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  1. Article ; Online: Picobirnaviruses in animals: a review

    Reddy, Mareddy Vineetha / Gupta, Vandana / Nayak, Anju / Tiwari, Sita Prasad

    Mol Biol Rep. 2023 Feb., v. 50, no. 2 p.1785-1797

    2023  

    Abstract: Picobirnaviruses (PBVs) are small non enveloped viruses with bi-segmented ds RNA. They have been observed in a wide variety of vertebrates, including mammals and birds with or without diarrhoea, as well as in sewage samples since its discovery (1988). ... ...

    Abstract Picobirnaviruses (PBVs) are small non enveloped viruses with bi-segmented ds RNA. They have been observed in a wide variety of vertebrates, including mammals and birds with or without diarrhoea, as well as in sewage samples since its discovery (1988). The source of the viruses is uncertain. True hosts of PBVs and their role as primary pathogens or secondary opportunistic agents or innocuous viruses in the gut remains alien. The mechanisms by which they play a role in pathogenicity are still unclear based on the fact that they can be found in both symptomatic and asymptomatic cases. There is a need to determine their tropism since they have not only been associated with viral gastroenteritis but also been reported in the respiratory tracts of pigs. As zoonotic agents with diverse hosts, the importance of epidemiological and surveillance studies cannot be overstated. The segmented genome of PBV might pose a serious public health issue because of the possibility of continuous genetic reassortment. Aware of the growing attention being given to emerging RNA viruses, we reviewed the current knowledge on PBVs and described the current status of PBVs in animals.
    Keywords Picobirnavirus ; RNA ; diarrhea ; digestive system ; genome ; monitoring ; pathogenicity ; public health ; sewage ; viral gastroenteritis
    Language English
    Dates of publication 2023-02
    Size p. 1785-1797.
    Publishing place Springer Netherlands
    Document type Article ; Online
    Note Review
    ZDB-ID 186544-4
    ISSN 1573-4978 ; 0301-4851
    ISSN (online) 1573-4978
    ISSN 0301-4851
    DOI 10.1007/s11033-022-08133-2
    Database NAL-Catalogue (AGRICOLA)

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  2. Article ; Online: Picobirnaviruses in animals: a review.

    Reddy, Mareddy Vineetha / Gupta, Vandana / Nayak, Anju / Tiwari, Sita Prasad

    Molecular biology reports

    2022  Volume 50, Issue 2, Page(s) 1785–1797

    Abstract: Picobirnaviruses (PBVs) are small non enveloped viruses with bi-segmented ds RNA. They have been observed in a wide variety of vertebrates, including mammals and birds with or without diarrhoea, as well as in sewage samples since its discovery (1988). ... ...

    Abstract Picobirnaviruses (PBVs) are small non enveloped viruses with bi-segmented ds RNA. They have been observed in a wide variety of vertebrates, including mammals and birds with or without diarrhoea, as well as in sewage samples since its discovery (1988). The source of the viruses is uncertain. True hosts of PBVs and their role as primary pathogens or secondary opportunistic agents or innocuous viruses in the gut remains alien. The mechanisms by which they play a role in pathogenicity are still unclear based on the fact that they can be found in both symptomatic and asymptomatic cases. There is a need to determine their tropism since they have not only been associated with viral gastroenteritis but also been reported in the respiratory tracts of pigs. As zoonotic agents with diverse hosts, the importance of epidemiological and surveillance studies cannot be overstated. The segmented genome of PBV might pose a serious public health issue because of the possibility of continuous genetic reassortment. Aware of the growing attention being given to emerging RNA viruses, we reviewed the current knowledge on PBVs and described the current status of PBVs in animals.
    MeSH term(s) Animals ; Swine ; Picobirnavirus/genetics ; Phylogeny ; RNA Virus Infections/veterinary ; RNA Virus Infections/epidemiology ; Feces ; Diarrhea ; Mammals
    Language English
    Publishing date 2022-12-03
    Publishing country Netherlands
    Document type Journal Article ; Review
    ZDB-ID 186544-4
    ISSN 1573-4978 ; 0301-4851
    ISSN (online) 1573-4978
    ISSN 0301-4851
    DOI 10.1007/s11033-022-08133-2
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  3. Article ; Online: Mbnl2 loss alters novel context processing and impairs object recognition memory.

    Khandelwal, Abinash / Cushman, Jesse / Choi, Jongkyu / Zhuravka, Irina / Rajbhandari, Abha / Valiulahi, Parvin / Li, Xiandu / Zhou, Chenyu / Comai, Lucio / Reddy, Sita

    iScience

    2023  Volume 26, Issue 5, Page(s) 106732

    Abstract: Patients with myotonic dystrophy type I (DM1) demonstrate visuospatial dysfunction and impaired performance in tasks requiring recognition or memory of figures and objects. In DM1, CUG expansion RNAs inactivate the muscleblind-like (MBNL) proteins. We ... ...

    Abstract Patients with myotonic dystrophy type I (DM1) demonstrate visuospatial dysfunction and impaired performance in tasks requiring recognition or memory of figures and objects. In DM1, CUG expansion RNAs inactivate the muscleblind-like (MBNL) proteins. We show that constitutive Mbnl2 inactivation in
    Language English
    Publishing date 2023-04-25
    Publishing country United States
    Document type Journal Article
    ISSN 2589-0042
    ISSN (online) 2589-0042
    DOI 10.1016/j.isci.2023.106732
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  4. Article: Navigating Complexity: A Rare Case of Down Syndrome With Dural Venous Thrombosis in a Neonate.

    Damam, SreeHarsha / Meshram, Revat J / Taksande, Amar / Karotkar, Sagar / Lakra, Mahaveer S / Rawat, Aditi / Khurana, Astha / Javvaji, Chaitanya Kumar / Reddy, Naramreddy Sudheesh / K, Sri Sita Naga Sai Priya

    Cureus

    2024  Volume 16, Issue 1, Page(s) e52982

    Abstract: This case report presents a unique clinical scenario of a 2 kg male neonate with Down syndrome complicated by dural venous thrombosis. Born via normal vaginal delivery, the infant exhibited syndromic features characteristic of Down syndrome, ... ...

    Abstract This case report presents a unique clinical scenario of a 2 kg male neonate with Down syndrome complicated by dural venous thrombosis. Born via normal vaginal delivery, the infant exhibited syndromic features characteristic of Down syndrome, necessitating admission to the neonatal intensive care unit (NICU) for respiratory distress. Confirmatory karyotyping established the diagnosis. Subsequent complications included germinal matrix haemorrhage, hypoxic-ischemic encephalopathy, and aspiration pneumonia. An MRI revealed dural venous thrombosis in the left transverse sinus, an uncommon manifestation in neonates with Down syndrome. Multidisciplinary management involved respiratory support, antibiotic therapy, and neurophysiotherapy. Infectious complications, including
    Language English
    Publishing date 2024-01-26
    Publishing country United States
    Document type Case Reports
    ZDB-ID 2747273-5
    ISSN 2168-8184
    ISSN 2168-8184
    DOI 10.7759/cureus.52982
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  5. Article: Recent advances in understanding the role of lamins in health and disease.

    Reddy, Sita / Comai, Lucio

    F1000Research

    2016  Volume 5, Page(s) 2536

    Abstract: Lamins are major components of the nuclear lamina, a network of proteins that supports the nuclear envelope in metazoan cells. Over the past decade, biochemical studies have provided support for the view that lamins are not passive bystanders providing ... ...

    Abstract Lamins are major components of the nuclear lamina, a network of proteins that supports the nuclear envelope in metazoan cells. Over the past decade, biochemical studies have provided support for the view that lamins are not passive bystanders providing mechanical stability to the nucleus but play an active role in the organization of the genome and the function of fundamental nuclear processes. It has also become apparent that lamins are critical for human health, as a large number of mutations identified in the gene that encodes for A-type lamins are associated with tissue-specific and systemic genetic diseases, including the accelerated aging disorder known as Hutchinson-Gilford progeria syndrome. Recent years have witnessed great advances in our understanding of the role of lamins in the nucleus and the functional consequences of disease-associated A-type lamin mutations. Many of these findings have been presented in comprehensive reviews. In this mini-review, we discuss recent breakthroughs in the role of lamins in health and disease and what lies ahead in lamin research.
    Language English
    Publishing date 2016
    Publishing country England
    Document type Review ; Journal Article
    ZDB-ID 2699932-8
    ISSN 2046-1402
    ISSN 2046-1402
    DOI 10.12688/f1000research.9260.1
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  6. Article ; Online: Recent advances in understanding the role of lamins in health and disease [version 1; referees

    Sita Reddy / Lucio Comai

    F1000Research, Vol

    2 approved]

    2016  Volume 5

    Abstract: Lamins are major components of the nuclear lamina, a network of proteins that supports the nuclear envelope in metazoan cells. Over the past decade, biochemical studies have provided support for the view that lamins are not passive bystanders providing ... ...

    Abstract Lamins are major components of the nuclear lamina, a network of proteins that supports the nuclear envelope in metazoan cells. Over the past decade, biochemical studies have provided support for the view that lamins are not passive bystanders providing mechanical stability to the nucleus but play an active role in the organization of the genome and the function of fundamental nuclear processes. It has also become apparent that lamins are critical for human health, as a large number of mutations identified in the gene that encodes for A-type lamins are associated with tissue-specific and systemic genetic diseases, including the accelerated aging disorder known as Hutchinson-Gilford progeria syndrome. Recent years have witnessed great advances in our understanding of the role of lamins in the nucleus and the functional consequences of disease-associated A-type lamin mutations. Many of these findings have been presented in comprehensive reviews. In this mini-review, we discuss recent breakthroughs in the role of lamins in health and disease and what lies ahead in lamin research.
    Keywords Aging ; Cardiovascular Physiology/Circulation ; Cell Adhesion ; Cell Growth & Division ; Control of Gene Expression ; Cytoskeleton ; Developmental Molecular Mechanisms ; Medical Genetics ; Morphogenesis & Cell Biology ; Muscle & Connective Tissue ; Neurobiology of Disease & Regeneration ; Neurodevelopment ; Neuronal & Glial Cell Biology ; Nuclear Structure & Function ; Medicine ; R ; Science ; Q
    Language English
    Publishing date 2016-10-01T00:00:00Z
    Publisher F1000 Research Ltd
    Document type Article ; Online
    Database BASE - Bielefeld Academic Search Engine (life sciences selection)

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  7. Article: Gelastic seizures due to inferior frontal gyrus cavernoma.

    Jayalakshmi, Sita / Reddy, Rajesh / Vadapalli, Rammohan / Vooturi, Sudhindra / Panigrahi, Manas

    Neurology India

    2018  Volume 66, Issue 5, Page(s) 1503–1505

    MeSH term(s) Adult ; Brain Neoplasms/complications ; Brain Neoplasms/diagnostic imaging ; Brain Neoplasms/surgery ; Epilepsies, Partial/diagnostic imaging ; Epilepsies, Partial/etiology ; Epilepsies, Partial/surgery ; Humans ; Magnetic Resonance Imaging ; Male ; Prefrontal Cortex/diagnostic imaging ; Prefrontal Cortex/surgery
    Language English
    Publishing date 2018-09-19
    Publishing country India
    Document type Case Reports ; Letter
    ZDB-ID 415522-1
    ISSN 1998-4022 ; 0028-3886
    ISSN (online) 1998-4022
    ISSN 0028-3886
    DOI 10.4103/0028-3886.241351
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  8. Article ; Online: The Werner Syndrome Helicase Coordinates Sequential Strand Displacement and FEN1-Mediated Flap Cleavage during Polymerase δ Elongation.

    Li, Baomin / Reddy, Sita / Comai, Lucio

    Molecular and cellular biology

    2017  Volume 37, Issue 3

    Abstract: The Werner syndrome protein (WRN) suppresses the loss of telomeres replicated by lagging-strand synthesis by a yet to be defined mechanism. Here, we show that whereas either WRN or the Bloom syndrome helicase (BLM) stimulates DNA polymerase δ progression ...

    Abstract The Werner syndrome protein (WRN) suppresses the loss of telomeres replicated by lagging-strand synthesis by a yet to be defined mechanism. Here, we show that whereas either WRN or the Bloom syndrome helicase (BLM) stimulates DNA polymerase δ progression across telomeric G-rich repeats, only WRN promotes sequential strand displacement synthesis and FEN1 cleavage, a critical step in Okazaki fragment maturation, at these sequences. Helicase activity, as well as the conserved winged-helix (WH) motif and the helicase and RNase D C-terminal (HRDC) domain play important but distinct roles in this process. Remarkably, WRN also influences the formation of FEN1 cleavage products during strand displacement on a nontelomeric substrate, suggesting that WRN recruitment and cooperative interaction with FEN1 during lagging-strand synthesis may serve to regulate sequential strand displacement and flap cleavage at other genomic sites. These findings define a biochemical context for the physiological role of WRN in maintaining genetic stability.
    MeSH term(s) Amino Acid Motifs ; DNA/biosynthesis ; DNA Polymerase III/metabolism ; DNA Replication ; Flap Endonucleases/metabolism ; HeLa Cells ; Homeostasis ; Humans ; Polymerization ; Protein Domains ; RecQ Helicases/metabolism ; Repetitive Sequences, Nucleic Acid/genetics ; Substrate Specificity ; Telomere/metabolism ; Werner Syndrome Helicase/chemistry ; Werner Syndrome Helicase/metabolism
    Chemical Substances DNA (9007-49-2) ; DNA Polymerase III (EC 2.7.7.-) ; Flap Endonucleases (EC 3.1.-) ; FEN1 protein, human (EC 3.1.11.-) ; Bloom syndrome protein (EC 3.6.1.-) ; RecQ Helicases (EC 3.6.4.12) ; Werner Syndrome Helicase (EC 3.6.4.12)
    Language English
    Publishing date 2017-01-19
    Publishing country United States
    Document type Journal Article ; Research Support, N.I.H., Extramural
    ZDB-ID 779397-2
    ISSN 1098-5549 ; 0270-7306
    ISSN (online) 1098-5549
    ISSN 0270-7306
    DOI 10.1128/MCB.00560-16
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  9. Article ; Online: Mbnl1 and Mbnl2 regulate brain structural integrity in mice.

    Sta Maria, Naomi S / Zhou, Chenyu / Lee, Se Jung / Valiulahi, Parvin / Li, Xiandu / Choi, Jongkyu / Liu, Xiaodan / Jacobs, Russell / Comai, Lucio / Reddy, Sita

    Communications biology

    2021  Volume 4, Issue 1, Page(s) 1342

    Abstract: Myotonic Dystrophy Type I (DM1) patients demonstrate widespread and variable brain structural alterations whose etiology is unclear. We demonstrate that inactivation of the Muscleblind-like proteins, Mbnl1 and Mbnl2, initiates brain structural defects. ... ...

    Abstract Myotonic Dystrophy Type I (DM1) patients demonstrate widespread and variable brain structural alterations whose etiology is unclear. We demonstrate that inactivation of the Muscleblind-like proteins, Mbnl1 and Mbnl2, initiates brain structural defects. 2D FSE T2w MRIs on 4-month-old Mbnl1
    MeSH term(s) Animals ; Brain/pathology ; DNA-Binding Proteins/genetics ; DNA-Binding Proteins/metabolism ; Female ; Genotype ; Mice ; RNA-Binding Proteins/genetics ; RNA-Binding Proteins/metabolism
    Chemical Substances DNA-Binding Proteins ; MBNL2 protein, human ; Mbnl1 protein, mouse ; RNA-Binding Proteins
    Language English
    Publishing date 2021-11-30
    Publishing country England
    Document type Journal Article ; Research Support, N.I.H., Extramural
    ISSN 2399-3642
    ISSN (online) 2399-3642
    DOI 10.1038/s42003-021-02845-0
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  10. Article ; Online: The Werner Syndrome Helicase Coordinates Sequential Strand Displacement and FEN1-Mediated Flap Cleavage during Polymerase δ Elongation

    Li, Baomin / Reddy, Sita / Comai, Lucio

    Molecular and Cellular Biology. 2017 Feb. 1, v. 37, no. 3 p.e00560-16-

    2017  

    Abstract: The Werner syndrome protein (WRN) suppresses the loss of telomeres replicated by lagging-strand synthesis by a yet to be defined mechanism. Here, we show that whereas either WRN or the Bloom syndrome helicase (BLM) stimulates DNA polymerase δ progression ...

    Abstract The Werner syndrome protein (WRN) suppresses the loss of telomeres replicated by lagging-strand synthesis by a yet to be defined mechanism. Here, we show that whereas either WRN or the Bloom syndrome helicase (BLM) stimulates DNA polymerase δ progression across telomeric G-rich repeats, only WRN promotes sequential strand displacement synthesis and FEN1 cleavage, a critical step in Okazaki fragment maturation, at these sequences. Helicase activity, as well as the conserved winged-helix (WH) motif and the helicase and RNase D C-terminal (HRDC) domain play important but distinct roles in this process. Remarkably, WRN also influences the formation of FEN1 cleavage products during strand displacement on a nontelomeric substrate, suggesting that WRN recruitment and cooperative interaction with FEN1 during lagging-strand synthesis may serve to regulate sequential strand displacement and flap cleavage at other genomic sites. These findings define a biochemical context for the physiological role of WRN in maintaining genetic stability.
    Keywords DNA-directed DNA polymerase ; genetic stability ; genomics ; ribonucleases ; telomeres ; Werner syndrome ; DNA replication ; lagging-strand synthesis ; DNA helicase ; Okazaki fragment ; aging ; lagging strand
    Language English
    Dates of publication 2017-0201
    Publishing place Taylor & Francis
    Document type Article ; Online
    ZDB-ID 779397-2
    ISSN 1098-5549 ; 0270-7306
    ISSN (online) 1098-5549
    ISSN 0270-7306
    DOI 10.1128/MCB.00560-16
    Database NAL-Catalogue (AGRICOLA)

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