins/*genetics ; Mice ; Mice, Inbred BALB C ; Mice, Inbred CBA ; NAD/metabolism ; Niacin/administration & dosage/*metabolism/pharmacology/urine ; Niacinamide/pharmacology/urine ; Sirtuins/genetics/metabolism ; Transcription, Genetic ; Urinary Bladder/microbiology ; Urinary Tract Infections/*microbiology ; Urine/microbiology ; Urothelium/microbiology ; Virulence
    Print ISSN: 0036-8075
    Electronic ISSN: 1095-9203
    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 5
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    Peptide binding and presentation by mouse CD1 (1995)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1995-07-14
    Description: CD1 molecules are distantly related to the major histocompatibility complex (MHC) class I proteins. They are of unknown function. Screening random peptide phage display libraries with soluble empty mouse CD1 (mCD1) identified a peptide binding motif. It consists of three anchor positions occupied by aromatic or bulky hydrophobic amino acids. Equilibrium binding studies demonstrated that mCD1 binds peptides containing the appropriate motif with relatively high affinity. However, in contrast to classical MHC class I molecules, strong binding to mCD1 required relatively long peptides. Peptide-specific, mCD1-restricted T cell responses can be raised, which suggests that the findings are of immunological significance.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Castano, A R -- Tangri, S -- Miller, J E -- Holcombe, H R -- Jackson, M R -- Huse, W D -- Kronenberg, M -- Peterson, P A -- New York, N.Y. -- Science. 1995 Jul 14;269(5221):223-6.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Immunology, La Jolla, CA 92037, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/7542403" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; *Antigen Presentation ; Antigens, CD/chemistry/*immunology/metabolism ; Antigens, CD1 ; Cell Line ; Mice ; Mice, Inbred C57BL ; Molecular Sequence Data ; Peptides/chemistry/*immunology/metabolism ; T-Lymphocytes, Cytotoxic/*immunology ; Transfection
    Print ISSN: 0036-8075
    Electronic ISSN: 1095-9203
    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 6
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    An ID2-dependent mechanism for VHL inactivation in cancer (2016)
    Nature Publishing Group (NPG)
    Details
    Publication Date: 2016-01-07
    Description: Mechanisms that maintain cancer stem cells are crucial to tumour progression. The ID2 protein supports cancer hallmarks including the cancer stem cell state. HIFalpha transcription factors, most notably HIF2alpha (also known as EPAS1), are expressed in and required for maintenance of cancer stem cells (CSCs). However, the pathways that are engaged by ID2 or drive HIF2alpha accumulation in CSCs have remained unclear. Here we report that DYRK1A and DYRK1B kinases phosphorylate ID2 on threonine 27 (Thr27). Hypoxia downregulates this phosphorylation via inactivation of DYRK1A and DYRK1B. The activity of these kinases is stimulated in normoxia by the oxygen-sensing prolyl hydroxylase PHD1 (also known as EGLN2). ID2 binds to the VHL ubiquitin ligase complex, displaces VHL-associated Cullin 2, and impairs HIF2alpha ubiquitylation and degradation. Phosphorylation of Thr27 of ID2 by DYRK1 blocks ID2-VHL interaction and preserves HIF2alpha ubiquitylation. In glioblastoma, ID2 positively modulates HIF2alpha activity. Conversely, elevated expression of DYRK1 phosphorylates Thr27 of ID2, leading to HIF2alpha destabilization, loss of glioma stemness, inhibition of tumour growth, and a more favourable outcome for patients with glioblastoma.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Lee, Sang Bae -- Frattini, Veronique -- Bansal, Mukesh -- Castano, Angelica M -- Sherman, Dan -- Hutchinson, Keino -- Bruce, Jeffrey N -- Califano, Andrea -- Liu, Guangchao -- Cardozo, Timothy -- Iavarone, Antonio -- Lasorella, Anna -- R01CA101644/CA/NCI NIH HHS/ -- R01CA131126/CA/NCI NIH HHS/ -- R01CA178546/CA/NCI NIH HHS/ -- R01NS061776/NS/NINDS NIH HHS/ -- England -- Nature. 2016 Jan 14;529(7585):172-7. doi: 10.1038/nature16475. Epub 2016 Jan 6.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Institute for Cancer Genetics, Columbia University Medical Center, New York 10032, USA. ; Department of Systems Biology, Columbia University Medical Center, New York 10032, USA. ; Center for Computational Biology and Bioinformatics, Columbia University Medical Center, New York 10032, USA. ; Department of Biochemistry and Molecular Pharmacology, NYU School of Medicine, New York 10014, USA. ; Department of Neurosurgery, Columbia University Medical Center, New York 10032, USA. ; Department of Neurology, Columbia University Medical Center, New York 10032, USA. ; Department of Pathology, Columbia University Medical Center, New York 10032, USA. ; Department of Pediatrics, Columbia University Medical Center, New York 10032, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/26735018" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Basic Helix-Loop-Helix Transcription Factors/metabolism ; Cell Hypoxia ; Cell Line, Tumor ; Cullin Proteins/metabolism ; Glioblastoma/*metabolism/*pathology ; Humans ; Hypoxia-Inducible Factor-Proline Dioxygenases/metabolism ; Inhibitor of Differentiation Protein 2/*metabolism ; Male ; Mice ; Neoplastic Stem Cells/*metabolism/pathology ; Oxygen/metabolism ; Phosphorylation ; Phosphothreonine/metabolism ; Protein Binding ; Protein-Serine-Threonine Kinases/antagonists & inhibitors/metabolism ; Protein-Tyrosine Kinases/antagonists & inhibitors/metabolism ; Ubiquitination ; Von Hippel-Lindau Tumor Suppressor Protein/*antagonists & inhibitors/metabolism ; Xenograft Model Antitumor Assays
    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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