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1. Full Text Modulation of dynamin-related protein 1 (DRP1) function by increased O-linked-β-N-acetylglucosamine modification (O-GlcNAc) in cardiac myocytes
by Gawlowski, Thomas and Suarez, Jorge and Scott, Brian and Torres-Gonzalez, Moises and Wang, Hong and Schwappacher, Raphaela and Han, Xuemei and Yates III, John R and Hoshijima, Masahiko and Dillmann, Wolfgang
Journal of Biological Chemistry, ISSN 0021-9258, 08/2012, Volume 287, Issue 35, pp. 30024 - 30034
O-linked-N-acetyl-glucosamine glycosylation (O-GlcNAcylation) of the serine and threonine residues of cellular proteins is a dynamic process and affects... 
CROSS-TALK | FUSION | GLCNACYLATION | PHOSPHORYLATION | REGULATES MITOCHONDRIAL FISSION | GLUCOSE | BIOCHEMISTRY & MOLECULAR BIOLOGY | KINASE | MAMMALIAN-CELLS | MASS-SPECTROMETRY | MORPHOLOGY | Mitochondrial Diseases - pathology | Dynamins - metabolism | Mitochondria, Heart - metabolism | Mitochondria, Heart - pathology | Humans | Diabetes Mellitus, Experimental - genetics | Mitochondrial Diseases - metabolism | Cytoplasm - metabolism | Acetylglucosaminidase - genetics | Cytoplasm - pathology | Acetylglucosamine - metabolism | Phosphorylation - genetics | Acetylglucosaminidase - metabolism | Muscle Proteins - metabolism | Membrane Potential, Mitochondrial - genetics | Cytoplasm - genetics | Diabetes Complications - genetics | Acetylation | Diabetes Complications - pathology | Diabetes Mellitus, Experimental - metabolism | Mitochondria, Heart - genetics | Mitochondrial Diseases - genetics | Diabetes Complications - metabolism | Dynamins - genetics | Acetylglucosamine - genetics | Protein Transport - genetics | Muscle Proteins - genetics | Myocytes, Cardiac - pathology | Animals | Diabetes Mellitus, Experimental - pathology | Myocytes, Cardiac - metabolism | Mice | O-GlcNAcylation | Mitochondria | Glycosylation | Diabetes | Cardiomyopathy | Cell Biology
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2. Full Text Integrative analysis of oncogenic fusion genes and their functional impact in colorectal cancer
by Choi, Yuri and Kwon, Chae Hwa and Lee, Seon Jin and Park, Joonghoon and Shin, Jong-Yeon and Park, Do Youn
British Journal of Cancer, ISSN 0007-0920, 07/2018, Volume 119, Issue 2, pp. 230 - 240
BACKGROUND: Fusion genes are good candidates of molecular targets for cancer therapy. However, there is insufficient research on the clinical implications and... 
CELL LUNG-CANCER | COLON-CANCER | DOMAIN | PROTEIN | ONCOLOGY | FOLATE RECEPTOR-BETA | CATENIN | POTENTIAL THERAPEUTIC TARGET | ALK FUSION | EXPRESSION | BREAST | Calmodulin-Binding Proteins - genetics | Cell Proliferation - genetics | Folate Receptor 2 - genetics | Membrane Proteins - genetics | Colorectal Neoplasms - genetics | Humans | Middle Aged | Kaplan-Meier Estimate | Transcription Factor TFIIIA - genetics | Male | Acetylglucosaminidase - genetics | Nerve Tissue Proteins - genetics | Cell Movement - genetics | Anaplastic Lymphoma Kinase - genetics | Ikaros Transcription Factor - genetics | Disease-Free Survival | Colorectal Neoplasms - therapy | Oncogene Proteins, Fusion - genetics | Cyclin-Dependent Kinase 8 - genetics | Female | High-Throughput Nucleotide Sequencing | Colorectal Neoplasms - pathology | Gene Expression Regulation, Neoplastic - genetics | Precision Medicine | Cell proliferation | Genes | Colorectal carcinoma | Colorectal cancer | Data processing | Ribonucleic acid--RNA | Gene expression | Cell fusion | Patients | Gene fusion | Molecular chains | Gene sequencing | Cell lines | Mutation | Cell migration | Tumors | Cancer
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3. Full Text Lysosomal Proteins as a Therapeutic Target in Neurodegeneration
by Mc Donald, Jessica M and Krainc, Dimitri
Annual Review of Medicine, ISSN 0066-4219, 1/2017, Volume 68, Issue 1, pp. 445 - 458
Several proteins that are mutated in lysosomal storage diseases are linked to neurodegenerative disease. This review focuses on some of these lysosomal enzymes... 
neurodegenerative disease | Parkinson's disease | lysosomal storage disease | neurodegenerative drug candidates | Neurodegenerative disease | Lysosomal storage disease | Neurodegenerative drug candidates | MEDICINE, RESEARCH & EXPERIMENTAL | UBIQUITIN-PROTEASOME SYSTEM | STORAGE DISEASES | PHARMACOLOGICAL CHAPERONES | GLUCOCEREBROSIDASE MUTATIONS | NIEMANN-PICK C1 | AMYLOID-BETA PEPTIDE | RISK-FACTOR | ALPHA-SYNUCLEIN ACCUMULATION | NEURONOPATHIC GAUCHER-DISEASE | PARKINSONS-DISEASE | Sphingomyelin Phosphodiesterase - genetics | Glucosylceramidase - genetics | Humans | Lysosomal Storage Diseases - genetics | Lysosomes - enzymology | Neurodegenerative Diseases - genetics | Acetylglucosaminidase - genetics | Autophagy | Membrane Glycoproteins - genetics | Proteins - genetics | Carrier Proteins - genetics | Amyloidogenic Proteins - metabolism | Endocytosis | Hexosaminidase B - genetics | Proteins - metabolism | Proton-Translocating ATPases - genetics | Lysosomal Storage Diseases - drug therapy | Lysosomal Storage Diseases - metabolism | Lysosomal Storage Diseases - complications | Hexosaminidase A - genetics | Metabolism, Inborn errors of | Complications and side effects | Care and treatment | Nervous system | Genetic aspects | Degeneration | Risk factors
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4. Full Text Mutational Effects on Transglycosylating Activity of Family 18 Chitinases and Construction of a Hypertransglycosylating Mutant
by Zakariassen, Henrik and Hansen, Mona Cecilie and Jøranli, Maje and Eijsink, Vincent G. H and Sørlie, Morten
Biochemistry, ISSN 0006-2960, 06/2011, Volume 50, Issue 25, pp. 5693 - 5703
Enzymatic features that determine transglycosylating activity have been investigated through site-directed mutagenesis studies on two family 18 chitinases,... 
CHITOOLIGOSACCHARIDES | BETA-N-ACETYLGLUCOSAMINIDASE | ACIDIC MAMMALIAN CHITINASE | OLIGOSACCHARIDES | CRYSTAL-STRUCTURE | BIOCHEMISTRY & MOLECULAR BIOLOGY | BINDING CLEFT | RESOLUTION | SERRATIA-MARCESCENS | AROMATIC RESIDUES | TRICHODERMA-HARZIANUM | Multigene Family - genetics | Mutagenesis, Site-Directed | Bacterial Proteins - chemical synthesis | Bacterial Proteins - genetics | Catalytic Domain - genetics | Glycosylation | Chitinases - chemical synthesis | Substrate Specificity - genetics | Chitinases - genetics | Aspartic Acid - genetics | Chitinases - classification | Hydrolysis | Point Mutation | Serratia marcescens - genetics | Oligosaccharides - chemistry | Serratia marcescens - enzymology | Enzyme Stability - genetics | Asparagine - genetics | Oligosaccharides - genetics | Chemical mutagenesis | Usage | Analysis | Digestive enzymes | Genetic aspects | Chemical properties | Mass spectrometry | Methods | Nocardia corallina | Index Medicus
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5. Full Text The role of extracellular DNA in the establishment, maintenance and perpetuation of bacterial biofilms
by Okshevsky, Mira and Meyer, Rikke Louise
Critical Reviews in Microbiology, ISSN 1040-841X, 8/2015, Volume 41, Issue 3, pp. 341 - 352
Abstract The significance of extracellular DNA (eDNA) in biofilms was overlooked until researchers added DNAse to a Pseudomonas aeruginosa biofilm and watched... 
extracellular DNA | Antimicrobial resistance | bacterial adhesion | biofilm | Biofilm | Bacterial adhesion | Extracellular DNA | NATURAL TRANSFORMATION | N-ACETYLGLUCOSAMINIDASE | MICROBIOLOGY | EDNA RELEASE | CHROMOSOMAL DNA | CELL-DEATH | STREPTOCOCCUS-PNEUMONIAE | PSEUDOMONAS-AERUGINOSA | NEISSERIA-GONORRHOEAE | STAPHYLOCOCCUS-AUREUS | HORIZONTAL GENE-TRANSFER | Bacteria - growth & development | Bacteria - immunology | DNA, Bacterial - genetics | Biofilms - growth & development | Immune Evasion - genetics | Bacterial Adhesion - genetics | Drug Resistance, Bacterial - genetics | Bacteria - genetics | Bacterial Physiological Phenomena - genetics | Immune Evasion - immunology | Gene Transfer, Horizontal - genetics | DNA, Bacterial - secretion
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6. Full Text Molecular characterization of 355 mucopolysaccharidosis patients reveals 104 novel mutations
by Pollard, Laura M and Pollard, Laura M and Jones, Julie R and Jones, Julie R and Wood, Tim C and Wood, Tim C
Journal of Inherited Metabolic Disease, ISSN 0141-8955, 3/2013, Volume 36, Issue 2, pp. 179 - 187
Mucopolysaccharidosis (MPS) disorders are heterogeneous and caused by deficient lysosomal degradation of glycosaminoglycans, resulting in distinct but... 
Human Genetics | Biochemistry, general | Pediatrics | Internal Medicine | Medicine & Public Health | Metabolic Diseases | MEDICINE, RESEARCH & EXPERIMENTAL | DIAGNOSIS | GLYCOSAMINOGLYCANS | FLUOROMETRIC ENZYME ASSAY | TANDEM MASS-SPECTROMETRY | SANFILIPPO | SCREENING NEWBORNS | BLOOD SPOTS APPLICATION | HUNTER-SYNDROME | IVA | ENDOCRINOLOGY & METABOLISM | GENETICS & HEREDITY | LYSOSOMAL-ENZYMES | Chondroitinsulfatases - genetics | Hydrolases - genetics | Exons | Mucopolysaccharidoses - enzymology | Gene Frequency | Humans | Acetylglucosaminidase - genetics | N-Acetylgalactosamine-4-Sulfatase - genetics | DNA Mutational Analysis | Iduronate Sulfatase - genetics | Mucopolysaccharidoses - genetics | Mutation | Iduronidase - genetics | Cohort Studies | Glycosaminoglycans | Invisibility | Analysis | Genes | Mucopolysaccharidosis | Genetic aspects | Population genetics
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7. Full Text Insulin-like growth factor II peptide fusion enables uptake and lysosomal delivery of α-N-acetylglucosaminidase to mucopolysaccharidosis type IIIB fibroblasts
by Kan, Shih-Hsin and Troitskaya, Larisa A and Sinow, Carolyn S and Haitz, Karyn and Todd, Amanda K and Di Stefano, Ariana and Le, Steven Q and Dickson, Patricia I and Tippin, Brigette L
Biochemical Journal, ISSN 0264-6021, 03/2014, Volume 458, Issue 2, pp. 281 - 289
Enzyme replacement therapy for MPS IIIB (mucopolysaccharidosis type IIIB; also known as Sanfilippo B syndrome) has been hindered by inadequate mannose 6... 
Mucopolysaccharidosis | Lysosomal storage disease | Enzyme replacement therapy | Sanfilippo | Insulin-like growth factor (IGF) | enzyme replacement therapy | NEUROLOGICAL DISEASE | GENE DELIVERY | lysosomal storage disease | SANFILIPPO-SYNDROME | BIOCHEMISTRY & MOLECULAR BIOLOGY | mucopolysaccharidosis | SYNDROME TYPE-B | CEREBROSPINAL-FLUID | ENZYME-REPLACEMENT THERAPY | MURINE MODEL | insulin-like growth factor (IGF) | HAMSTER OVARY CELLS | MOUSE MODEL | CENTRAL-NERVOUS-SYSTEM | Fibroblasts - enzymology | Protein Binding - genetics | Cricetulus | Humans | Lysosomes - genetics | Lysosomes - enzymology | Acetylglucosaminidase - genetics | Recombinant Fusion Proteins - metabolism | Insulin-Like Growth Factor II - genetics | Lysosomes - metabolism | Acetylglucosaminidase - metabolism | Mucopolysaccharidosis III - metabolism | Endocytosis - genetics | Acetylglucosaminidase - biosynthesis | CHO Cells | Fibroblasts - metabolism | Cricetinae | Mucopolysaccharidosis III - genetics | Up-Regulation - genetics | Binding Sites - genetics | Fibroblasts - pathology | Mucopolysaccharidosis III - enzymology | Animals | Cell Line, Tumor | Recombinant Fusion Proteins - genetics | Amino Acid Motifs - genetics | insulin-like growth factor
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8. Full Text Correction of Neurological Disease of Mucopolysaccharidosis IIIB in Adult Mice by rAAV9 Trans-Blood–Brain Barrier Gene Delivery
by Fu, Haiyan and DiRosario, Julianne and Killedar, Smruti and Zaraspe, Kimberly and McCarty, Douglas M
Molecular Therapy, ISSN 1525-0016, 06/2011, Volume 19, Issue 6, pp. 1025 - 1033
The greatest challenge in developing therapies for mucopolysaccharidosis (MPS) IIIB is to achieve efficient central nervous system (CNS) delivery across the... 
MEDICINE, RESEARCH & EXPERIMENTAL | AAV VECTORS | LYSOSOMAL STORAGE DISEASE | NEUTRALIZING ANTIBODIES | ADENOASSOCIATED VIRUS | SYNDROME TYPE-B | FUNCTIONAL CORRECTION | BIOTECHNOLOGY & APPLIED MICROBIOLOGY | IMMUNE-RESPONSES | MOUSE MODEL | GENETICS & HEREDITY | MPS IIIB | ALPHA-N-ACETYLGLUCOSAMINIDASE | Dependovirus - genetics | Animals | Acetylglucosaminidase - metabolism | Mucopolysaccharidosis III - therapy | Polymerase Chain Reaction | Mice | Acetylglucosaminidase - genetics | Genetic Vectors - genetics | Blood-Brain Barrier - metabolism | Genetic Therapy - methods | Mice, Knockout | Nervous System Diseases - therapy | Original
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9. Controlling autolysis during flagella insertion in gram-negative bacteria
by Herlihey, Francesca A and Clarke, Anthony J
Advances in Experimental Medicine and Biology, ISSN 0065-2598, 2017, Volume 925, pp. 41 - 56
The flagellum is an important macromolecular machine for many pathogenic bacteria. It is a hetero-oligomeric structure comprised of three major sub-structures:... 
Peptidoglycan | β-N-acetylglucosaminidases | Flagella | Lytic transglycosylases | Peptidoglycan - metabolism | Multigene Family | Bacterial Proteins - chemistry | Helicobacter pylori - genetics | Flagella - enzymology | Acetylglucosaminidase - genetics | Salmonella typhimurium - ultrastructure | Acetylglucosaminidase - metabolism | Helicobacter pylori - enzymology | Pseudomonas aeruginosa - enzymology | Flagella - genetics | Salmonella typhimurium - enzymology | Amino Acid Sequence | Escherichia coli - enzymology | Peptidoglycan Glycosyltransferase - metabolism | Flagella - ultrastructure | Peptidoglycan Glycosyltransferase - chemistry | Salmonella typhimurium - genetics | Bacterial Proteins - genetics | Helicobacter pylori - ultrastructure | Bacteriolysis - genetics | Peptidoglycan Glycosyltransferase - genetics | Sequence Alignment | Pseudomonas aeruginosa - genetics | Escherichia coli - genetics | Acetylglucosaminidase - chemistry | Bacterial Proteins - metabolism | Gene Expression Regulation, Bacterial | Pseudomonas aeruginosa - ultrastructure | Escherichia coli - ultrastructure
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10. Full Text Sanfilippo syndrome: a mini-review
by Valstar, M. J and Ruijter, G. J. G and van Diggelen, O. P and Poorthuis, B. J and Wijburg, F. A
Journal of Inherited Metabolic Disease, ISSN 0141-8955, 2008, Volume 31, Issue 2, pp. 240 - 252
Mucopolysaccharidosis type III (MPS III, Sanfilippo syndrome) is an autosomal recessive disorder, caused by a deficiency in one of the four enzymes involved in... 
Biochemistry, general | Human Genetics | Pediatrics | Internal Medicine | Medicine & Public Health | Metabolic Diseases | MUCOPOLYSACCHARIDOSIS TYPE IIIA | BONE-MARROW-TRANSPLANTATION | ENDOCRINOLOGY & METABOLISM | GENETICS & HEREDITY | SYNDROME TYPE-B | SYNDROME TYPE-A | LYSOSOMAL STORAGE DISEASES | FLUOROMETRIC ENZYME ASSAY | MANNOSE 6-PHOSPHATE RECEPTOR | BLOOD-BRAIN-BARRIER | ALPHA-N-ACETYLGLUCOSAMINIDASE | SUBSTRATE DEPRIVATION THERAPY | Sulfatases - genetics | Hydrolases - genetics | Prognosis | Humans | Child, Preschool | Lysosomes - enzymology | Infant | Acetylglucosaminidase - genetics | Acetyltransferases - genetics | Heparitin Sulfate - metabolism | Incidence | Young Adult | Mucopolysaccharidosis III - diagnosis | Mucopolysaccharidosis III - mortality | Acetyltransferases - deficiency | Time Factors | Adult | Child | Acetylglucosaminidase - deficiency | Genetic Predisposition to Disease | Mucopolysaccharidosis III - genetics | Sulfatases - deficiency | Hydrolases - deficiency | Mucopolysaccharidosis III - enzymology | Phenotype | Animals | Adolescent | Mucopolysaccharidosis III - therapy
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