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  1. Article ; Online: Multiple tissue-specific roles for the O-GlcNAc post-translational modification in the induction of and complications arising from type II diabetes.

    Vaidyanathan, Krithika / Wells, Lance

    The Journal of biological chemistry

    2014  Volume 289, Issue 50, Page(s) 34466–34471

    Abstract: In this minireview, we will highlight work in the last 30 years that has clearly demonstrated that the O-GlcNAc modification is nutrient-responsive and plays multiple roles in metabolic regulation of signaling and gene expression. Further, we will ... ...

    Abstract In this minireview, we will highlight work in the last 30 years that has clearly demonstrated that the O-GlcNAc modification is nutrient-responsive and plays multiple roles in metabolic regulation of signaling and gene expression. Further, we will examine recent studies that have investigated the impact of O-GlcNAc in a variety of glucose- and insulin-responsive tissues and the roles attributed to O-GlcNAc in the induction of insulin resistance and glucose toxicity, the hallmarks of type II diabetes mellitus. We will also summarize potential causal roles for the O-GlcNAc modification in complications associated with diabetes.
    MeSH term(s) Acetylglucosamine/metabolism ; Animals ; Diabetes Mellitus, Type 2/complications ; Diabetes Mellitus, Type 2/metabolism ; Diabetes Mellitus, Type 2/pathology ; Humans ; Insulin/metabolism ; Organ Specificity ; Protein Processing, Post-Translational ; Signal Transduction
    Chemical Substances Insulin ; Acetylglucosamine (V956696549)
    Language English
    Publishing date 2014-10-21
    Publishing country United States
    Document type Journal Article ; Research Support, N.I.H., Extramural ; Review
    ZDB-ID 2997-x
    ISSN 1083-351X ; 0021-9258
    ISSN (online) 1083-351X
    ISSN 0021-9258
    DOI 10.1074/jbc.R114.591560
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  2. Article ; Online: O-GlcNAc transferase regulates transcriptional activity of human Oct4.

    Constable, Sandii / Lim, Jae-Min / Vaidyanathan, Krithika / Wells, Lance

    Glycobiology

    2017  Volume 27, Issue 10, Page(s) 927–937

    Abstract: O-linked β-N-acetylglucosamine (O-GlcNAc) is a single sugar modification found on many different classes of nuclear and cytoplasmic proteins. Addition of this modification, by the enzyme O-linked N-acetylglucosamine transferase (OGT), is dynamic and ... ...

    Abstract O-linked β-N-acetylglucosamine (O-GlcNAc) is a single sugar modification found on many different classes of nuclear and cytoplasmic proteins. Addition of this modification, by the enzyme O-linked N-acetylglucosamine transferase (OGT), is dynamic and inducible. One major class of proteins modified by O-GlcNAc is transcription factors. O-GlcNAc regulates transcription factor properties through a variety of different mechanisms including localization, stability and transcriptional activation. Maintenance of embryonic stem (ES) cell pluripotency requires tight regulation of several key transcription factors, many of which are modified by O-GlcNAc. Octamer-binding protein 4 (Oct4) is one of the key transcription factors required for pluripotency of ES cells and more recently, the generation of induced pluripotent stem (iPS) cells. The action of Oct4 is modulated by the addition of several post-translational modifications, including O-GlcNAc. Previous studies in mice found a single site of O-GlcNAc addition responsible for transcriptional regulation. This study was designed to determine if this mechanism is conserved in humans. We mapped 10 novel sites of O-GlcNAc attachment on human Oct4, and confirmed a role for OGT in transcriptional activation of Oct4 at a site distinct from that found in mouse that allows distinction between different Oct4 target promoters. Additionally, we uncovered a potential new role for OGT that does not include its catalytic function. These results confirm that human Oct4 activity is being regulated by OGT by a mechanism that is distinct from mouse Oct4.
    MeSH term(s) Embryonic Stem Cells/metabolism ; Glycosylation ; HEK293 Cells ; Humans ; N-Acetylglucosaminyltransferases/metabolism ; Octamer Transcription Factor-3/metabolism ; Protein Processing, Post-Translational ; Transcriptional Activation
    Chemical Substances Octamer Transcription Factor-3 ; POU5F1 protein, human ; N-Acetylglucosaminyltransferases (EC 2.4.1.-)
    Language English
    Publishing date 2017-09-18
    Publishing country England
    Document type Journal Article ; Research Support, N.I.H., Extramural ; Research Support, Non-U.S. Gov't
    ZDB-ID 1067689-2
    ISSN 1460-2423 ; 0959-6658
    ISSN (online) 1460-2423
    ISSN 0959-6658
    DOI 10.1093/glycob/cwx055
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  3. Article ; Online: Functional O-GlcNAc modifications: implications in molecular regulation and pathophysiology.

    Vaidyanathan, Krithika / Durning, Sean / Wells, Lance

    Critical reviews in biochemistry and molecular biology

    2014  Volume 49, Issue 2, Page(s) 140–163

    Abstract: O-linked β-N-acetylglucosamine (O-GlcNAc) is a regulatory post-translational modification of intracellular proteins. The dynamic and inducible cycling of the modification is governed by O-GlcNAc transferase (OGT) and O-GlcNAcase (OGA) in response to UDP- ... ...

    Abstract O-linked β-N-acetylglucosamine (O-GlcNAc) is a regulatory post-translational modification of intracellular proteins. The dynamic and inducible cycling of the modification is governed by O-GlcNAc transferase (OGT) and O-GlcNAcase (OGA) in response to UDP-GlcNAc levels in the hexosamine biosynthetic pathway (HBP). Due to its reliance on glucose flux and substrate availability, a major focus in the field has been on how O-GlcNAc contributes to metabolic disease. For years this post-translational modification has been known to modify thousands of proteins implicated in various disorders, but direct functional connections have until recently remained elusive. New research is beginning to reveal the specific mechanisms through which O-GlcNAc influences cell dynamics and disease pathology including clear examples of O-GlcNAc modification at a specific site on a given protein altering its biological functions. The following review intends to focus primarily on studies in the last half decade linking O-GlcNAc modification of proteins with chromatin-directed gene regulation, developmental processes, and several metabolically related disorders including Alzheimer's, heart disease and cancer. These studies illustrate the emerging importance of this post-translational modification in biological processes and multiple pathophysiologies.
    MeSH term(s) Acetylglucosamine/genetics ; Acetylglucosamine/metabolism ; Alzheimer Disease/genetics ; Alzheimer Disease/metabolism ; Animals ; Chromatin/genetics ; Chromatin/metabolism ; Gene Expression Regulation ; Heart Diseases/genetics ; Heart Diseases/metabolism ; Humans ; Metabolic Diseases/genetics ; Metabolic Diseases/metabolism ; N-Acetylglucosaminyltransferases/genetics ; N-Acetylglucosaminyltransferases/metabolism ; Neoplasms/genetics ; Neoplasms/metabolism ; Protein Processing, Post-Translational ; Proteins/genetics ; Proteins/metabolism ; beta-N-Acetylhexosaminidases/genetics ; beta-N-Acetylhexosaminidases/metabolism
    Chemical Substances Chromatin ; Proteins ; N-Acetylglucosaminyltransferases (EC 2.4.1.-) ; O-GlcNAc transferase (EC 2.4.1.-) ; hexosaminidase C (EC 3.2.1.50) ; beta-N-Acetylhexosaminidases (EC 3.2.1.52) ; Acetylglucosamine (V956696549)
    Language English
    Publishing date 2014-02-14
    Publishing country England
    Document type Journal Article ; Research Support, N.I.H., Extramural ; Review
    ZDB-ID 1000977-2
    ISSN 1549-7798 ; 1381-3455 ; 1040-9238
    ISSN (online) 1549-7798
    ISSN 1381-3455 ; 1040-9238
    DOI 10.3109/10409238.2014.884535
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  4. Article: Health-Related Quality of Life Improvements in Moderate to Very Severe Chronic Obstructive Pulmonary Disease Patients on Nebulized Glycopyrrolate: Evidence from the GOLDEN Studies.

    Ferguson, Gary T / Kerwin, Edward M / Donohue, James F / Ganapathy, Vaidyanathan / Tosiello, Robert L / Bollu, Vamsi K / Rajagopalan, Krithika

    Chronic obstructive pulmonary diseases (Miami, Fla.)

    2018  Volume 5, Issue 3, Page(s) 193–207

    Abstract: Background: ...

    Abstract Background:
    Language English
    Publishing date 2018-06-06
    Publishing country United States
    Document type Journal Article
    ZDB-ID 2771715-X
    ISSN 2372-952X
    ISSN 2372-952X
    DOI 10.15326/jcopdf.5.3.2017.0178
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  5. Article ; Online: Satisfaction with the Use of eFlow Closed-System Nebulizer in Patients with Moderate-to-Very Severe Chronic Obstructive Pulmonary Disease: Findings from a Long-Term Safety Study.

    Kerwin, Edward M / Donohue, James F / Ferguson, Gary T / Ganapathy, Vaidyanathan / Ozol-Godfrey, Ayca / Rajagopalan, Krithika

    Journal of aerosol medicine and pulmonary drug delivery

    2018  Volume 32, Issue 1, Page(s) 24–33

    Abstract: Background: Effective delivery of inhaled drugs in chronic obstructive pulmonary disease (COPD) depends on patients' ability to correctly use an inhalation device. Nebulized delivery may be appropriate for COPD patients who cannot coordinate breath with ...

    Abstract Background: Effective delivery of inhaled drugs in chronic obstructive pulmonary disease (COPD) depends on patients' ability to correctly use an inhalation device. Nebulized delivery may be appropriate for COPD patients who cannot coordinate breath with inhalation or generate adequate inhalational force. Until recently, long-acting muscarinic antagonists (LAMAs), used for maintenance treatment of COPD, were available for delivery only via handheld inhalers. Lonhala™ Magnair™ (glycopyrrolate inhalation solution) is a LAMA delivered via the eFlow
    Methods: GOLDEN-5, a phase 3, randomized, open-label trial, evaluated the safety and efficacy of glycopyrrolate/eFlow CS 50 μg twice daily versus tiotropium 18 μg once daily (administered via HandiHaler™) in patients with moderate-to-very severe COPD. Only patients in the glycopyrrolate/eFlow CS group completed a study-specific device use questionnaire, evaluating patients' perceptions about ease of use, confidence in drug delivery, and overall device satisfaction at week 48 or end of study. Responses were summarized by counts and percentages.
    Results: Of 620 patients who received glycopyrrolate/eFlow CS, 454 completed the questionnaire (mean age [standard deviation, SD] 63.3 [8.5] years; mean BMI [SD] 28.45 [6.208] kg/m
    Conclusions: High levels of satisfaction, confidence, and ease of use were reported with the eFlow CS nebulizer in this study. These findings support the use of the eFlow CS for maintenance treatment of COPD with glycopyrrolate inhalation solution.
    MeSH term(s) Administration, Inhalation ; Aged ; Bronchodilator Agents/administration & dosage ; Bronchodilator Agents/adverse effects ; Equipment Design ; Female ; Glycopyrrolate/administration & dosage ; Glycopyrrolate/adverse effects ; Humans ; Lung/drug effects ; Lung/physiopathology ; Male ; Middle Aged ; Muscarinic Antagonists/administration & dosage ; Muscarinic Antagonists/adverse effects ; Nebulizers and Vaporizers ; Patient Satisfaction ; Pulmonary Disease, Chronic Obstructive/diagnosis ; Pulmonary Disease, Chronic Obstructive/drug therapy ; Pulmonary Disease, Chronic Obstructive/physiopathology ; Severity of Illness Index ; Time Factors ; Tiotropium Bromide/administration & dosage ; Treatment Outcome
    Chemical Substances Bronchodilator Agents ; Muscarinic Antagonists ; Glycopyrrolate (V92SO9WP2I) ; Tiotropium Bromide (XX112XZP0J)
    Language English
    Publishing date 2018-11-17
    Publishing country United States
    Document type Clinical Trial, Phase III ; Journal Article ; Multicenter Study ; Randomized Controlled Trial ; Research Support, Non-U.S. Gov't
    ZDB-ID 2417924-3
    ISSN 1941-2703 ; 1941-2711
    ISSN (online) 1941-2703
    ISSN 1941-2711
    DOI 10.1089/jamp.2018.1477
    Database MEDical Literature Analysis and Retrieval System OnLINE

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    Zs.A 2460: Show issues Location:
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  6. Article ; Online: Identification and characterization of a missense mutation in the

    Vaidyanathan, Krithika / Niranjan, Tejasvi / Selvan, Nithya / Teo, Chin Fen / May, Melanie / Patel, Sneha / Weatherly, Brent / Skinner, Cindy / Opitz, John / Carey, John / Viskochil, David / Gecz, Jozef / Shaw, Marie / Peng, Yunhui / Alexov, Emil / Wang, Tao / Schwartz, Charles / Wells, Lance

    The Journal of biological chemistry

    2017  Volume 292, Issue 21, Page(s) 8948–8963

    Abstract: ... ...

    Abstract O
    MeSH term(s) Amino Acid Substitution ; Cell Line, Transformed ; Chromosomes, Human, X ; Gene Expression Regulation, Enzymologic ; Glycosylation ; Humans ; Male ; Mental Retardation, X-Linked/enzymology ; Mental Retardation, X-Linked/genetics ; Mental Retardation, X-Linked/pathology ; Mutation, Missense ; N-Acetylglucosaminyltransferases/genetics ; N-Acetylglucosaminyltransferases/metabolism ; Protein Processing, Post-Translational ; RNA, Messenger/biosynthesis ; RNA, Messenger/genetics
    Chemical Substances RNA, Messenger ; N-Acetylglucosaminyltransferases (EC 2.4.1.-) ; O-GlcNAc transferase (EC 2.4.1.-)
    Language English
    Publishing date 2017-03-16
    Publishing country United States
    Document type Journal Article ; Research Support, N.I.H., Extramural ; Research Support, Non-U.S. Gov't
    ZDB-ID 2997-x
    ISSN 1083-351X ; 0021-9258
    ISSN (online) 1083-351X
    ISSN 0021-9258
    DOI 10.1074/jbc.M116.771030
    Database MEDical Literature Analysis and Retrieval System OnLINE

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