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  • 1
    Publication Date: 1999-01-29
    Description: Although dispensable, costimulation through CD28 facilitates activation of naive T lymphocytes. CD28 engagement led to the redistribution and clustering of membrane and intracellular kinase-rich raft microdomains at the site of T cell receptor (TCR) engagements. Although not affecting TCR down-regulation, this process led to higher and more stable tyrosine phosphorylation of several substrates and higher consumption of Lck. These results may provide a general mechanism for amplifying receptor signaling by reorganization of membrane microdomains.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Viola, A -- Schroeder, S -- Sakakibara, Y -- Lanzavecchia, A -- New York, N.Y. -- Science. 1999 Jan 29;283(5402):680-2.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Basel Institute for Immunology, Grenzacherstrasse 487, CH 4005 Basel, Switzerland. viola@bii.ch〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/9924026" target="_blank"〉PubMed〈/a〉
    Keywords: Antigen-Presenting Cells/immunology ; Antigens, CD28/immunology/*metabolism ; Antigens, CD3/immunology ; Cell Membrane/metabolism ; G(M1) Ganglioside/metabolism ; Humans ; *Lymphocyte Activation ; Lymphocyte Specific Protein Tyrosine Kinase p56(lck)/metabolism ; Membrane Lipids/*metabolism ; Phosphorylation ; Phosphotyrosine/metabolism ; Receptors, Antigen, T-Cell/immunology/*metabolism ; Signal Transduction ; T-Lymphocytes/*immunology/metabolism
    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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  • 2
    Publication Date: 1998-02-07
    Description: Benign familial neonatal convulsions (BFNC) is an autosomal dominant epilepsy of infancy, with loci mapped to human chromosomes 20q13.3 and 8q24. By positional cloning, a potassium channel gene (KCNQ2) located on 20q13.3 was isolated and found to be expressed in brain. Expression of KCNQ2 in frog (Xenopus laevis) oocytes led to potassium-selective currents that activated slowly with depolarization. In a large pedigree with BFNC, a five-base pair insertion would delete more than 300 amino acids from the KCNQ2 carboxyl terminus. Expression of the mutant channel did not yield measurable currents. Thus, impairment of potassium-dependent repolarization is likely to cause this age-specific epileptic syndrome.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Biervert, C -- Schroeder, B C -- Kubisch, C -- Berkovic, S F -- Propping, P -- Jentsch, T J -- Steinlein, O K -- New York, N.Y. -- Science. 1998 Jan 16;279(5349):403-6.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Institute for Human Genetics, University of Bonn, Bonn, Germany.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/9430594" target="_blank"〉PubMed〈/a〉
    Keywords: Action Potentials ; Amino Acid Sequence ; Animals ; Brain/metabolism ; Chromosome Mapping ; Chromosomes, Human, Pair 20 ; Cloning, Molecular ; Epilepsy/*genetics/metabolism ; Female ; Frameshift Mutation ; Humans ; Infant, Newborn ; KCNQ2 Potassium Channel ; Male ; Molecular Sequence Data ; Mutagenesis, Insertional ; Oocytes/metabolism ; Open Reading Frames ; Pedigree ; Potassium/metabolism ; Potassium Channels/chemistry/*genetics/metabolism ; *Potassium Channels, Voltage-Gated ; Xenopus laevis
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    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 3
    Publication Date: 2010-07-30
    Description: The post-translational methylation of alpha-amino groups was first discovered over 30 years ago on the bacterial ribosomal proteins L16 and L33 (refs 1, 2), but almost nothing is known about the function or enzymology of this modification. Several other bacterial and eukaryotic proteins have since been shown to be alpha-N-methylated. However, the Ran guanine nucleotide-exchange factor, RCC1, is the only protein for which any biological function of alpha-N-methylation has been identified. Methylation-defective mutants of RCC1 have reduced affinity for DNA and cause mitotic defects, but further characterization of this modification has been hindered by ignorance of the responsible methyltransferase. All fungal and animal N-terminally methylated proteins contain a unique N-terminal motif, Met-(Ala/Pro/Ser)-Pro-Lys, indicating that they may be targets of the same, unknown enzyme. The initiating Met is cleaved, and the exposed alpha-amino group is mono-, di- or trimethylated. Here we report the discovery of the first alpha-N-methyltransferase, which we named N-terminal RCC1 methyltransferase (NRMT). Substrate docking and mutational analysis of RCC1 defined the NRMT recognition sequence and enabled the identification of numerous new methylation targets, including SET (also known as TAF-I or PHAPII) and the retinoblastoma protein, RB. Knockdown of NRMT recapitulates the multi-spindle phenotype seen with methylation-defective RCC1 mutants, demonstrating the importance of alpha-N-methylation for normal bipolar spindle formation and chromosome segregation.〈br /〉〈br /〉〈a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2939154/" 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/PMC2939154/" target="_blank"〉This paper as free author manuscript - peer-reviewed and accepted for publication〈/a〉〈br /〉〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Tooley, Christine E Schaner -- Petkowski, Janusz J -- Muratore-Schroeder, Tara L -- Balsbaugh, Jeremy L -- Shabanowitz, Jeffrey -- Sabat, Michal -- Minor, Wladek -- Hunt, Donald F -- Macara, Ian G -- R01 GM050526/GM/NIGMS NIH HHS/ -- R01 GM050526-17/GM/NIGMS NIH HHS/ -- England -- Nature. 2010 Aug 26;466(7310):1125-8. doi: 10.1038/nature09343.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Microbiology, Center for Cell Signaling, University of Virginia School of Medicine, Charlottesville, Virginia 22908, USA. ces5g@virginia.edu〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/20668449" target="_blank"〉PubMed〈/a〉
    Keywords: Cell Cycle Proteins/*metabolism ; Cell Line ; Chromosome Segregation ; Gene Knockdown Techniques ; Guanine Nucleotide Exchange Factors/*metabolism ; HeLa Cells ; Histone Chaperones/metabolism ; Humans ; Methyltransferases/chemistry/genetics/*metabolism ; Models, Molecular ; Mutation/genetics ; Nuclear Proteins/*metabolism ; Protein Binding ; Protein Structure, Tertiary ; Retinoblastoma Protein/*metabolism ; Spindle Apparatus/metabolism ; Transcription Factors/metabolism
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  • 4
    Publication Date: 2008-05-16
    Description: The ability to observe biological processes continuously, instead of at discrete time points, holds great promise for the study of tissue regeneration. Ideally, single cells would be followed continuously within large tissue volumes (such as organs) over long periods of time. Technical limitations, however, preclude such studies. But, recently, there have been improvements in imaging technologies and biologically compatible labelling agents. Together with new insights into the molecular characteristics of stem cells, which are ultimately responsible for the regenerative potential of all tissues, researchers are now much closer to applying single-cell imaging approaches to research into regeneration and its clinical applications.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Schroeder, Timm -- England -- Nature. 2008 May 15;453(7193):345-51. doi: 10.1038/nature07043.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Institute of Stem Cell Research, Helmholtz Zentrum Munchen - German Research Center for Environmental Health, Ingolstadter Landstrasse 1, D-85764 Neuherberg, Germany. timm.schroeder@helmholtz-muenchen.de〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/18480816" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Humans ; Image Processing, Computer-Assisted/*methods ; Mammals ; Microscopy, Fluorescence/*methods ; Regeneration/*physiology ; Sensitivity and Specificity ; Stem Cells/*cytology
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    Topics: Biology , Chemistry and Pharmacology , Medicine , Natural Sciences in General , Physics
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  • 5
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 2007-11-17
    Description: 〈br /〉〈br /〉〈a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3725277/" 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/PMC3725277/" target="_blank"〉This paper as free author manuscript - peer-reviewed and accepted for publication〈/a〉〈br /〉〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Imaizumi, Takato -- Kay, Steve A -- Schroeder, Julian I -- R01 GM079712/GM/NIGMS NIH HHS/ -- R01 GM079712-02/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 2007 Dec 14;318(5857):1730-1. Epub 2007 Nov 15.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Division of Biological Sciences, Section of Cell and Developmental Biology, University of California, San Diego, La Jolla, CA 92093-0116, USA. timaizumi@ucsd.edu〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/18006706" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Arabidopsis/genetics/*metabolism ; Biological Clocks ; Calcium/*metabolism ; Calcium Signaling ; *Circadian Rhythm ; Cyclic ADP-Ribose/metabolism ; DNA-Binding Proteins/*metabolism ; Feedback, Physiological ; Gene Expression Regulation ; Gene Expression Regulation, Plant ; Glucose/*metabolism ; Heme/metabolism ; Homeostasis ; Humans ; Inositol 1,4,5-Trisphosphate/metabolism ; Metabolic Networks and Pathways ; Nuclear Receptor Subfamily 1, Group D, Member 1 ; Receptors, Cytoplasmic and Nuclear/*metabolism
    Print ISSN: 0036-8075
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    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 6
    Publication Date: 2008-04-26
    Description: beta-Secretase plays a critical role in beta-amyloid formation and thus provides a therapeutic target for Alzheimer's disease. Inhibitor design has usually focused on active-site binding, neglecting the subcellular localization of active enzyme. We have addressed this issue by synthesizing a membrane-anchored version of a beta-secretase transition-state inhibitor by linking it to a sterol moiety. Thus, we targeted the inhibitor to active beta-secretase found in endosomes and also reduced the dimensionality of the inhibitor, increasing its local membrane concentration. This inhibitor reduced enzyme activity much more efficiently than did the free inhibitor in cultured cells and in vivo. In addition to effectively targeting beta-secretase, this strategy could also be used in designing potent drugs against other membrane protein targets.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Rajendran, Lawrence -- Schneider, Anja -- Schlechtingen, Georg -- Weidlich, Sebastian -- Ries, Jonas -- Braxmeier, Tobias -- Schwille, Petra -- Schulz, Jorg B -- Schroeder, Cornelia -- Simons, Mikael -- Jennings, Gary -- Knolker, Hans-Joachim -- Simons, Kai -- New York, N.Y. -- Science. 2008 Apr 25;320(5875):520-3. doi: 10.1126/science.1156609.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Max Planck Institute of Molecular Cell Biology and Genetics, Pfotenhauerstr. 108, 01307 Dresden, Germany.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/18436784" target="_blank"〉PubMed〈/a〉
    Keywords: Alzheimer Disease/drug therapy/enzymology ; Amyloid Precursor Protein Secretases/*antagonists & inhibitors/metabolism ; Amyloid beta-Peptides/metabolism ; Amyloid beta-Protein Precursor/metabolism ; Animals ; Animals, Genetically Modified ; Drosophila/genetics ; Drug Delivery Systems ; *Drug Design ; Endocytosis ; Endosomes/*enzymology ; HeLa Cells ; Humans ; Intracellular Membranes/metabolism ; Membrane Microdomains/enzymology ; Mice ; Peptides/chemistry/metabolism/*pharmacology ; Protease Inhibitors/chemical synthesis/chemistry/metabolism/*pharmacology ; *Sterols
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  • 7
    Publication Date: 2011-01-21
    Description: Human epithelia are permanently challenged by bacteria and fungi, including commensal and pathogenic microbiota. In the gut, the fraction of strict anaerobes increases from proximal to distal, reaching 99% of bacterial species in the colon. At colonic mucosa, oxygen partial pressure is below 25% of airborne oxygen content, moreover microbial metabolism causes reduction to a low redox potential of -200 mV to -300 mV in the colon. Defensins, characterized by three intramolecular disulphide-bridges, are key effector molecules of innate immunity that protect the host from infectious microbes and shape the composition of microbiota at mucosal surfaces. Human beta-defensin 1 (hBD-1) is one of the most prominent peptides of its class but despite ubiquitous expression by all human epithelia, comparison with other defensins suggested only minor antibiotic killing activity. Whereas much is known about the activity of antimicrobial peptides in aerobic environments, data about reducing environments are limited. Herein we show that after reduction of disulphide-bridges hBD-1 becomes a potent antimicrobial peptide against the opportunistic pathogenic fungus Candida albicans and against anaerobic, Gram-positive commensals of Bifidobacterium and Lactobacillus species. Reduced hBD-1 differs structurally from oxidized hBD-1 and free cysteines in the carboxy terminus seem important for the bactericidal effect. In vitro, the thioredoxin (TRX) system is able to reduce hBD-1 and TRX co-localizes with reduced hBD-1 in human epithelia. Hence our study indicates that reduced hBD-1 shields the healthy epithelium against colonisation by commensal bacteria and opportunistic fungi. Accordingly, an intimate interplay between redox-regulation and innate immune defence seems crucial for an effective barrier protecting human epithelia.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Schroeder, Bjoern O -- Wu, Zhihong -- Nuding, Sabine -- Groscurth, Sandra -- Marcinowski, Moritz -- Beisner, Julia -- Buchner, Johannes -- Schaller, Martin -- Stange, Eduard F -- Wehkamp, Jan -- England -- Nature. 2011 Jan 20;469(7330):419-23. doi: 10.1038/nature09674.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Dr. Margarete Fischer-Bosch-Institute of Clinical Pharmacology, 70376 Stuttgart, Germany.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/21248850" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Anti-Infective Agents/chemistry/immunology/*metabolism/*pharmacology ; Bifidobacterium/drug effects/immunology ; Biocatalysis ; Candida albicans/drug effects/immunology ; Colon/immunology/metabolism/microbiology ; Disulfides/chemistry/*metabolism ; Dithiothreitol/pharmacology ; Humans ; Immunity, Innate ; Intestinal Mucosa/immunology/metabolism/microbiology ; Lactobacillus/drug effects/immunology ; Molecular Sequence Data ; Oxidation-Reduction/drug effects ; Oxygen/metabolism ; Partial Pressure ; Protein Conformation/drug effects ; Thioredoxins/metabolism ; beta-Defensins/chemistry/immunology/*metabolism/*pharmacology
    Print ISSN: 0028-0836
    Electronic ISSN: 1476-4687
    Topics: Biology , Chemistry and Pharmacology , Medicine , Natural Sciences in General , Physics
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  • 8
    Publication Date: 2014-05-30
    Description: The availability of human genome sequence has transformed biomedical research over the past decade. However, an equivalent map for the human proteome with direct measurements of proteins and peptides does not exist yet. Here we present a draft map of the human proteome using high-resolution Fourier-transform mass spectrometry. In-depth proteomic profiling of 30 histologically normal human samples, including 17 adult tissues, 7 fetal tissues and 6 purified primary haematopoietic cells, resulted in identification of proteins encoded by 17,294 genes accounting for approximately 84% of the total annotated protein-coding genes in humans. A unique and comprehensive strategy for proteogenomic analysis enabled us to discover a number of novel protein-coding regions, which includes translated pseudogenes, non-coding RNAs and upstream open reading frames. This large human proteome catalogue (available as an interactive web-based resource at http://www.humanproteomemap.org) will complement available human genome and transcriptome data to accelerate biomedical research in health and disease.〈br /〉〈br /〉〈a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4403737/" 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/PMC4403737/" target="_blank"〉This paper as free author manuscript - peer-reviewed and accepted for publication〈/a〉〈br /〉〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Kim, Min-Sik -- Pinto, Sneha M -- Getnet, Derese -- Nirujogi, Raja Sekhar -- Manda, Srikanth S -- Chaerkady, Raghothama -- Madugundu, Anil K -- Kelkar, Dhanashree S -- Isserlin, Ruth -- Jain, Shobhit -- Thomas, Joji K -- Muthusamy, Babylakshmi -- Leal-Rojas, Pamela -- Kumar, Praveen -- Sahasrabuddhe, Nandini A -- Balakrishnan, Lavanya -- Advani, Jayshree -- George, Bijesh -- Renuse, Santosh -- Selvan, Lakshmi Dhevi N -- Patil, Arun H -- Nanjappa, Vishalakshi -- Radhakrishnan, Aneesha -- Prasad, Samarjeet -- Subbannayya, Tejaswini -- Raju, Rajesh -- Kumar, Manish -- Sreenivasamurthy, Sreelakshmi K -- Marimuthu, Arivusudar -- Sathe, Gajanan J -- Chavan, Sandip -- Datta, Keshava K -- Subbannayya, Yashwanth -- Sahu, Apeksha -- Yelamanchi, Soujanya D -- Jayaram, Savita -- Rajagopalan, Pavithra -- Sharma, Jyoti -- Murthy, Krishna R -- Syed, Nazia -- Goel, Renu -- Khan, Aafaque A -- Ahmad, Sartaj -- Dey, Gourav -- Mudgal, Keshav -- Chatterjee, Aditi -- Huang, Tai-Chung -- Zhong, Jun -- Wu, Xinyan -- Shaw, Patrick G -- Freed, Donald -- Zahari, Muhammad S -- Mukherjee, Kanchan K -- Shankar, Subramanian -- Mahadevan, Anita -- Lam, Henry -- Mitchell, Christopher J -- Shankar, Susarla Krishna -- Satishchandra, Parthasarathy -- Schroeder, John T -- Sirdeshmukh, Ravi -- Maitra, Anirban -- Leach, Steven D -- Drake, Charles G -- Halushka, Marc K -- Prasad, T S Keshava -- Hruban, Ralph H -- Kerr, Candace L -- Bader, Gary D -- Iacobuzio-Donahue, Christine A -- Gowda, Harsha -- Pandey, Akhilesh -- HHSN268201000032C/HL/NHLBI NIH HHS/ -- HHSN268201000032C/PHS HHS/ -- P41 GM103504/GM/NIGMS NIH HHS/ -- P41GM103504/GM/NIGMS NIH HHS/ -- T32 GM007814/GM/NIGMS NIH HHS/ -- U24 CA160036/CA/NCI NIH HHS/ -- U24CA160036/CA/NCI NIH HHS/ -- U54 GM103520/GM/NIGMS NIH HHS/ -- U54GM103520/GM/NIGMS NIH HHS/ -- England -- Nature. 2014 May 29;509(7502):575-81. doi: 10.1038/nature13302.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉1] McKusick-Nathans Institute of Genetic Medicine, Johns Hopkins University School of Medicine, Baltimore, Maryland 21205, USA [2] Department of Biological Chemistry, Johns Hopkins University School of Medicine, Baltimore, Maryland 21205, USA. ; Institute of Bioinformatics, International Tech Park, Bangalore 560066, India. ; 1] McKusick-Nathans Institute of Genetic Medicine, Johns Hopkins University School of Medicine, Baltimore, Maryland 21205, USA [2] Adrienne Helis Malvin Medical Research Foundation, New Orleans, Louisiana 70130, USA. ; The Donnelly Centre, University of Toronto, Toronto, Ontario M5S 3E1, Canada. ; 1] McKusick-Nathans Institute of Genetic Medicine, Johns Hopkins University School of Medicine, Baltimore, Maryland 21205, USA [2] Department of Pathology, Universidad de La Frontera, Center of Genetic and Immunological Studies-Scientific and Technological Bioresource Nucleus, Temuco 4811230, Chile. ; McKusick-Nathans Institute of Genetic Medicine, Johns Hopkins University School of Medicine, Baltimore, Maryland 21205, USA. ; School of Medicine, Imperial College London, South Kensington Campus, London SW7 2AZ, UK. ; Department of Biological Chemistry, Johns Hopkins University School of Medicine, Baltimore, Maryland 21205, USA. ; Department of Neurosurgery, Postgraduate Institute of Medical Education & Research, Chandigarh 160012, India. ; Department of Internal Medicine Armed Forces Medical College, Pune 411040, India. ; 1] Department of Neuropathology, National Institute of Mental Health and Neurosciences, Bangalore 560029, India [2] Human Brain Tissue Repository, Neurobiology Research Centre, National Institute of Mental Health and Neurosciences, Bangalore 560029, India. ; Department of Chemical and Biomolecular Engineering and Division of Biomedical Engineering, The Hong Kong University of Science and Technology, Clear Water Bay, Hong Kong. ; Department of Neurology, National Institute of Mental Health and Neurosciences, Bangalore 560029, India. ; Department of Medicine, Johns Hopkins University School of Medicine, Baltimore, Maryland 21224, USA. ; 1] The Sol Goldman Pancreatic Cancer Research Center, Department of Pathology, Johns Hopkins University School of Medicine, Baltimore, Maryland 21231, USA [2] Department of Oncology, Johns Hopkins University School of Medicine, Baltimore, Maryland 21231, USA. ; 1] McKusick-Nathans Institute of Genetic Medicine, Johns Hopkins University School of Medicine, Baltimore, Maryland 21205, USA [2] Department of Surgery, Johns Hopkins University School of Medicine, Baltimore, Maryland 21231, USA. ; 1] Department of Oncology, Johns Hopkins University School of Medicine, Baltimore, Maryland 21231, USA [2] Departments of Immunology and Urology, Sidney Kimmel Comprehensive Cancer Center, Johns Hopkins University School of Medicine, Baltimore, Maryland 21231, USA. ; The Sol Goldman Pancreatic Cancer Research Center, Department of Pathology, Johns Hopkins University School of Medicine, Baltimore, Maryland 21231, USA. ; 1] Department of Obstetrics and Gynecology, Johns Hopkins University School of Medicine Baltimore, Maryland 21205, USA [2] Department of Biochemistry and Molecular Biology, University of Maryland School of Medicine, Baltimore, Maryland 21201, USA. ; 1] The Sol Goldman Pancreatic Cancer Research Center, Department of Pathology, Johns Hopkins University School of Medicine, Baltimore, Maryland 21231, USA [2] Department of Oncology, Johns Hopkins University School of Medicine, Baltimore, Maryland 21231, USA [3] Department of Surgery, Johns Hopkins University School of Medicine, Baltimore, Maryland 21231, USA. ; 1] McKusick-Nathans Institute of Genetic Medicine, Johns Hopkins University School of Medicine, Baltimore, Maryland 21205, USA [2] Department of Biological Chemistry, Johns Hopkins University School of Medicine, Baltimore, Maryland 21205, USA [3] Institute of Bioinformatics, International Tech Park, Bangalore 560066, India [4] Adrienne Helis Malvin Medical Research Foundation, New Orleans, Louisiana 70130, USA [5] The Sol Goldman Pancreatic Cancer Research Center, Department of Pathology, Johns Hopkins University School of Medicine, Baltimore, Maryland 21231, USA [6] Department of Oncology, Johns Hopkins University School of Medicine, Baltimore, Maryland 21231, USA [7] Diana Helis Henry Medical Research Foundation, New Orleans, Louisiana 70130, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/24870542" target="_blank"〉PubMed〈/a〉
    Keywords: Adult ; Cells, Cultured ; Databases, Protein ; Fetus/metabolism ; Fourier Analysis ; Gene Expression Profiling ; Genome, Human/genetics ; Hematopoietic Stem Cells/cytology/metabolism ; Humans ; Internet ; Mass Spectrometry ; Molecular Sequence Annotation ; Open Reading Frames/genetics ; Organ Specificity ; Protein Biosynthesis ; Protein Isoforms/analysis/genetics/metabolism ; Protein Sorting Signals ; Protein Transport ; Proteome/analysis/chemistry/genetics/*metabolism ; *Proteomics ; Pseudogenes/genetics ; RNA, Untranslated/genetics ; Reproducibility of Results ; Untranslated Regions/genetics
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  • 9
    Publication Date: 2013-05-03
    Description: With the global population predicted to grow by at least 25 per cent by 2050, the need for sustainable production of nutritious foods is critical for human and environmental health. Recent advances show that specialized plant membrane transporters can be used to enhance yields of staple crops, increase nutrient content and increase resistance to key stresses, including salinity, pathogens and aluminium toxicity, which in turn could expand available arable land.〈br /〉〈br /〉〈a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3954111/" 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/PMC3954111/" target="_blank"〉This paper as free author manuscript - peer-reviewed and accepted for publication〈/a〉〈br /〉〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Schroeder, Julian I -- Delhaize, Emmanuel -- Frommer, Wolf B -- Guerinot, Mary Lou -- Harrison, Maria J -- Herrera-Estrella, Luis -- Horie, Tomoaki -- Kochian, Leon V -- Munns, Rana -- Nishizawa, Naoko K -- Tsay, Yi-Fang -- Sanders, Dale -- 55005946/Howard Hughes Medical Institute/ -- BB/J004561/1/Biotechnology and Biological Sciences Research Council/United Kingdom -- GM060396/GM/NIGMS NIH HHS/ -- GM078536/GM/NIGMS NIH HHS/ -- P42 ES007373/ES/NIEHS NIH HHS/ -- P42 ES010337/ES/NIEHS NIH HHS/ -- P42ES007373/ES/NIEHS NIH HHS/ -- P42ES010337/ES/NIEHS NIH HHS/ -- R01 GM060396/GM/NIGMS NIH HHS/ -- R01 GM078536/GM/NIGMS NIH HHS/ -- England -- Nature. 2013 May 2;497(7447):60-6. doi: 10.1038/nature11909.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Division of Biological Sciences, Food and Fuel for the 21st Century Center, University of California San Diego, La Jolla, California 92093-0116, USA. jischroeder@ucsd.edu〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/23636397" target="_blank"〉PubMed〈/a〉
    Keywords: Agriculture/*methods ; Aluminum/toxicity ; Biological Transport ; Cell Wall/metabolism ; *Conservation of Natural Resources ; Crops, Agricultural/drug effects/genetics/*metabolism/microbiology ; Food Supply/*statistics & numerical data ; Genetic Engineering ; Humans ; Iron/metabolism ; Membrane Transport Proteins/genetics/*metabolism ; Nitrates/metabolism ; Nutritive Value ; Phosphates/metabolism ; Public Health ; Salinity ; Sodium/toxicity ; Soil/chemistry ; Sucrose/metabolism ; Zinc/metabolism
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  • 10
    Publication Date: 1994-12-02
    Description: Inward-rectifying potassium channels located in the plasma membrane of higher plant and animal cells contribute to cellular homeostasis and excitability. The genes encoding this specific class of K+ channels have not been functionally identified. This report shows that a single messenger RNA transcript from the Arabidopsis thaliana KAT1 complementary DNA confers the functional expression of a hyperpolarization-activated K+ channel in Xenopus oocytes. The channels encoded by KAT1 are highly selective for K+ over other monovalent cations, are blocked by tetraethylammonium and barium, and have a single channel conductance of 28 +/- 7 picosiemens with 118 millimolar K+ in the bathing solution. These functional characteristics, typical of inward-rectifying K+ channels in eukaryotic cells, demonstrate that KAT1 encodes an inward-rectifying K+ channel.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Schachtman, D P -- Schroeder, J I -- Lucas, W J -- Anderson, J A -- Gaber, R F -- New York, N.Y. -- Science. 1992 Dec 4;258(5088):1654-8.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Biology, University of California, San Diego, La Jolla, CA 92093, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8966547" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Arabidopsis/genetics/*metabolism ; Barium/pharmacology ; Biological Transport ; Gene Expression ; Genes, Plant ; Humans ; KB Cells/*metabolism ; Oocytes ; Patch-Clamp Techniques ; Plant Proteins/genetics/metabolism ; Potassium/*metabolism ; Quaternary Ammonium Compounds/metabolism ; Receptors, Interleukin-1/genetics ; Tetraethylammonium Compounds/pharmacology ; Xenopus
    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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