Database : MEDLINE
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[PMID]: 25164820
[Au] Autor:Rotunno MS; Auclair JR; Maniatis S; Shaffer SA; Agar J; Bosco DA
[Ad] Address:From the Department of Neurology, University of Massachusetts Medical School, Worcester, Massachusetts 01605....
[Ti] Title:Identification of a misfolded region in superoxide dismutase 1 that is exposed in amyotrophic lateral sclerosis.
[So] Source:J Biol Chem;289(41):28527-38, 2014 Oct 10.
[Is] ISSN:1083-351X
[Cp] Country of publication:United States
[La] Language:eng
[Ab] Abstract:Mutations and aberrant post-translational modifications within Cu,Zn-superoxide dismutase (SOD1) cause this otherwise protective enzyme to misfold, leading to amyotrophic lateral sclerosis (ALS). The C4F6 antibody selectively binds misfolded SOD1 in spinal cord tissues from postmortem human ALS cases, as well as from an ALS-SOD1 mouse model, suggesting that the C4F6 epitope reports on a pathogenic conformation that is common to misfolded SOD1 variants. To date, the residues and structural elements that comprise this epitope have not been elucidated. Using a chemical cross-linking and mass spectrometry approach, we identified the C4F6 epitope within several ALS-linked SOD1 variants, as well as an oxidized form of WT SOD1, supporting the notion that a similar misfolded conformation is shared among pathological SOD1 proteins. Exposure of the C4F6 epitope was modulated by the SOD1 electrostatic (loop VII) and zinc binding (loop IV) loops and correlated with SOD1-induced toxicity in a primary microglia activation assay. Site-directed mutagenesis revealed Asp(92) and Asp(96) as key residues within the C4F6 epitope required for the SOD1-C4F6 binding interaction. We propose that stabilizing the functional loops within SOD1 and/or obscuring the C4F6 epitope are viable therapeutic strategies for treating SOD1-mediated ALS.
[Pt] Publication type:JOURNAL ARTICLE
[Em] Entry month:1410
[Js] Journal subset:IM
[St] Status:In-Data-Review
[do] DOI:10.1074/jbc.M114.581801

  2 / 178764 MEDLINE  
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[PMID]: 24215402
[Au] Autor:Messina S; Vargas-Lowy D; Musallam A; Healy BC; Kivisakk P; Gandhi R; Bove R; Gholipour T; Khoury S; Weiner HL; Chitnis T
[Ti] Title:Increased leptin and A-FABP levels in relapsing and progressive forms of MS.
[So] Source:BMC Neurol;13(1):172, 2013.
[Is] ISSN:1471-2377
[Cp] Country of publication:England
[La] Language:eng
[Ab] Abstract:BACKGROUND: Leptin and adipocyte-fatty acid binding protein (A-FABP) are produced by white adipose tissue and may play a role in chronic inflammation in Multiple Sclerosis (MS). To assess leptin and A-FABP in relapsing and progressive forms of MS. METHODS: Adipokine levels were measured in untreated adult relapsing-remitting MS (RRMS), secondary progressive MS (SPMS), primary progressive MS (PPMS) and Healthy control (HC). Pediatric-onset MS (POMS) and pediatric healthy controls (PHC) were also assessed. Leptin and A-FABP levels were measured in serum by ELISA. Groups were compared using linear mixed-effects model. RESULTS: Excluding two patients with Body Mass Index (BMI) > 50, a significant difference in leptin level was found between RRMS and HC controlling for age (p = 0.007), SPMS and HC controlling for age alone (p = 0.002), or age and BMI (p = 0.007). A-FABP levels were higher in SPMS than HC (p = 0.007), controlling for age and BMI. Differences in A-FABP levels between POMS and PHC was observed after controlling for age (p = 0.019), but not when BMI was added to the model (p = 0.081). CONCLUSION: Leptin and A-FABP levels are highest in SPMS compared to HC, suggesting a role in pathogenesis of this disease subtype. A-FABP levels are increased in POMS patients and may play a role in the early stages of disease.
[Pt] Publication type:JOURNAL ARTICLE
[Em] Entry month:1410
[Js] Journal subset:IM
[St] Status:In-Data-Review
[do] DOI:10.1186/1471-2377-13-172

  3 / 178764 MEDLINE  
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[PMID]: 25298631
[Au] Autor:Moawad EY
[Ad] Address:Faculty of Engineering, Ain Shams University, Cairo, Egypt ; 217 Alhegaz Street, Alnozha, Cairo, 11351 Egypt.
[Ti] Title:Induction of multiple sclerosis and response to tyrosine kinase inhibitors.
[So] Source:Indian J Clin Biochem;29(4):491-5, 2014 Oct.
[Is] ISSN:0970-1915
[Cp] Country of publication:India
[La] Language:eng
[Ab] Abstract:The goal of this work is to determine the role of the autoimmune cells in multiple sclerosis (MS) induction and the immunomodulatory mechanism of therapy with tyrosine kinase inhibitors (TKIs) in MS attenuation. Samples (5 × 10(5) cells per well) of C6 and primary rat astrocytes were stimulated with 10 ng/mL of platelet-derived growth factor (PDGFbb) as a positive control forming a mouse model of MS. PDGFbb was added to the astrocytes in the absence or presence of 0.1 and 1 µM of imatinib. Proliferation of C6 and primary rat astrocytes samples were assessed for samples staging by the addition of 1 µCi of (3)H-thymidine per well. Samples of RAW 264.7 cells were stimulated for 48 h with 10 ng/mL of PDGFbb in the absence or presence of 0.1 and 1 µM of sorafenib. Tumour necrotic factor (TNF) levels in culture supernatants from RAW 264.7 cells were measured by ELISA. The histologic grade (HG) and the level of TNF of the mouse model of MS was 1/5 and 5 times respectively of those in the control one to clarify that MS induction is due to a major decrease in HG inversely proportional to the accompanied increase in TNF level perpetuating local inflammation and demyelination in MS lesion. The addition of 0.1 and 1 µM doses of imatinib increased HG of the mouse model of MS by 6 and 11 times respectively while 0.1 and 1 µM doses of sorafenib decreased TNF level to be 1/2 and 1/5 of that in the mouse model of MS respectively restoring normal rate of TNF level of normal lesion to show that HGand TNF level would be strongly inversely correlated (r = -0.99) in attenuating MS effectively by TKIs therapy but not in an inverse proportion as in MS induction.
[Pt] Publication type:JOURNAL ARTICLE
[Em] Entry month:1410
[Cu] Class update date: 141011
[Lr] Last revision date:141011
[Da] Date of entry for processing:141009
[St] Status:PubMed-not-MEDLINE
[do] DOI:10.1007/s12291-013-0387-z

  4 / 178764 MEDLINE  
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[PMID]: 25298871
[Au] Autor:Makary MS; Kirsch CF
[Ad] Address:Department of Radiology, The Ohio State University Wexner Medical Center, Columbus, OH, USA ; Department of Radiology, Mount Carmel West Medical Center, Columbus, OH, USA.
[Ti] Title:Tumefactive demyelinating disease with isolated spinal cord involvement.
[So] Source:Acta Radiol Short Rep;3(5):2047981614539324, 2014 Jun.
[Is] ISSN:2047-9816
[Cp] Country of publication:England
[La] Language:eng
[Ab] Abstract:Tumefactive multiple sclerosis (TMS) is an unusual variant of demyelinating disease. TMS has a variable and unknown progression and presents with features similar to a neoplasm making the determination a diagnostic challenge to clinicians. This report presents one of the very few reported cases of isolated spinal cord TMS, and the second case to describe TMS of the lower spinal cord, given that the lesions are typically cervical. This case study presents a diagnostic approach based on clinical, laboratory, and imaging characteristics, as well as sheds some light on the response to therapy and disease evolution.
[Pt] Publication type:JOURNAL ARTICLE
[Em] Entry month:1410
[Cu] Class update date: 141011
[Lr] Last revision date:141011
[Da] Date of entry for processing:141009
[St] Status:PubMed-not-MEDLINE
[do] DOI:10.1177/2047981614539324

  5 / 178764 MEDLINE  
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[PMID]: 25156039
[Au] Autor:Brody AL; Okita K; Shieh J; Liang L; Hubert R; Mamoun M; Farahi J; Mandelkern MA
[Ad] Address:Department of Research, VA Greater Los Angeles Healthcare System (VAGLAHS), 11301 Wilshire Blvd., Los Angeles, CA 90073; Department of Psychiatry, University of California at Los Angeles, 300 UCLA Medical Plaza, Suite 2200, Los Angeles, CA 90095. Electronic address: abrody@ucla.edu....
[Ti] Title:Radiation dosimetry and biodistribution of the translocator protein radiotracer [(11)C]DAA1106 determined with PET/CT in healthy human volunteers.
[So] Source:Nucl Med Biol;41(10):871-5, 2014 Nov-Dec.
[Is] ISSN:1872-9614
[Cp] Country of publication:United States
[La] Language:eng
[Ab] Abstract:INTRODUCTION: When microglia become activated (an integral part of neuroinflammation), cellular morphology changes and expression of translocator protein (TSPO) 18kDa is increased. Over the past several years, [(11)C]DAA1106 has emerged as a reliable radiotracer for labeling TSPO with high affinity during positron emission tomography (PET) scanning. While [(11)C]DAA1106 PET scanning has been used in several research studies, a radiation dosimetry study of this radiotracer in humans has not yet been published. METHODS: Twelve healthy participants underwent full body dynamic [(11)C]DAA1106 PET scanning, with 8 sequential whole body scans (approximately 12 bed positions each), following a single injection. Regions of interest were drawn manually, and time activity curves (TACs) were obtained for 15 organs. OLINDA/EXM 1.1 was used to compute radiation absorbed doses to the target organs, as well as effective dose (ED) and effective dose equivalent (EDE). RESULTS: The ED and EDE were 4.06 ± 0.58µSv/MBq and 5.89 ± 0.83µSv/MBq, respectively. The highest absorbed doses were to the heart wall, kidney, liver, pancreas, and spleen. TACs revealed that peak dose rates are during the first scan (at 6min) for all organs other than the urinary bladder wall, which had its peak dose rate during the fourth scan (at 30min). CONCLUSIONS: The recently developed radiotracer [(11)C]DAA1106 has its EDE and target-organ absorbed dose such that, for a single administration, its radiation dosimetry is well within the U.S. FDA guidelines for basic research studies in adults. This dose level implies that the dosimetry for multiple [(11)C]DAA1106 scans within a given year also falls within FDA guidelines, and this favorable property makes this radiotracer suitable for examining microglial activation repeatedly over time, which may in the future be useful for longitudinal tracking of disease progression and monitoring of therapy response in conditions marked by neuroinflammation (e.g., head trauma and multiple sclerosis).
[Pt] Publication type:JOURNAL ARTICLE
[Em] Entry month:1410
[Js] Journal subset:IM
[St] Status:In-Data-Review

  6 / 178764 MEDLINE  
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[PMID]: 25247274
[Au] Autor:Maughan D; Toth M
[Ad] Address:Department of Molecular Physiology & Biophysics, University of Vermont, Burlington, VT 05405, USA. dmaughan@uvm.edu.
[Ti] Title:Discerning primary and secondary factors responsible for clinical fatigue in multisystem diseases.
[So] Source:Biology (Basel);3(3):606-22, 2014.
[Is] ISSN:2079-7737
[Cp] Country of publication:Switzerland
[La] Language:eng
[Ab] Abstract:Fatigue is a common symptom of numerous acute and chronic diseases, including myalgic encephalomyelitis/chronic fatigue syndrome, multiple sclerosis, heart failure, cancer, and many others. In these multi-system diseases the physiological determinants of enhanced fatigue encompass a combination of metabolic, neurological, and myofibrillar adaptations. Previous research studies have focused on adaptations specific to skeletal muscle and their role in fatigue. However, most have neglected the contribution of physical inactivity in assessing disease syndromes, which, through deconditioning, likely contributes to symptomatic fatigue. In this commentary, we briefly review disease-related muscle phenotypes in the context of whether they relate to the primary disease or whether they develop secondary to reduced physical activity. Knowledge of the etiology of the skeletal muscle adaptations in these conditions and their contribution to fatigue symptoms is important for understanding the utility of exercise rehabilitation as an intervention to alleviate the physiological precipitants of fatigue.
[Pt] Publication type:JOURNAL ARTICLE; REVIEW
[Em] Entry month:1409
[Cu] Class update date: 141011
[Lr] Last revision date:141011
[Da] Date of entry for processing:140924
[St] Status:PubMed-not-MEDLINE
[do] DOI:10.3390/biology3030606

  7 / 178764 MEDLINE  
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[PMID]: 24349280
[Au] Autor:Mike A; Strammer E; Aradi M; Orsi G; Perlaki G; Hajnal A; Sandor J; Banati M; Illes E; Zaitsev A; Herold R; Guttmann CR; Illes Z
[Ad] Address:Division of Clinical and Experimental Neuroimmunology, Department of Neurology, University of Pecs, Pecs, Hungary ; Center for Neurological Imaging, Departments of Radiology and Neurology, Brigham and Women's Hospital, Harvard Medical School, Boston, MA, United States of America....
[Ti] Title:Disconnection mechanism and regional cortical atrophy contribute to impaired processing of facial expressions and theory of mind in multiple sclerosis: a structural MRI study.
[So] Source:PLoS One;8(12):e82422, 2013.
[Is] ISSN:1932-6203
[Cp] Country of publication:United States
[La] Language:eng
[Ab] Abstract:Successful socialization requires the ability of understanding of others' mental states. This ability called as mentalization (Theory of Mind) may become deficient and contribute to everyday life difficulties in multiple sclerosis. We aimed to explore the impact of brain pathology on mentalization performance in multiple sclerosis. Mentalization performance of 49 patients with multiple sclerosis was compared to 24 age- and gender matched healthy controls. T1- and T2-weighted three-dimensional brain MRI images were acquired at 3Tesla from patients with multiple sclerosis and 18 gender- and age matched healthy controls. We assessed overall brain cortical thickness in patients with multiple sclerosis and the scanned healthy controls, and measured the total and regional T1 and T2 white matter lesion volumes in patients with multiple sclerosis. Performances in tests of recognition of mental states and emotions from facial expressions and eye gazes correlated with both total T1-lesion load and regional T1-lesion load of association fiber tracts interconnecting cortical regions related to visual and emotion processing (genu and splenium of corpus callosum, right inferior longitudinal fasciculus, right inferior fronto-occipital fasciculus, uncinate fasciculus). Both of these tests showed correlations with specific cortical areas involved in emotion recognition from facial expressions (right and left fusiform face area, frontal eye filed), processing of emotions (right entorhinal cortex) and socially relevant information (left temporal pole). Thus, both disconnection mechanism due to white matter lesions and cortical thinning of specific brain areas may result in cognitive deficit in multiple sclerosis affecting emotion and mental state processing from facial expressions and contributing to everyday and social life difficulties of these patients.
[Mh] MeSH terms primary: Cerebral Cortex/pathology
Cerebral Cortex/physiopathology
Facial Expression
Mental Processes/physiology
Multiple Sclerosis/pathology
Multiple Sclerosis/physiopathology
Theory of Mind
[Mh] MeSH terms secundary: Adult
Atrophy
Case-Control Studies
Cognition
Demography
Female
Humans
Magnetic Resonance Imaging
Male
Middle Aged
Social Behavior
Young Adult
[Pt] Publication type:JOURNAL ARTICLE; RESEARCH SUPPORT, N.I.H., EXTRAMURAL; RESEARCH SUPPORT, NON-U.S. GOV'T
[Em] Entry month:1410
[Js] Journal subset:IM
[Da] Date of entry for processing:131218
[St] Status:MEDLINE
[do] DOI:10.1371/journal.pone.0082422

  8 / 178764 MEDLINE  
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[PMID]: 24349219
[Au] Autor:Murdock DG; Bradford Y; Schnetz-Boutaud N; Mayo P; Allen MJ; D'Aoust LN; Liang X; Mitchell SL; Zuchner S; Small GW; Gilbert JR; Pericak-Vance MA; Haines JL
[Ad] Address:Center for Human Genetics Research and Department of Molecular Physiology and Biophysics, Vanderbilt University, Nashville, Tennessee, United States of America....
[Ti] Title:KIAA1462, a coronary artery disease associated gene, is a candidate gene for late onset Alzheimer disease in APOE carriers.
[So] Source:PLoS One;8(12):e82194, 2013.
[Is] ISSN:1932-6203
[Cp] Country of publication:United States
[La] Language:eng
[Ab] Abstract:Alzheimer disease (AD) is a devastating neurodegenerative disease affecting more than five million Americans. In this study, we have used updated genetic linkage data from chromosome 10 in combination with expression data from serial analysis of gene expression to choose a new set of thirteen candidate genes for genetic analysis in late onset Alzheimer disease (LOAD). Results in this study identify the KIAA1462 locus as a candidate locus for LOAD in APOE4 carriers. Two genes exist at this locus, KIAA1462, a gene associated with coronary artery disease, and "rokimi", encoding an untranslated spliced RNA The genetic architecture at this locus suggests that the gene product important in this association is either "rokimi", or a different isoform of KIAA1462 than the isoform that is important in cardiovascular disease. Expression data suggests that isoform f of KIAA1462 is a more attractive candidate for association with LOAD in APOE4 carriers than "rokimi" which had no detectable expression in brain.
[Mh] MeSH terms primary: Alzheimer Disease/genetics
Apolipoprotein E4/genetics
Cell Adhesion Molecules/genetics
Coronary Artery Disease/genetics
Genetic Association Studies
Genetic Predisposition to Disease
[Mh] MeSH terms secundary: Alleles
Brain/metabolism
Brain/pathology
Chromosomes, Human, Pair 10/genetics
Databases, Genetic
Exons/genetics
Female
Gene Expression Regulation
Genetic Loci
Genome, Human/genetics
Heterozygote
Humans
Introns/genetics
Linkage Disequilibrium/genetics
Lod Score
Male
Polymorphism, Single Nucleotide/genetics
RNA/isolation & purification
Real-Time Polymerase Chain Reaction
[Pt] Publication type:JOURNAL ARTICLE; RESEARCH SUPPORT, N.I.H., EXTRAMURAL; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Name of substance:0 (Apolipoprotein E4); 0 (Cell Adhesion Molecules); 0 (KIAA1462 protein, human); 63231-63-0 (RNA)
[Em] Entry month:1410
[Js] Journal subset:IM
[Da] Date of entry for processing:131218
[St] Status:MEDLINE
[do] DOI:10.1371/journal.pone.0082194

  9 / 178764 MEDLINE  
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[PMID]: 23920243
[Au] Autor:Skorupa A; Urbach S; Vigy O; King MA; Chaumont-Dubel S; Prehn JH; Marin P
[Ad] Address:Institut de Génomique Fonctionnelle, CNRS UMR 5203, F-34094 Montpellier, France; INSERM U661, F-34094 Montpellier, France; Université Montpellier I, F-34094 Montpellier, France; Université Montpellier II, F-34094 Montpellier, France; Royal College of Surgeons in Ireland, Dept. of Physiology and Medical Physics, Dublin 2, Ireland.
[Ti] Title:Angiogenin induces modifications in the astrocyte secretome: relevance to amyotrophic lateral sclerosis.
[So] Source:J Proteomics;91:274-85, 2013 Oct 8.
[Is] ISSN:1876-7737
[Cp] Country of publication:Netherlands
[La] Language:eng
[Ab] Abstract:UNLABELLED: Amyotrophic lateral sclerosis (ALS) is a fatal neurodegenerative disease affecting lower and upper motoneurons. Recent studies have shown that both motor neurons and non-neuronal neighbouring cells such as astrocytes and microglia contribute to disease pathology. Loss-of-function mutations in the angiogenin (ANG) gene have been identified in ALS patients. Angiogenin is enriched in motor neurons and exerts neuroprotective effects in vitro and in vivo. We have recently shown that motoneurons secrete angiogenin, and that secreted angiogenin is exclusively taken up by astrocytes, suggesting a paracrine mechanism of neuroprotection. To gain insights into astrocyte effectors of angiogenin-induced neuroprotection, we examined alterations in the astrocyte secretome induced by angiogenin treatment using quantitative proteomics based on Stable Isotope Labelling by Amino Acids in Cell Culture (SILAC). We identified 2128 proteins in conditioned media from primary cultured mouse astrocytes, including 1247 putative secreted proteins. Of these, 60 proteins showed significant regulation of secretion in response to angiogenin stimulation. Regulated proteins include chemokines and cytokines, proteases and protease inhibitors as well as proteins involved in reorganising the extracellular matrix. In conclusion, this proteomic analysis increases our knowledge of the astrocyte secretome and reveals potential molecular substrates underlying the paracrine, neuroprotective effects of angiogenin. BIOLOGICAL SIGNIFICANCE: This study provides the most extensive list of astrocyte-secreted proteins available and reveals novel potential molecular substrates of astrocyte-neuron communication. It also identifies a set of astrocyte-derived proteins that might slow down ALS disease progression. It should be relevant to a large readership of neuroscientists and clinicians, in particular those with an interest in the physiological and pathological roles of astrocytes and in the molecular and cellular mechanisms underlying neurodegenerative disorders.
[Mh] MeSH terms primary: Amyotrophic Lateral Sclerosis/metabolism
Astrocytes/metabolism
Gene Expression Regulation
Ribonuclease, Pancreatic/metabolism
[Mh] MeSH terms secundary: Animals
Animals, Newborn
Astrocytes/cytology
Cell Communication
Cell Survival
Culture Media, Conditioned/chemistry
Disease Progression
Extracellular Matrix/metabolism
Mice
Mice, Inbred C57BL
Motor Neurons/metabolism
Mutation
Neurons/metabolism
Proteome
Proteomics
[Pt] Publication type:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Name of substance:0 (Culture Media, Conditioned); 0 (Proteome); EC 3.1.27.- (angiogenin); EC 3.1.27.5 (Ribonuclease, Pancreatic)
[Em] Entry month:1410
[Js] Journal subset:IM
[Da] Date of entry for processing:131111
[St] Status:MEDLINE

  10 / 178764 MEDLINE  
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[PMID]: 24136005
[Au] Autor:Sethi DK; Gordo S; Schubert DA; Wucherpfennig KW
[Ad] Address:Department of Cancer Immunology and AIDS, Dana-Farber Cancer Institute, Boston, Massachusetts 02115, USA.
[Ti] Title:Crossreactivity of a human autoimmune TCR is dominated by a single TCR loop.
[So] Source:Nat Commun;4:2623, 2013.
[Is] ISSN:2041-1723
[Cp] Country of publication:England
[La] Language:eng
[Ab] Abstract:Self-reactive CD4 T cells are thought to have a central role in the pathogenesis of many chronic inflammatory human diseases. Microbial peptides can activate self-reactive T cells, but the structural basis for such crossreactivity is not well understood. The Hy.1B11 T cell receptor (TCR) originates from a patient with multiple sclerosis and recognizes the self-antigen myelin basic protein. Here we report the structural mechanism of TCR crossreactivity with two distinct peptides from human pathogens. The structures show that a single TCR residue (CDR3α F95) makes the majority of contacts with the self-peptide and both microbial peptides (66.7-80.6%) due to a highly tilted TCR-binding topology on the peptide-MHC surface. Further, a neighbouring residue located on the same TCR loop (CDR3α E98) forms an energetically critical interaction with the MHC molecule. These data show how binding by a self-reactive TCR favors crossreactivity between self and microbial antigens.
[Mh] MeSH terms primary: Autoantigens/chemistry
Bacterial Proteins/chemistry
CD4-Positive T-Lymphocytes/immunology
Myelin Basic Protein/chemistry
Receptors, Antigen, T-Cell/chemistry
Viral Proteins/chemistry
[Mh] MeSH terms secundary: Amino Acid Sequence
Autoantigens/immunology
Autoimmunity
Bacterial Proteins/immunology
Binding Sites
CD4-Positive T-Lymphocytes/chemistry
CD4-Positive T-Lymphocytes/pathology
Cross Reactions
Crystallography, X-Ray
Humans
Models, Molecular
Molecular Sequence Data
Multiple Sclerosis/metabolism
Multiple Sclerosis/pathology
Myelin Basic Protein/immunology
Protein Binding
Protein Structure, Secondary
Protein Structure, Tertiary
Pseudomonas aeruginosa/chemistry
Receptors, Antigen, T-Cell/immunology
Sequence Alignment
Sequence Homology, Amino Acid
Simplexvirus/chemistry
Viral Proteins/immunology
[Pt] Publication type:JOURNAL ARTICLE; RESEARCH SUPPORT, N.I.H., EXTRAMURAL; RESEARCH SUPPORT, NON-U.S. GOV'T; RESEARCH SUPPORT, U.S. GOV'T, NON-P.H.S.
[Nm] Name of substance:0 (Autoantigens); 0 (Bacterial Proteins); 0 (Myelin Basic Protein); 0 (Receptors, Antigen, T-Cell); 0 (Viral Proteins)
[Em] Entry month:1405
[Cu] Class update date: 141011
[Lr] Last revision date:141011
[Js] Journal subset:IM
[Da] Date of entry for processing:131018
[St] Status:MEDLINE
[do] DOI:10.1038/ncomms3623


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