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  1. Book ; Online ; E-Book: Cellular Nanomachinesb

    Jena, Bhanu P.

    From Discovery to Structure-Function and Therapeutic Applications

    2020  

    Abstract: In this book, the major paradigm-shifting discoveries made in the past century on key cellular nanomachines are described in great detail: their complex yet precise and elegant design and function, as well as the diseases linked to their dysfunction and ... ...

    Author's details by Bhanu P. Jena
    Abstract In this book, the major paradigm-shifting discoveries made in the past century on key cellular nanomachines are described in great detail: their complex yet precise and elegant design and function, as well as the diseases linked to their dysfunction and the therapeutic approaches to overcome them. The major focus of this book is the “porosome” nanomachine, the universal secretory portal in cells. This is an ideal book for students, researchers, and professionals in the fields of nanoscience and nanotechnology.
    Keywords Cell biology ; Proteins  ; Microscopy ; Biochemistry ; Biophysics ; Biological physics ; Cell Biology ; Protein Science ; Biological Microscopy ; Animal Biochemistry ; Biological and Medical Physics, Biophysics ; Nanociència ; Nanotecnologia
    Subject code 621.3815
    Language English
    Size 1 online resource (118 pages)
    Edition 1st ed. 2020.
    Publisher Springer International Publishing ; Imprint: Springer
    Publishing place Cham
    Document type Book ; Online ; E-Book
    Remark Zugriff für angemeldete ZB MED-Nutzerinnen und -Nutzer
    ISBN 3-030-44496-1 ; 3-030-44495-3 ; 978-3-030-44496-9 ; 978-3-030-44495-2
    DOI 10.1007/978-3-030-44496-9
    Database ZB MED Catalogue: Medicine, Health, Nutrition, Environment, Agriculture

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  2. Book: Nanocellbiology of secretion

    Jena, Bhanu P.

    imaging its cellular and molecular underpinnings

    2012  

    Author's details Bhanu P. Jena
    Language English
    Size XII, 70 S. : Ill., graph. Darst.
    Publisher Springer
    Publishing place New York u.a.
    Publishing country United States
    Document type Book
    HBZ-ID HT017222052
    ISBN 978-1-4614-2437-6 ; 9781461424383 ; 1-4614-2437-2 ; 1461424380
    Database Catalogue ZB MED Medicine, Health

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    In stock of ZB MED Cologne/Königswinter

    Shelf markLoan statusLocation
    2012 A 1983 order for loan Magazin

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  3. Book: Nanocellbiology

    Jena, Bhanu P. / Taatjes, Douglas J.

    multimodal imaging in biology and medicine

    2014  

    Author's details ed. by Bhanu P. Jena and Douglas J. Taatjes
    Language English
    Size XIX, 375 S. : Ill., graph. Darst.
    Publisher Pan Stanford
    Publishing place Singapore
    Publishing country Singapore
    Document type Book
    HBZ-ID HT017699648
    ISBN 978-981-4411-79-0 ; 9789814411806 ; 981-4411-79-5 ; 9814411809
    Database Catalogue ZB MED Medicine, Health

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    In stock of ZB MED Cologne/Königswinter

    Shelf markLoan statusLocation
    2014 A 1948 available for loan (reading room) Lesesaal EG

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  4. Book: Force microscopy

    Jena, Bhanu P.

    applications in biology and medicine

    2006  

    Author's details ed. by Bhanu P. Jena
    Language English
    Size X, 300 S. : Ill., graph. Darst.
    Publisher Wiley-Liss
    Publishing place Hoboken, NJ
    Publishing country United States
    Document type Book
    Note Includes bibliographical references and index
    HBZ-ID HT014712640
    ISBN 978-0-471-39628-4 ; 0-471-39628-1
    Database Catalogue ZB MED Medicine, Health

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    In stock of ZB MED Cologne/Königswinter

    Shelf markLoan statusLocation
    2006 A 4599 order for loan Magazin

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  5. Article: Aquaporin regulation: Lessons from secretory vesicles.

    Jena, Bhanu P

    Vitamins and hormones

    2019  Volume 112, Page(s) 147–162

    Abstract: Secretory vesicle swelling has been demonstrated to be a requirement in cell secretion. In the past 25 years, the quest to elucidate the molecular mechanism of secretory vesicle swelling, serendipitously revealed the presence of water channels or ... ...

    Abstract Secretory vesicle swelling has been demonstrated to be a requirement in cell secretion. In the past 25 years, the quest to elucidate the molecular mechanism of secretory vesicle swelling, serendipitously revealed the presence of water channels or aquaporins at the secretory vesicle membrane and their involvement in rapid gaiting of water into secretory vesicles and their swelling during secretion. These studies further provided an understanding of aquaporin regulation at the secretory vesicle membrane. Secretory vesicles within live cells, isolated secretory vesicles, single vesicle electrophysiological patch clamp studies and the swelling complex reconstituted into liposomes, have all been utilized to elucidate the mechanism and regulation of secretory vesicle swelling. Results from these studies collectively demonstrate the involvement of β-adrenergic receptor, heterotrimeric GTP-binding G-proteins such as GαI; PLA2 and potassium and chloride channels, in the regulation of aquaporins at the secretory vesicle membrane.
    MeSH term(s) Animals ; Aquaporin 2/metabolism ; Aquaporins/metabolism ; Humans ; Secretory Vesicles/metabolism
    Chemical Substances Aquaporin 2 ; Aquaporins
    Language English
    Publishing date 2019-10-18
    Publishing country United States
    Document 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.
    ZDB-ID 201161-x
    ISSN 2162-2620 ; 0083-6729
    ISSN (online) 2162-2620
    ISSN 0083-6729
    DOI 10.1016/bs.vh.2019.08.007
    Database MEDical Literature Analysis and Retrieval System OnLINE

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    In stock of ZB MED Cologne/Königswinter

    Uc I Zs.238: Show issues Location:
    Je nach Verfügbarkeit (siehe Angabe bei Bestand)
    bis Jg. 2021: Bestellungen von Artikeln über das Online-Bestellformular
    ab Jg. 2022: Lesesaal (EG)

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  6. Book: Atomic force microscopy in cell biology

    Jena, Bhanu P.

    (Methods in cell biology ; 68)

    2002  

    Author's details ed. by Bhanu P. Jena
    Series title Methods in cell biology ; 68
    Collection
    Keywords Cytological Techniques ; Microscopy, Atomic Force / methods ; Zelle ; Rasterkraftmikroskopie
    Subject Kraftmikroskopie ; AFM ; Atomic force microscopy ; RKM ; SFM ; Scanning force microscopy
    Language English
    Size XIV, 415 S., [11] Bl. : Ill., graph. Darst.
    Publisher Acad. Press
    Publishing place Amsterdam u.a.
    Publishing country Netherlands
    Document type Book
    HBZ-ID HT013381988
    ISBN 0-12-383851-7 ; 0-12-544171-1 ; 978-0-12-383851-3 ; 978-0-12-544171-1
    Database Catalogue ZB MED Medicine, Health

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    In stock of ZB MED Cologne/Königswinter

    Shelf markLoan statusLocation
    Se 375 -68- verfügbar in Königswinter Königswinter

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  7. Article: Neuronal

    Jena, Bhanu P

    Journal of molecular structure

    2015  Volume 1073, Page(s) 187–195

    Abstract: Cup-shaped secretory portals at the cell plasma membrane ... ...

    Abstract Cup-shaped secretory portals at the cell plasma membrane called
    Language English
    Publishing date 2015-11-14
    Publishing country Netherlands
    Document type Journal Article
    ZDB-ID 194476-9
    ISSN 0022-2860 ; 0377-046X
    ISSN 0022-2860 ; 0377-046X
    DOI 10.1016/j.molstruc.2014.04.055
    Database MEDical Literature Analysis and Retrieval System OnLINE

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    In stock of ZB MED Cologne/Königswinter

    Zs.A 1205: Show issues Location:
    Je nach Verfügbarkeit (siehe Angabe bei Bestand)
    bis Jg. 1994: Bestellungen von Artikeln über das Online-Bestellformular
    Jg. 1995 - 2021: Lesesall (1.OG)
    ab Jg. 2022: Lesesaal (EG)

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  8. Article ; Online: The optimized quantum dot mediated thermometry reveals isoform specific differences in efficiency of myosin extracted from muscle mini bundles.

    Li, Meishan / Coppo, Lucia / Jena, Bhanu P / Larsson, Lars

    Archives of biochemistry and biophysics

    2022  Volume 722, Page(s) 109212

    Abstract: The biophysical function of myosin in vitro has been extensively investigated in different motility assays, but the study of myosin ATPase properties at the fiber level is insufficiently investigated. In this study, quantum dot (QD) mediated thermometry ... ...

    Abstract The biophysical function of myosin in vitro has been extensively investigated in different motility assays, but the study of myosin ATPase properties at the fiber level is insufficiently investigated. In this study, quantum dot (QD) mediated thermometry measurements were optimized to measure the efficiency of myosin extracted from muscle mini bundles. A reduction in fluorescent intensity of QD reflects an increase in temperature caused by the heat released during ATP hydrolysis and denotes the efficiency of the motor protein myosin. The procedure for extracting myosin was similar to the single fiber in vitro motility assay with some small modifications, and the concentration of myosin was represented by the extracted total protein since the ratio of extracted myosin to total protein was constant. Moreover, the efficiencies of myosin extracted from preparations containing different myosin heavy chain isoforms reveal lower efficiency of slow compared to fast myosin isoforms. Specifically, more heat was released in slow myosin enzymatic reaction, resulting in faster decay of QD fluorescence intensity. Hence, the optimized QD mediated thermometry provides a novel and sensitive approach to evaluate efficiency of myosin ATPase obtained from small muscle samples, representing a significant advantage in the clinical evaluation of neuromuscular disorders.
    MeSH term(s) Muscle, Skeletal/metabolism ; Myosin Heavy Chains ; Myosins/metabolism ; Protein Isoforms/metabolism ; Quantum Dots ; Thermometry
    Chemical Substances Protein Isoforms ; Myosin Heavy Chains (EC 3.6.4.1) ; Myosins (EC 3.6.4.1)
    Language English
    Publishing date 2022-04-06
    Publishing country United States
    Document type Journal Article ; Research Support, Non-U.S. Gov't
    ZDB-ID 523-x
    ISSN 1096-0384 ; 0003-9861
    ISSN (online) 1096-0384
    ISSN 0003-9861
    DOI 10.1016/j.abb.2022.109212
    Database MEDical Literature Analysis and Retrieval System OnLINE

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    In stock of ZB MED Cologne/Königswinter

    Uc I Zs.237: Show issues Location:
    Je nach Verfügbarkeit (siehe Angabe bei Bestand)
    bis Jg. 2021: Bestellungen von Artikeln über das Online-Bestellformular
    ab Jg. 2022: Lesesaal (EG)

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  9. Article: Porosome in Cystic Fibrosis.

    Jena, Bhanu P

    Discoveries (Craiova, Romania)

    2015  Volume 2, Issue 3

    Abstract: Macromolecular structures embedded in the cell plasma membrane called 'porosomes', are involved in the regulated fractional release of intravesicular contents from cells during secretion. Porosomes range in size from 15 nm in neurons and astrocytes to ... ...

    Abstract Macromolecular structures embedded in the cell plasma membrane called 'porosomes', are involved in the regulated fractional release of intravesicular contents from cells during secretion. Porosomes range in size from 15 nm in neurons and astrocytes to 100-180 nm in the exocrine pancreas and neuroendocrine cells. Porosomes have been isolated from a number of cells, and their morphology, composition, and functional reconstitution well documented. The 3D contour map of the assembly of proteins within the porosome complex, and its native X-ray solution structure at sub-nm resolution has also advanced. This understanding now provides a platform to address diseases that may result from secretory defects. Water and ion binding to mucin impart hydration, critical for regulating viscosity of the mucus in the airways epithelia. Appropriate viscosity is required for the movement of mucus by the underlying cilia. Hence secretion of more viscous mucus prevents its proper transport, resulting in chronic and fatal airways disease such as cystic fibrosis (CF). CF is caused by the malfunction of CF transmembrane conductance regulator (CFTR), a chloride channel transporter, resulting in viscous mucus in the airways. Studies in mice lacking functional CFTR secrete highly viscous mucous that adhered to the epithelium. Since CFTR is known to interact with the t-SNARE protein syntaxin-1A, and with the chloride channel CLC-3, which are also components of the porosome complex, the interactions between CFTR and the porosome complex in the mucin-secreting human airway epithelial cell line Calu-3 was hypothesized and tested. Results from the study demonstrate the presence of approximately 100 nm in size porosome complex composed of 34 proteins at the cell plasma membrane in Calu-3 cells, and the association of CFTR with the complex. In comparison, the nuclear pore complex measures 120 nm and is comprised of over 500 protein molecules. The involvement of CFTR in porosome-mediated mucin secretion is hypothesized, and is currently being tested.
    Language English
    Publishing date 2015-09-16
    Publishing country Romania
    Document type Journal Article
    ISSN 2359-7232
    ISSN 2359-7232
    DOI 10.15190/d.2014.16
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  10. Article ; Online: 'Porosome' discovered nearly 20 years ago provides molecular insights into the kiss-and-run mechanism of cell secretion.

    Jena, Bhanu P

    Journal of cellular and molecular medicine

    2015  Volume 19, Issue 7, Page(s) 1427–1440

    Abstract: Secretion is a fundamental cellular process in living organisms, from yeast to cells in humans. Since the 1950s, it was believed that secretory vesicles completely merged with the cell plasma membrane during secretion. While this may occur, the ... ...

    Abstract Secretion is a fundamental cellular process in living organisms, from yeast to cells in humans. Since the 1950s, it was believed that secretory vesicles completely merged with the cell plasma membrane during secretion. While this may occur, the observation of partially empty vesicles in cells following secretion suggests the presence of an additional mechanism that allows partial discharge of intra-vesicular contents during secretion. This proposed mechanism requires the involvement of a plasma membrane structure called 'porosome', which serves to prevent the collapse of secretory vesicles, and to transiently fuse with the plasma membrane (Kiss-and-run), expel a portion of its contents and disengage. Porosomes are cup-shaped supramolecular lipoprotein structures at the cell plasma membrane ranging in size from 15 nm in neurons and astrocytes to 100-180 nm in endocrine and exocrine cells. Neuronal porosomes are composed of nearly 40 proteins. In comparison, the 120 nm nuclear pore complex is composed of >500 protein molecules. Elucidation of the porosome structure, its chemical composition and functional reconstitution into artificial lipid membrane, and the molecular assembly of membrane-associated t-SNARE and v-SNARE proteins in a ring or rosette complex resulting in the establishment of membrane continuity to form a fusion pore at the porosome base, has been demonstrated. Additionally, the molecular mechanism of secretory vesicle swelling, and its requirement for intra-vesicular content release during cell secretion has also been elucidated. Collectively, these observations provide a molecular understanding of cell secretion, resulting in a paradigm shift in our understanding of the secretory process.
    MeSH term(s) Animals ; Calcium/metabolism ; Cell Membrane/metabolism ; Cell Membrane/ultrastructure ; Humans ; Membrane Fusion ; Models, Biological ; SNARE Proteins/metabolism ; Secretory Vesicles/metabolism ; Secretory Vesicles/ultrastructure
    Chemical Substances SNARE Proteins ; Calcium (SY7Q814VUP)
    Language English
    Publishing date 2015-07
    Publishing country England
    Document type Journal Article ; Research Support, N.I.H., Extramural ; Research Support, U.S. Gov't, Non-P.H.S. ; Review
    ZDB-ID 2074559-X
    ISSN 1582-4934 ; 1582-4934 ; 1582-1838
    ISSN (online) 1582-4934
    ISSN 1582-4934 ; 1582-1838
    DOI 10.1111/jcmm.12598
    Database MEDical Literature Analysis and Retrieval System OnLINE

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    Zs.A 5752: Show issues Location:
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    Jg. 1995 - 2021: Lesesall (2.OG)
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