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Tytuł :
A CRISPR-Cas9-engineered mouse model for GPI-anchor deficiency mirrors human phenotypes and exhibits hippocampal synaptic dysfunctions.
Autorzy :
Rodríguez de Los Santos M; Institute for Medical Genetics and Human Genetics, Charité-Universitätsmedizin Berlin, 13353 Berlin, Germany.; Berlin-Brandenburg School for Regenerative Therapies, Charité-Universitätsmedizin Berlin, 13353 Berlin, Germany.; Research Group Development and Disease, Max Planck Institute for Molecular Genetics, 14195 Berlin, Germany.; Institute for Genomic Statistics and Bioinformatics, University of Bonn, 53127 Bonn, Germany.
Rivalan M; Animal Outcome Core Facility of the NeuroCure Center, Charité-Universitätsmedizin Berlin, 10117 Berlin, Germany.; Institute of Cognitive Neurobiology, Humboldt University, 10117 Berlin, Germany.
David FS; Institute for Genomic Statistics and Bioinformatics, University of Bonn, 53127 Bonn, Germany.; Institute of Human Genetics, Faculty of Medicine, University Hospital Bonn, 53127 Bonn, Germany.
Stumpf A; Neuroscience Research Center, Charité-Universitätsmedizin Berlin, 10117 Berlin, Germany.
Pitsch J; Section for Translational Epilepsy Research, Department of Neuropathology, University Hospital Bonn, 53127 Bonn, Germany.; Department of Epileptology, University Hospital Bonn, 53127 Bonn, Germany.
Tsortouktzidis D; Section for Translational Epilepsy Research, Department of Neuropathology, University Hospital Bonn, 53127 Bonn, Germany.
Velasquez LM; Neuroscience Research Center, Charité-Universitätsmedizin Berlin, 10117 Berlin, Germany.
Voigt A; Neuroscience Research Center, Charité-Universitätsmedizin Berlin, 10117 Berlin, Germany.
Schilling K; Anatomisches Institut, Anatomie und Zellbiologie, Faculty of Medicine, University of Bonn, 53115 Bonn, Germany.
Mattei D; Institute of Veterinary Pharmacology and Toxicology, University of Zürich (UZH), 8057 Zürich, Switzerland.
Long M; Animal Outcome Core Facility of the NeuroCure Center, Charité-Universitätsmedizin Berlin, 10117 Berlin, Germany.; Institute of Cognitive Neurobiology, Humboldt University, 10117 Berlin, Germany.
Vogt G; Institute for Medical Genetics and Human Genetics, Charité-Universitätsmedizin Berlin, 13353 Berlin, Germany.; Research Group Development and Disease, Max Planck Institute for Molecular Genetics, 14195 Berlin, Germany.
Knaus A; Institute for Genomic Statistics and Bioinformatics, University of Bonn, 53127 Bonn, Germany.
Fischer-Zirnsak B; Institute for Medical Genetics and Human Genetics, Charité-Universitätsmedizin Berlin, 13353 Berlin, Germany.; Research Group Development and Disease, Max Planck Institute for Molecular Genetics, 14195 Berlin, Germany.
Wittler L; Department Developmental Genetics, Max Planck Institute for Molecular Genetics, 14195 Berlin, Germany.
Timmermann B; Sequencing Core Facility, Max Planck Institute for Molecular Genetics, 14195 Berlin, Germany.
Robinson PN; The Jackson Laboratory for Genomic Medicine, Farmington, CT 06032.; Institute for Systems Genomics, University of Connecticut, Farmington, CT 06032.
Horn D; Institute for Medical Genetics and Human Genetics, Charité-Universitätsmedizin Berlin, 13353 Berlin, Germany.
Mundlos S; Institute for Medical Genetics and Human Genetics, Charité-Universitätsmedizin Berlin, 13353 Berlin, Germany.; Research Group Development and Disease, Max Planck Institute for Molecular Genetics, 14195 Berlin, Germany.
Kornak U; Institute for Medical Genetics and Human Genetics, Charité-Universitätsmedizin Berlin, 13353 Berlin, Germany.; Research Group Development and Disease, Max Planck Institute for Molecular Genetics, 14195 Berlin, Germany.; Institute of Human Genetics, University Medical Center Göttingen, 37073 Göttingen, Germany.
Becker AJ; Section for Translational Epilepsy Research, Department of Neuropathology, University Hospital Bonn, 53127 Bonn, Germany.
Schmitz D; Neuroscience Research Center, Charité-Universitätsmedizin Berlin, 10117 Berlin, Germany.
Winter Y; Animal Outcome Core Facility of the NeuroCure Center, Charité-Universitätsmedizin Berlin, 10117 Berlin, Germany.; Institute of Cognitive Neurobiology, Humboldt University, 10117 Berlin, Germany.
Krawitz PM; Institute for Genomic Statistics and Bioinformatics, University of Bonn, 53127 Bonn, Germany; .
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Źródło :
Proceedings of the National Academy of Sciences of the United States of America [Proc Natl Acad Sci U S A] 2021 Jan 12; Vol. 118 (2).
Typ publikacji :
Journal Article; Research Support, Non-U.S. Gov't
MeSH Terms :
Glycosylphosphatidylinositols/*genetics
Glycosylphosphatidylinositols/*metabolism
Mannosyltransferases/*metabolism
Abnormalities, Multiple/genetics ; Amino Acid Sequence ; Amino Acids/genetics ; Animals ; CRISPR-Cas Systems ; Disease Models, Animal ; Epilepsy/genetics ; Glycosylphosphatidylinositols/deficiency ; Hippocampus/metabolism ; Intellectual Disability/genetics ; Mannosyltransferases/physiology ; Mice ; Mice, Inbred C57BL ; Mutation ; Mutation, Missense ; Phenotype ; Protein Engineering/methods ; Seizures/genetics ; Seizures/physiopathology
SCR Disease Name :
Glycosylphosphatidylinositol deficiency
Czasopismo naukowe
Tytuł :
Structural basis for the core-mannan biosynthesis of cell wall fungal-type galactomannan in Aspergillus fumigatus .
Autorzy :
Hira D; Department of Applied Life Science, Faculty of Biotechnology and Life Science, Sojo University, Kumamoto, Kumamoto, Japan. Electronic address: .
Onoue T; Department of Applied Microbial Technology, Faculty of Biotechnology and Life Science, Sojo University, Kumamoto, Kumamoto, Japan.
Oka T; Department of Applied Microbial Technology, Faculty of Biotechnology and Life Science, Sojo University, Kumamoto, Kumamoto, Japan. Electronic address: .
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Źródło :
The Journal of biological chemistry [J Biol Chem] 2020 Nov 06; Vol. 295 (45), pp. 15407-15417. Date of Electronic Publication: 2020 Sep 01.
Typ publikacji :
Journal Article; Research Support, Non-U.S. Gov't
MeSH Terms :
Aspergillus fumigatus/*metabolism
Cell Wall/*chemistry
Fungal Proteins/*metabolism
Mannans/*biosynthesis
Mannosyltransferases/*metabolism
Aspergillus fumigatus/cytology ; Cell Wall/metabolism ; Fungal Proteins/chemistry ; Fungal Proteins/genetics ; Mannans/chemistry ; Mannosyltransferases/chemistry ; Mannosyltransferases/genetics ; Molecular Dynamics Simulation
Czasopismo naukowe
Tytuł :
Yil102c-A is a Functional Homologue of the DPMII Subunit of Dolichyl Phosphate Mannose Synthase in Saccharomyces cerevisiae .
Autorzy :
Piłsyk S; Institute of Biochemistry and Biophysics Polish Academy of Sciences, 02-106 Warsaw, Poland.
Perlinska-Lenart U; Institute of Biochemistry and Biophysics Polish Academy of Sciences, 02-106 Warsaw, Poland.
Janik A; Institute of Biochemistry and Biophysics Polish Academy of Sciences, 02-106 Warsaw, Poland.
Gryz E; Institute of Biochemistry and Biophysics Polish Academy of Sciences, 02-106 Warsaw, Poland.
Ajchler-Adamska M; Institute of Biochemistry and Biophysics Polish Academy of Sciences, 02-106 Warsaw, Poland.
Kruszewska JS; Institute of Biochemistry and Biophysics Polish Academy of Sciences, 02-106 Warsaw, Poland.
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Źródło :
International journal of molecular sciences [Int J Mol Sci] 2020 Nov 25; Vol. 21 (23). Date of Electronic Publication: 2020 Nov 25.
Typ publikacji :
Journal Article
MeSH Terms :
Fungal Proteins/*genetics
Mannosyltransferases/*genetics
Saccharomyces cerevisiae/*genetics
Amino Acid Sequence/genetics ; Dolichol Phosphates/metabolism ; Fungal Proteins/metabolism ; Glycosylation ; Humans ; Mannose/metabolism ; Mannosyltransferases/metabolism ; Saccharomyces cerevisiae/metabolism ; Sequence Homology, Amino Acid ; Trichoderma/genetics
Czasopismo naukowe
Tytuł :
A mutation in Asparagine-Linked Glycosylation 12 (ALG12) leads to receptor misglycosylation and attenuated responses to multiple microbial elicitors.
Autorzy :
Trempel F; Leibniz Institute of Plant Biochemistry, Halle, Germany.
Eschen-Lippold L; Leibniz Institute of Plant Biochemistry, Halle, Germany.
Bauer N; Leibniz Institute of Plant Biochemistry, Halle, Germany.
Ranf S; Leibniz Institute of Plant Biochemistry, Halle, Germany.
Westphal L; Leibniz Institute of Plant Biochemistry, Halle, Germany.
Scheel D; Leibniz Institute of Plant Biochemistry, Halle, Germany.
Lee J; Leibniz Institute of Plant Biochemistry, Halle, Germany.
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Źródło :
FEBS letters [FEBS Lett] 2020 Aug; Vol. 594 (15), pp. 2440-2451. Date of Electronic Publication: 2020 Jun 15.
Typ publikacji :
Journal Article; Research Support, Non-U.S. Gov't
MeSH Terms :
Arabidopsis/*enzymology
Arabidopsis Proteins/*metabolism
Mannosyltransferases/*metabolism
Arabidopsis/genetics ; Arabidopsis Proteins/genetics ; Glycosylation ; Mannosyltransferases/genetics
Czasopismo naukowe
Tytuł :
LncRNA MEG3 contributes to drug resistance in acute myeloid leukemia by positively regulating ALG9 through sponging miR-155.
Autorzy :
Yu Y; College of Laboratory Medicine, Dalian Medical University, Dalian, China.; Department of Emergency, Affiliated Dalian Friend-ship Hospital of Dalian Medical University, Dalian, China.
Kou D; Department of Clinical Laboratory, the First Affiliated Hospital of Dalian Medical University, Dalian, China.
Liu B; College of Laboratory Medicine, Dalian Medical University, Dalian, China.
Huang Y; College of Laboratory Medicine, Dalian Medical University, Dalian, China.
Li S; College of Laboratory Medicine, Dalian Medical University, Dalian, China.
Qi Y; College of Laboratory Medicine, Dalian Medical University, Dalian, China.
Guo Y; College of Laboratory Medicine, Dalian Medical University, Dalian, China.
Huang T; College of Laboratory Medicine, Dalian Medical University, Dalian, China.
Qi X; College of Laboratory Medicine, Dalian Medical University, Dalian, China.
Jia L; College of Laboratory Medicine, Dalian Medical University, Dalian, China.
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Źródło :
International journal of laboratory hematology [Int J Lab Hematol] 2020 Aug; Vol. 42 (4), pp. 464-472. Date of Electronic Publication: 2020 May 02.
Typ publikacji :
Journal Article
MeSH Terms :
Drug Resistance, Neoplasm*
Gene Expression Regulation, Leukemic*
Leukemia, Myeloid, Acute/*metabolism
Mannosyltransferases/*biosynthesis
Membrane Proteins/*biosynthesis
MicroRNAs/*metabolism
Neoplasm Proteins/*biosynthesis
RNA, Long Noncoding/*metabolism
RNA, Neoplasm/*metabolism
Female ; Humans ; Leukemia, Myeloid, Acute/genetics ; Leukemia, Myeloid, Acute/pathology ; Male ; Mannosyltransferases/genetics ; Membrane Proteins/genetics ; MicroRNAs/genetics ; Neoplasm Proteins/genetics ; RNA, Long Noncoding/genetics ; RNA, Neoplasm/genetics ; THP-1 Cells ; U937 Cells
Czasopismo naukowe
Tytuł :
ALG3-CDG: a patient with novel variants and review of the genetic and ophthalmic findings.
Autorzy :
Farolfi M; Department of Paediatrics and Inherited Metabolic Disorders, First Faculty of Medicine, Charles University and General University Hospital in Prague, Ke Karlovu 2, 128 08, Prague, Czech Republic.
Cechova A; Department of Paediatrics and Inherited Metabolic Disorders, First Faculty of Medicine, Charles University and General University Hospital in Prague, Ke Karlovu 2, 128 08, Prague, Czech Republic.
Ondruskova N; Department of Paediatrics and Inherited Metabolic Disorders, First Faculty of Medicine, Charles University and General University Hospital in Prague, Ke Karlovu 2, 128 08, Prague, Czech Republic.
Zidkova J; Centre of Molecular Biology and Genetics, University Hospital Brno and Masaryk University, Brno, Czech Republic.
Kousal B; Department of Ophthalmology, First Faculty of Medicine, Charles University and General University Hospital in Prague, Prague, Czech Republic.
Hansikova H; Department of Paediatrics and Inherited Metabolic Disorders, First Faculty of Medicine, Charles University and General University Hospital in Prague, Ke Karlovu 2, 128 08, Prague, Czech Republic.
Honzik T; Department of Paediatrics and Inherited Metabolic Disorders, First Faculty of Medicine, Charles University and General University Hospital in Prague, Ke Karlovu 2, 128 08, Prague, Czech Republic.
Liskova P; Department of Paediatrics and Inherited Metabolic Disorders, First Faculty of Medicine, Charles University and General University Hospital in Prague, Ke Karlovu 2, 128 08, Prague, Czech Republic. .; Department of Ophthalmology, First Faculty of Medicine, Charles University and General University Hospital in Prague, Prague, Czech Republic. .
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Źródło :
BMC ophthalmology [BMC Ophthalmol] 2021 Jun 05; Vol. 21 (1), pp. 249. Date of Electronic Publication: 2021 Jun 05.
Typ publikacji :
Case Reports; Journal Article; Review
MeSH Terms :
Congenital Disorders of Glycosylation*/genetics
Retinal Degeneration*
Child, Preschool ; Eye ; Female ; High-Throughput Nucleotide Sequencing ; Humans ; Infant ; Infant, Newborn ; Mannosyltransferases/genetics ; Phenotype
Czasopismo naukowe
Tytuł :
Enhanced influenza A H1N1 T cell epitope recognition and cross-reactivity to protein-O-mannosyltransferase 1 in Pandemrix-associated narcolepsy type 1.
Autorzy :
Vuorela A; Clinicum, University of Helsinki, Helsinki, Finland.
Freitag TL; Department of Bacteriology and Immunology, University of Helsinki, Helsinki, Finland. .; Translational Immunology Research Program, University of Helsinki, Helsinki, Finland. .
Leskinen K; Translational Immunology Research Program, University of Helsinki, Helsinki, Finland.
Pessa H; Translational Immunology Research Program, University of Helsinki, Helsinki, Finland.
Härkönen T; Clinicum, University of Helsinki, Helsinki, Finland.
Stracenski I; Department of Bacteriology and Immunology, University of Helsinki, Helsinki, Finland.
Kirjavainen T; Children's Hospital, University of Helsinki, and Helsinki University Hospital, Helsinki, Finland.
Olsen P; Department of Child Neurology, Oulu University Hospital, Oulu, Finland.
Saarenpää-Heikkilä O; Department of Pediatrics, Tampere University Hospital, Tampere, Finland.
Ilonen J; Immunogenetics Laboratory, Institute of Biomedicine, University of Turku, Turku, Finland.; Clinical Microbiology, Turku University Hospital, Turku, Finland.
Knip M; Clinicum, University of Helsinki, Helsinki, Finland.; Children's Hospital, University of Helsinki, and Helsinki University Hospital, Helsinki, Finland.; Research Program for Clinical and Molecular Metabolism, University of Helsinki, Helsinki, Finland.
Vaheri A; Department of Virology, University of Helsinki, Helsinki, Finland.
Partinen M; Clinicum, University of Helsinki, Helsinki, Finland.; Department of Neurosciences, University of Helsinki, Helsinki, Finland.; Helsinki Sleep Clinic, Vitalmed Research Center, Helsinki, Finland.
Saavalainen P; Translational Immunology Research Program, University of Helsinki, Helsinki, Finland.
Meri S; Department of Bacteriology and Immunology, University of Helsinki, Helsinki, Finland.; Translational Immunology Research Program, University of Helsinki, Helsinki, Finland.
Vaarala O; Clinicum, University of Helsinki, Helsinki, Finland.
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Źródło :
Nature communications [Nat Commun] 2021 Apr 16; Vol. 12 (1), pp. 2283. Date of Electronic Publication: 2021 Apr 16.
Typ publikacji :
Journal Article; Observational Study; Research Support, Non-U.S. Gov't
MeSH Terms :
Influenza A Virus, H1N1 Subtype/*immunology
Influenza Vaccines/*adverse effects
Influenza, Human/*prevention & control
Mannosyltransferases/*immunology
Narcolepsy/*immunology
Adolescent ; Animals ; Autoantibodies/blood ; Autoantibodies/immunology ; Autoantigens/immunology ; B-Lymphocytes/immunology ; CD4 Antigens/genetics ; Case-Control Studies ; Child ; Child, Preschool ; Cross Reactions/immunology ; Disease Models, Animal ; Epitopes, T-Lymphocyte/immunology ; Female ; HLA-DQ beta-Chains/immunology ; Humans ; Infant ; Influenza Vaccines/immunology ; Influenza, Human/immunology ; Influenza, Human/virology ; Male ; Mice, Transgenic ; Narcolepsy/blood ; Narcolepsy/chemically induced ; Neuraminidase/immunology ; T-Lymphocytes/immunology ; Viral Proteins/immunology ; Young Adult
SCR Disease Name :
Narcolepsy 1
Czasopismo naukowe
Tytuł :
Clostridioides difficile cd2775 Encodes a Unique Mannosyl-1-Phosphotransferase for Polysaccharide II Biosynthesis.
Autorzy :
Ma Z; Department of Chemistry, Georgia State University, 50 Decatur Street SE, Atlanta, Georgia 30303, United States.
Zhang GL; Department of Chemistry, Georgia State University, 50 Decatur Street SE, Atlanta, Georgia 30303, United States.
Gadi MR; Department of Chemistry, Georgia State University, 50 Decatur Street SE, Atlanta, Georgia 30303, United States.
Guo Y; Department of Chemistry, Georgia State University, 50 Decatur Street SE, Atlanta, Georgia 30303, United States.
Wang P; Department of Chemistry, Georgia State University, 50 Decatur Street SE, Atlanta, Georgia 30303, United States.
Li L; Department of Chemistry, Georgia State University, 50 Decatur Street SE, Atlanta, Georgia 30303, United States.
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Źródło :
ACS infectious diseases [ACS Infect Dis] 2020 Apr 10; Vol. 6 (4), pp. 680-686. Date of Electronic Publication: 2020 Feb 20.
Typ publikacji :
Letter; Research Support, N.I.H., Extramural
MeSH Terms :
Clostridioides difficile/*enzymology
Clostridioides difficile/*genetics
Mannosyltransferases/*genetics
Phosphotransferases/*genetics
Polysaccharides, Bacterial/*biosynthesis
Bacterial Proteins/chemistry ; Bacterial Proteins/genetics ; Escherichia coli/genetics ; Mannose/metabolism ; Mannosyltransferases/chemistry ; Multigene Family ; Phosphorylation ; Phosphotransferases/chemistry ; Substrate Specificity
Raport
Tytuł :
Both Svp26 and Mnn6 are required for the efficient ER exit of Mnn4 in Saccharomyces cerevisiae.
Autorzy :
Noda Y; Department of Biotechnology, The University of Tokyo.; Collaborative Research Institute for Innovative Microbiology, The University of Tokyo.
Arai S; Department of Cell Science, Institute of Biomedical Sciences, Fukushima Medical University School of Medicine.
Wada I; Department of Cell Science, Institute of Biomedical Sciences, Fukushima Medical University School of Medicine.
Yoda K; Department of Biotechnology, The University of Tokyo.
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Źródło :
The Journal of general and applied microbiology [J Gen Appl Microbiol] 2019 Dec 19; Vol. 65 (5), pp. 215-224. Date of Electronic Publication: 2019 Mar 06.
Typ publikacji :
Journal Article
MeSH Terms :
Endoplasmic Reticulum/*metabolism
Mannosyltransferases/*metabolism
Membrane Proteins/*metabolism
Saccharomyces cerevisiae/*metabolism
Saccharomyces cerevisiae Proteins/*metabolism
Vesicular Transport Proteins/*metabolism
Amino Acid Motifs/genetics ; Golgi Apparatus/metabolism ; Mannosyltransferases/chemistry ; Mannosyltransferases/genetics ; Membrane Proteins/chemistry ; Membrane Proteins/genetics ; Mutation ; Protein Binding ; Saccharomyces cerevisiae/genetics ; Saccharomyces cerevisiae Proteins/chemistry ; Saccharomyces cerevisiae Proteins/genetics ; Transport Vesicles/metabolism ; Vesicular Transport Proteins/genetics
Czasopismo naukowe
Tytuł :
Cloning and Partial Characterization of an Endo-α-(1→6)-d-Mannanase Gene from Bacillus circulans .
Autorzy :
Angala SK; Mycobacteria Research Laboratories, Department of Microbiology, Immunology and Pathology, Colorado State University, Fort Collins, CO 80523-1682, USA.
Li W; Mycobacteria Research Laboratories, Department of Microbiology, Immunology and Pathology, Colorado State University, Fort Collins, CO 80523-1682, USA.
Palčeková Z; Mycobacteria Research Laboratories, Department of Microbiology, Immunology and Pathology, Colorado State University, Fort Collins, CO 80523-1682, USA.
Zou L; Department of Chemistry, The University of Alberta, Edmonton, AB T6G 2G2, Canada.
Lowary TL; Department of Chemistry, The University of Alberta, Edmonton, AB T6G 2G2, Canada.
McNeil MR; Mycobacteria Research Laboratories, Department of Microbiology, Immunology and Pathology, Colorado State University, Fort Collins, CO 80523-1682, USA.
Jackson M; Mycobacteria Research Laboratories, Department of Microbiology, Immunology and Pathology, Colorado State University, Fort Collins, CO 80523-1682, USA.
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Źródło :
International journal of molecular sciences [Int J Mol Sci] 2019 Dec 11; Vol. 20 (24). Date of Electronic Publication: 2019 Dec 11.
Typ publikacji :
Journal Article
MeSH Terms :
Cloning, Molecular*
Genes, Bacterial*
Bacillus/*enzymology
Bacillus/*genetics
Mannosyltransferases/*genetics
Lipopolysaccharides/chemistry ; Lipopolysaccharides/metabolism ; Mannosides/metabolism ; Mannosyltransferases/chemistry ; Mannosyltransferases/isolation & purification ; Mycobacterium smegmatis/metabolism ; Protein Domains ; Substrate Specificity
Czasopismo naukowe
Tytuł :
Translational Regulation of Pmt1 and Pmt2 by Bfr1 Affects Unfolded Protein O-Mannosylation.
Autorzy :
Castells-Ballester J; Centre for Organismal Studies (COS), Glycobiology, Heidelberg University, D-69120 Heidelberg, Germany.
Rinis N; Centre for Organismal Studies (COS), Glycobiology, Heidelberg University, D-69120 Heidelberg, Germany.
Kotan I; Center for Molecular Biology of Heidelberg University (ZMBH), German Cancer Research Center (DKFZ), ZMBH-DKFZ Alliance, D-69120 Heidelberg, Germany.
Gal L; Department of Molecular Genetics, Weizmann Institute of Science, Rehovot 7610001, Israel.
Bausewein D; Centre for Organismal Studies (COS), Glycobiology, Heidelberg University, D-69120 Heidelberg, Germany.; spm2-Safety Projects & More GmbH, D-69493 Hirschberg a. d. Bergstraße, Germany.
Kats I; Center for Molecular Biology of Heidelberg University (ZMBH), German Cancer Research Center (DKFZ), ZMBH-DKFZ Alliance, D-69120 Heidelberg, Germany.
Zatorska E; Centre for Organismal Studies (COS), Glycobiology, Heidelberg University, D-69120 Heidelberg, Germany.
Kramer G; Center for Molecular Biology of Heidelberg University (ZMBH), German Cancer Research Center (DKFZ), ZMBH-DKFZ Alliance, D-69120 Heidelberg, Germany.
Bukau B; Center for Molecular Biology of Heidelberg University (ZMBH), German Cancer Research Center (DKFZ), ZMBH-DKFZ Alliance, D-69120 Heidelberg, Germany.
Schuldiner M; Department of Molecular Genetics, Weizmann Institute of Science, Rehovot 7610001, Israel.
Strahl S; Centre for Organismal Studies (COS), Glycobiology, Heidelberg University, D-69120 Heidelberg, Germany.
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Źródło :
International journal of molecular sciences [Int J Mol Sci] 2019 Dec 10; Vol. 20 (24). Date of Electronic Publication: 2019 Dec 10.
Typ publikacji :
Journal Article
MeSH Terms :
Mannosyltransferases/*chemistry
Mannosyltransferases/*genetics
Repressor Proteins/*genetics
Saccharomyces cerevisiae/*metabolism
Saccharomyces cerevisiae Proteins/*genetics
Endoplasmic Reticulum/metabolism ; Glycosylation ; Mannosyltransferases/metabolism ; Protein Folding ; Protein Processing, Post-Translational ; Protein Stability ; Repressor Proteins/metabolism ; Saccharomyces cerevisiae/genetics ; Saccharomyces cerevisiae Proteins/metabolism ; Sequence Deletion
Czasopismo naukowe
Tytuł :
[Novel therapeutics for paroxysmal nocturnal hemoglobinuria].
Autorzy :
Nishimura JI; Department of Hematology and Oncology, Osaka University Graduate School of Medicine.
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Źródło :
[Rinsho ketsueki] The Japanese journal of clinical hematology [Rinsho Ketsueki] 2021; Vol. 62 (5), pp. 463-471.
Typ publikacji :
Journal Article
MeSH Terms :
Hemoglobinuria, Paroxysmal*/drug therapy
Glycosylphosphatidylinositols ; Hematopoietic Stem Cells ; Hemolysis ; Humans ; Mannosyltransferases ; Quality of Life
Czasopismo naukowe
Tytuł :
A Plasmodium falciparum C -mannosyltransferase is dispensable for parasite asexual blood stage development.
Autorzy :
López-Gutiérrez B; ISGlobal, Barcelona Ctr. Int. Health Res. (CRESIB), Hospital Clínic - Universitat de Barcelona, Barcelona, Spain.
Cova M; ISGlobal, Barcelona Ctr. Int. Health Res. (CRESIB), Hospital Clínic - Universitat de Barcelona, Barcelona, Spain.
Izquierdo L; ISGlobal, Barcelona Ctr. Int. Health Res. (CRESIB), Hospital Clínic - Universitat de Barcelona, Barcelona, Spain.
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Źródło :
Parasitology [Parasitology] 2019 Dec; Vol. 146 (14), pp. 1767-1772. Date of Electronic Publication: 2019 Oct 23.
Typ publikacji :
Journal Article; Research Support, Non-U.S. Gov't
MeSH Terms :
Life Cycle Stages*
Mannosyltransferases/*physiology
Plasmodium falciparum/*enzymology
Plasmodium falciparum/*physiology
Protozoan Proteins/*physiology
Blood/parasitology ; CRISPR-Cas Systems ; Glycosylation ; Loss of Function Mutation ; Mannosyltransferases/genetics ; Plasmodium falciparum/genetics ; Protozoan Proteins/genetics ; Reproduction, Asexual ; Salivary Glands/parasitology ; Thrombospondins/genetics ; Thrombospondins/physiology
Czasopismo naukowe
Tytuł :
ALG12-CDG: novel glycophenotype insights endorse the molecular defect.
Autorzy :
Sturiale L; CNR, Institute for Polymers, Composites and Biomaterials, IPCB, Catania, Italy.
Bianca S; Medical Genetics, Referral Centre for Rare Genetic Diseases, ARNAS Garibaldi, Catania, Italy.
Garozzo D; CNR, Institute for Polymers, Composites and Biomaterials, IPCB, Catania, Italy.
Terracciano A; Laboratory of Medical Genetics, Bambino Gesù Children's Hospital, IRCCS, Rome, Italy.
Agolini E; Laboratory of Medical Genetics, Bambino Gesù Children's Hospital, IRCCS, Rome, Italy.
Messina A; CNR, Institute for Polymers, Composites and Biomaterials, IPCB, Catania, Italy.
Palmigiano A; CNR, Institute for Polymers, Composites and Biomaterials, IPCB, Catania, Italy.
Esposito F; CNR, Institute for Polymers, Composites and Biomaterials, IPCB, Catania, Italy.
Barone C; Medical Genetics, Referral Centre for Rare Genetic Diseases, ARNAS Garibaldi, Catania, Italy.
Novelli A; Laboratory of Medical Genetics, Bambino Gesù Children's Hospital, IRCCS, Rome, Italy.
Fiumara A; Referral Centre for Inherited Metabolic Diseases Policlinico, University of Catania, Catania, Italy.
Jaeken J; Center for Metabolic Diseases, UZ and KU Leuven, Leuven, Belgium.
Barone R; CNR, Institute for Polymers, Composites and Biomaterials, IPCB, Catania, Italy. .; Child Neurology and Psychiatry, Department of Clinical and Experimental Medicine, University of Catania, Catania, Italy. .
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Źródło :
Glycoconjugate journal [Glycoconj J] 2019 Dec; Vol. 36 (6), pp. 461-472. Date of Electronic Publication: 2019 Sep 16.
Typ publikacji :
Journal Article
MeSH Terms :
Congenital Disorders of Glycosylation/*genetics
IgG Deficiency/*genetics
Immunoglobulins/*genetics
Mannosyltransferases/*genetics
Child ; Child, Preschool ; Congenital Disorders of Glycosylation/blood ; Congenital Disorders of Glycosylation/pathology ; Endoplasmic Reticulum/genetics ; Endoplasmic Reticulum/metabolism ; Female ; Glycoproteins/blood ; Glycosylation ; Humans ; IgG Deficiency/blood ; IgG Deficiency/metabolism ; IgG Deficiency/pathology ; Immunoglobulins/blood ; Immunoglobulins/deficiency ; Infant ; Male ; Mannosyltransferases/blood ; Oligosaccharides/genetics ; Oligosaccharides/metabolism ; Polysaccharides/genetics ; Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization ; Transferrin/genetics ; Transferrin/metabolism ; Whole Exome Sequencing
SCR Disease Name :
Congenital disorder of glycosylation type 1G; Congenital disorder of glycosylation type II
Czasopismo naukowe
Tytuł :
A Family of Dual-Activity Glycosyltransferase-Phosphorylases Mediates Mannogen Turnover and Virulence in Leishmania Parasites.
Autorzy :
Sernee MF; Department of Biochemistry and Molecular Biology, Bio21 Molecular Science and Biotechnology Institute, University of Melbourne, Parkville, VIC 3010, Australia.
Ralton JE; Department of Biochemistry and Molecular Biology, Bio21 Molecular Science and Biotechnology Institute, University of Melbourne, Parkville, VIC 3010, Australia.
Nero TL; Department of Biochemistry and Molecular Biology, Bio21 Molecular Science and Biotechnology Institute, University of Melbourne, Parkville, VIC 3010, Australia; ACRF Rational Drug Discovery Centre, St. Vincent's Institute of Medical Research, Fitzroy, VIC 3065, Australia.
Sobala LF; Department of Chemistry, University of York, York YO10 5DD, UK.
Kloehn J; Department of Biochemistry and Molecular Biology, Bio21 Molecular Science and Biotechnology Institute, University of Melbourne, Parkville, VIC 3010, Australia.
Vieira-Lara MA; Department of Biochemistry and Molecular Biology, Bio21 Molecular Science and Biotechnology Institute, University of Melbourne, Parkville, VIC 3010, Australia.
Cobbold SA; Department of Biochemistry and Molecular Biology, Bio21 Molecular Science and Biotechnology Institute, University of Melbourne, Parkville, VIC 3010, Australia.
Stanton L; Department of Biochemistry and Molecular Biology, Bio21 Molecular Science and Biotechnology Institute, University of Melbourne, Parkville, VIC 3010, Australia.
Pires DEV; Department of Biochemistry and Molecular Biology, Bio21 Molecular Science and Biotechnology Institute, University of Melbourne, Parkville, VIC 3010, Australia.
Hanssen E; Department of Biochemistry and Molecular Biology, Bio21 Molecular Science and Biotechnology Institute, University of Melbourne, Parkville, VIC 3010, Australia; Advanced Microscopy Facility, Bio21 Molecular Science and Biotechnology Institute, University of Melbourne, Parkville, VIC 3010, Australia.
Males A; Department of Chemistry, University of York, York YO10 5DD, UK.
Ward T; Department of Chemistry, University of York, York YO10 5DD, UK.
Bastidas LM; Department of Chemistry, University of York, York YO10 5DD, UK.
van der Peet PL; School of Chemistry, Bio21 Molecular Science and Biotechnology Institute, University of Melbourne, Parkville, VIC 3010, Australia.
Parker MW; Department of Biochemistry and Molecular Biology, Bio21 Molecular Science and Biotechnology Institute, University of Melbourne, Parkville, VIC 3010, Australia; ACRF Rational Drug Discovery Centre, St. Vincent's Institute of Medical Research, Fitzroy, VIC 3065, Australia.
Ascher DB; Department of Biochemistry and Molecular Biology, Bio21 Molecular Science and Biotechnology Institute, University of Melbourne, Parkville, VIC 3010, Australia.
Williams SJ; School of Chemistry, Bio21 Molecular Science and Biotechnology Institute, University of Melbourne, Parkville, VIC 3010, Australia.
Davies GJ; Department of Chemistry, University of York, York YO10 5DD, UK.
McConville MJ; Department of Biochemistry and Molecular Biology, Bio21 Molecular Science and Biotechnology Institute, University of Melbourne, Parkville, VIC 3010, Australia. Electronic address: .
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Źródło :
Cell host & microbe [Cell Host Microbe] 2019 Sep 11; Vol. 26 (3), pp. 385-399.e9.
Typ publikacji :
Journal Article
MeSH Terms :
Glycosyltransferases/*classification
Glycosyltransferases/*metabolism
Leishmania/*enzymology
Mannosyltransferases/*metabolism
Phosphorylases/*classification
Phosphorylases/*metabolism
Crystallography, X-Ray ; Gene Transfer, Horizontal ; Glycosyltransferases/chemistry ; Glycosyltransferases/genetics ; Mannans ; Mannosyltransferases/chemistry ; Mannosyltransferases/genetics ; Models, Molecular ; Oligosaccharides ; Phosphorylases/chemistry ; Phosphorylases/genetics ; Protein Conformation ; Thermotolerance ; Virulence
Czasopismo naukowe
Tytuł :
Structure of the eukaryotic protein O-mannosyltransferase Pmt1-Pmt2 complex.
Autorzy :
Bai L; Structural Biology Program, Van Andel Research Institute, Grand Rapids, MI, USA.
Kovach A; Structural Biology Program, Van Andel Research Institute, Grand Rapids, MI, USA.
You Q; Structural Biology Program, Van Andel Research Institute, Grand Rapids, MI, USA.
Kenny A; Structural Biology Program, Van Andel Research Institute, Grand Rapids, MI, USA.
Li H; Structural Biology Program, Van Andel Research Institute, Grand Rapids, MI, USA. .
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Źródło :
Nature structural & molecular biology [Nat Struct Mol Biol] 2019 Aug; Vol. 26 (8), pp. 704-711. Date of Electronic Publication: 2019 Jul 08.
Typ publikacji :
Journal Article; Research Support, N.I.H., Extramural; Research Support, Non-U.S. Gov't; Video-Audio Media
MeSH Terms :
Mannosyltransferases/*ultrastructure
Multienzyme Complexes/*ultrastructure
Saccharomyces cerevisiae/*enzymology
Saccharomyces cerevisiae Proteins/*ultrastructure
Cryoelectron Microscopy ; Glycosylation ; Humans ; Image Processing, Computer-Assisted ; Mannose/metabolism ; Mannosyltransferases/chemistry ; Mannosyltransferases/genetics ; Mannosyltransferases/metabolism ; Models, Molecular ; Multienzyme Complexes/chemistry ; Multienzyme Complexes/metabolism ; Protein Conformation ; Protein Domains ; Protein Folding ; Protein Processing, Post-Translational ; Recombinant Proteins/chemistry ; Recombinant Proteins/metabolism ; Saccharomyces cerevisiae Proteins/chemistry ; Saccharomyces cerevisiae Proteins/metabolism ; Species Specificity ; Substrate Specificity ; Walker-Warburg Syndrome/genetics
Czasopismo naukowe
Tytuł :
Svp26 facilitates ER exit of mannosyltransferases Mnt2 and Mnt3 in Saccharomyces cerevisiae.
Autorzy :
Tanabe Y; Department of Biotechnology, The University of Tokyo.; Department of Applied Biological Science, Tokyo University of Science.
Arai S; Department of Cell Science, Institute of Biomedical Sciences, Fukushima Medical University School of Medicine.
Wada I; Department of Cell Science, Institute of Biomedical Sciences, Fukushima Medical University School of Medicine.
Adachi H; Department of Biotechnology, The University of Tokyo.; Collaborative Research Institute for Innovative Microbiology, The University of Tokyo.
Kamakura T; Department of Applied Biological Science, Tokyo University of Science.
Yoda K; Department of Biotechnology, The University of Tokyo.
Noda Y; Department of Biotechnology, The University of Tokyo.; Collaborative Research Institute for Innovative Microbiology, The University of Tokyo.
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Źródło :
The Journal of general and applied microbiology [J Gen Appl Microbiol] 2019 Sep 14; Vol. 65 (4), pp. 180-187. Date of Electronic Publication: 2019 Jan 31.
Typ publikacji :
Journal Article
MeSH Terms :
Endoplasmic Reticulum/*physiology
Mannosyltransferases/*metabolism
Saccharomyces cerevisiae/*enzymology
Saccharomyces cerevisiae Proteins/*metabolism
Vesicular Transport Proteins/*metabolism
Biological Transport ; Golgi Apparatus/physiology ; Mannosyltransferases/genetics ; Protein Binding ; Saccharomyces cerevisiae/genetics ; Saccharomyces cerevisiae Proteins/genetics ; Vesicular Transport Proteins/genetics
Czasopismo naukowe
Tytuł :
Toward understanding tissue-specific symptoms in dolichol-phosphate-mannose synthesis disorders; insight from DPM3-CDG.
Autorzy :
van Tol W; Department of Neurology, Donders Institute for Brain, Cognition and Behavior, Radboud University Medical Center, Nijmegen, The Netherlands.; Translational Metabolic Laboratory, Department of Laboratory Medicine, Radboud Institute for Molecular Life Sciences, Radboud University Medical Center, Nijmegen, The Netherlands.
Michelakakis H; Department of Enzymology and Cellular Function, Institute of Child Health, Athens, Greece.
Georgiadou E; First Department of Pediatrics, University of Athens, Aghia Sophia Children's Hospital, Athens, Greece.
van den Bergh P; Neuromuscular Reference Center, University Hospital St-Luc, University of Louvain, Brussels, Belgium.
Moraitou M; Department of Enzymology and Cellular Function, Institute of Child Health, Athens, Greece.
Papadimas GK; First Department of Neurology, Eginition Hospital, Medical School, National and Kapodistrian University of Athens, Athens, Greece.
Papadopoulos C; First Department of Neurology, Eginition Hospital, Medical School, National and Kapodistrian University of Athens, Athens, Greece.
Huijben K; Translational Metabolic Laboratory, Department of Laboratory Medicine, Radboud Institute for Molecular Life Sciences, Radboud University Medical Center, Nijmegen, The Netherlands.
Alsady M; Department of Neurology, Donders Institute for Brain, Cognition and Behavior, Radboud University Medical Center, Nijmegen, The Netherlands.
Willemsen MA; Department of Pediatric Neurology, Amalia Children's Hospital, Donders Institute for Brain, Cognition and Behavior, Radboud University Medical Center, Nijmegen, The Netherlands.
Lefeber DJ; Department of Neurology, Donders Institute for Brain, Cognition and Behavior, Radboud University Medical Center, Nijmegen, The Netherlands.; Translational Metabolic Laboratory, Department of Laboratory Medicine, Radboud Institute for Molecular Life Sciences, Radboud University Medical Center, Nijmegen, The Netherlands.
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Źródło :
Journal of inherited metabolic disease [J Inherit Metab Dis] 2019 Sep; Vol. 42 (5), pp. 984-992. Date of Electronic Publication: 2019 Apr 23.
Typ publikacji :
Journal Article; Research Support, Non-U.S. Gov't
MeSH Terms :
Congenital Disorders of Glycosylation/*diagnosis
Congenital Disorders of Glycosylation/*genetics
Mannosyltransferases/*genetics
Membrane Proteins/*genetics
Muscular Dystrophies/*diagnosis
Adult ; Biopsy ; Child ; Dystroglycans/genetics ; Dystroglycans/metabolism ; Female ; Glycosylation ; Humans ; Male ; Mannosyltransferases/metabolism ; Membrane Proteins/metabolism ; Middle Aged ; Muscle, Skeletal/pathology ; Mutation ; Phenotype
Czasopismo naukowe
Tytuł :
The α-1,6-mannosyltransferase VdOCH1 plays a major role in microsclerotium formation and virulence in the soil-borne pathogen Verticillium dahliae.
Autorzy :
Zhang J; College of Horticulture and Plant Protection, Inner Mongolia Agricultural University, Hohhot, China.
Zhang Y; College of Horticulture and Plant Protection, Inner Mongolia Agricultural University, Hohhot, China.
Yang J; College of Horticulture and Plant Protection, Inner Mongolia Agricultural University, Hohhot, China.
Kang L; College of Horticulture and Plant Protection, Inner Mongolia Agricultural University, Hohhot, China.
EloRM AM; College of Horticulture and Plant Protection, Inner Mongolia Agricultural University, Hohhot, China.
Zhou H; College of Horticulture and Plant Protection, Inner Mongolia Agricultural University, Hohhot, China.
Zhao J; College of Horticulture and Plant Protection, Inner Mongolia Agricultural University, Hohhot, China. Electronic address: .
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Źródło :
Fungal biology [Fungal Biol] 2019 Jul; Vol. 123 (7), pp. 539-546. Date of Electronic Publication: 2019 May 18.
Typ publikacji :
Journal Article; Research Support, Non-U.S. Gov't
MeSH Terms :
Fungal Proteins/*metabolism
Mannosyltransferases/*metabolism
Verticillium/*enzymology
Verticillium/*pathogenicity
Cell Wall/metabolism ; Fungal Proteins/genetics ; Genetic Complementation Test ; Helianthus/microbiology ; Mannosyltransferases/genetics ; Mutagenesis, Insertional ; Plant Diseases/microbiology ; Sequence Deletion ; Soil Microbiology ; Spores, Fungal/genetics ; Spores, Fungal/growth & development ; Verticillium/genetics ; Verticillium/growth & development ; Virulence
Czasopismo naukowe
Tytuł :
Aspergillus fumigatus Mnn9 is responsible for mannan synthesis and required for covalent linkage of mannoprotein to the cell wall.
Autorzy :
Du T; State Key Laboratory of Mycology, Institute of Microbiology, Chinese Academy of Sciences, Beijing 100101, China; University of Chinese Academy of Sciences, Beijing, China.
Ouyang H; State Key Laboratory of Mycology, Institute of Microbiology, Chinese Academy of Sciences, Beijing 100101, China.
Voglmeir J; Department of Chemistry, University of Natural Resources and Life Sciences, Vienna A-1190, Austria.
Wilson IBH; Department of Chemistry, University of Natural Resources and Life Sciences, Vienna A-1190, Austria.
Jin C; State Key Laboratory of Mycology, Institute of Microbiology, Chinese Academy of Sciences, Beijing 100101, China; Guangxi Academy of Sciences, Nanning 530007, Guangxi, China. Electronic address: .
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Źródło :
Fungal genetics and biology : FG & B [Fungal Genet Biol] 2019 Jul; Vol. 128, pp. 20-28. Date of Electronic Publication: 2019 Mar 20.
Typ publikacji :
Journal Article; Research Support, Non-U.S. Gov't
MeSH Terms :
Aspergillus fumigatus/*enzymology
Mannans/*biosynthesis
Mannosyltransferases/*metabolism
Membrane Glycoproteins/*metabolism
Aspergillus fumigatus/genetics ; Benzenesulfonates ; Cell Wall/metabolism ; Congo Red ; Gene Deletion ; Hygromycin B ; Mannosyltransferases/genetics
Czasopismo naukowe

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