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  1. Book ; Online ; Conference proceedings: Proceedings of the 5th International Symposium on Biological Control of Arthropods

    Mason, Peter G. / Gillespie, David R. / Vincent, Charles

    Langkawi, Malaysia : September 11-15, 2017

    2017  

    Event/congress International Symposium on Biological Control of Arthropods (5., 2017, Langkawi)
    Author's details edited by Peter G. Mason, David R. Gillespie and Charles Vincent
    Language English
    Size 1 Online-Ressource (332 Seiten)
    Publisher CABI
    Publishing place Wallingford ; Boston, MA
    Publishing country Great Britain
    Document type Book ; Online ; Conference proceedings
    Note Open Access
    HBZ-ID HT020561781
    ISBN 9781786394118 ; 1786394111
    DOI 10.1079/9781786394118.0000
    Database ZB MED Catalogue: Medicine, Health, Nutrition, Environment, Agriculture

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  2. Article ; Online: Ca

    Halford, Julia / Bateschell, Michael / Barr-Gillespie, Peter G

    Molecular biology of the cell

    2022  Volume 33, Issue 4, Page(s) br6

    Abstract: Brain-specific angiogenesis inhibitor 1-associated protein 2-like protein 2 (BAIAP2L2), a membrane-binding protein required for the maintenance of mechanotransduction in hair cells, is selectively retained at the tips of transducing stereocilia. BAIAP2L2 ...

    Abstract Brain-specific angiogenesis inhibitor 1-associated protein 2-like protein 2 (BAIAP2L2), a membrane-binding protein required for the maintenance of mechanotransduction in hair cells, is selectively retained at the tips of transducing stereocilia. BAIAP2L2 trafficked to stereocilia tips in the absence of EPS8, but EPS8 increased the efficiency of localization. A tripartite complex of BAIAP2L2, EPS8, and MYO15A formed efficiently in vitro, and these three proteins robustly targeted to filopodia tips when coexpressed in cultured cells. Mice lacking functional transduction channels no longer concentrated BAIAP2L2 at row 2 stereocilia tips, a result that was phenocopied by blocking channels with tubocurarine in cochlear explants. Transduction channels permit Ca
    MeSH term(s) Animals ; Calcium/metabolism ; Hair Cells, Auditory ; Mechanotransduction, Cellular/physiology ; Membrane Proteins/metabolism ; Mice ; Stereocilia
    Chemical Substances Baiap2l2 protein, mouse ; Membrane Proteins ; Calcium (SY7Q814VUP)
    Language English
    Publishing date 2022-01-19
    Publishing country United States
    Document type Journal Article ; Research Support, N.I.H., Extramural
    ZDB-ID 1098979-1
    ISSN 1939-4586 ; 1059-1524
    ISSN (online) 1939-4586
    ISSN 1059-1524
    DOI 10.1091/mbc.E21-10-0491
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  3. Article ; Online: Honing In on TMC as the Hair Cell's Transduction Channel.

    Barr-Gillespie, Peter G

    Neuron

    2018  Volume 99, Issue 4, Page(s) 628–629

    Abstract: The identity of the inner ear's transduction channel has bedeviled auditory neuroscientists for decades. In this issue of Neuron, Pan et al. (2018) report the most convincing evidence to date implicating the transmembrane channel-like (TMC) proteins as ... ...

    Abstract The identity of the inner ear's transduction channel has bedeviled auditory neuroscientists for decades. In this issue of Neuron, Pan et al. (2018) report the most convincing evidence to date implicating the transmembrane channel-like (TMC) proteins as forming the pore of the transduction channel.
    MeSH term(s) Animals ; Ear, Inner ; Hair ; Hair Cells, Auditory ; Mechanotransduction, Cellular ; Vertebrates
    Language English
    Publishing date 2018-08-22
    Publishing country United States
    Document type Journal Article ; Comment
    ZDB-ID 808167-0
    ISSN 1097-4199 ; 0896-6273
    ISSN (online) 1097-4199
    ISSN 0896-6273
    DOI 10.1016/j.neuron.2018.08.013
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  4. Article ; Online: Cy3-ATP labeling of unfixed, permeabilized mouse hair cells.

    Pacentine, Itallia V / Barr-Gillespie, Peter G

    Scientific reports

    2021  Volume 11, Issue 1, Page(s) 23855

    Abstract: ATP-utilizing enzymes play key roles in hair bundles, the mechanically sensitive organelles of sensory hair cells in the inner ear. We used a fluorescent ATP analog, EDA-ATP-Cy3 (Cy3-ATP), to label ATP-binding proteins in two different preparations of ... ...

    Abstract ATP-utilizing enzymes play key roles in hair bundles, the mechanically sensitive organelles of sensory hair cells in the inner ear. We used a fluorescent ATP analog, EDA-ATP-Cy3 (Cy3-ATP), to label ATP-binding proteins in two different preparations of unfixed hair-cell stereocilia of the mouse. In the first preparation, we lightly permeabilized dissected cochleas, then labeled them with Cy3-ATP. Hair cells and their stereocilia remained intact, and stereocilia tips in rows 1 and 2 were labeled particularly strongly with Cy3-ATP. In many cases, vanadate (V
    MeSH term(s) Actins/metabolism ; Adenosine Triphosphate/analogs & derivatives ; Adenosine Triphosphate/metabolism ; Animals ; Bridged Bicyclo Compounds, Heterocyclic/pharmacology ; Cells, Cultured ; Cytochalasin D/pharmacology ; Hair Cells, Auditory/cytology ; Hair Cells, Auditory/drug effects ; Hair Cells, Auditory/metabolism ; Indoles/metabolism ; Mice ; Mice, Inbred C57BL ; Myosins/metabolism ; Stereocilia/metabolism ; Stereocilia/ultrastructure ; Thiazolidines/pharmacology ; Vanadates/pharmacology
    Chemical Substances 3'(2')-O-(N-(2-((2-((1-ethyl-3,3-dimethyl-5-sulfoindol-2-yl)prop-2-enylidene)-3,3-dimethyl-5-sulfoindol-1-yl)amino)ethyl)carbamoyl)-adenosine triphosphate ; Actins ; Bridged Bicyclo Compounds, Heterocyclic ; Indoles ; Thiazolidines ; Cytochalasin D (22144-77-0) ; Vanadates (3WHH0066W5) ; Adenosine Triphosphate (8L70Q75FXE) ; Myosins (EC 3.6.4.1) ; latrunculin A (SRQ9WWM084)
    Language English
    Publishing date 2021-12-13
    Publishing country England
    Document type Journal Article ; Research Support, N.I.H., Extramural
    ZDB-ID 2615211-3
    ISSN 2045-2322 ; 2045-2322
    ISSN (online) 2045-2322
    ISSN 2045-2322
    DOI 10.1038/s41598-021-03365-x
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  5. Article ; Online: Ultrasound Secondary Signs for the Diagnosis of Pediatric Distal Forearm Fractures: A Diagnostic Study.

    Snelling, Peter J / Jones, Philip / Bade, David / Gillespie, Alan / Keijzers, Gerben / Ware, Robert S

    Ultrasound in medicine & biology

    2024  Volume 50, Issue 6, Page(s) 898–907

    Abstract: Objective: To evaluate the diagnostic accuracy of ultrasound secondary signs of fractures in pediatric patients aged 5-15 y presenting to the emergency department with a clinically non-deformed distal forearm injury.: Methods: This diagnostic study ... ...

    Abstract Objective: To evaluate the diagnostic accuracy of ultrasound secondary signs of fractures in pediatric patients aged 5-15 y presenting to the emergency department with a clinically non-deformed distal forearm injury.
    Methods: This diagnostic study was conducted in South East Queensland, Australia. Emergency clinicians performed point-of-care ultrasound on eligible patients and recorded secondary signs of fractures (pronator quadratus hematoma [PQH] sign, periosteal hematoma, visible angulation) or physeal fractures (fracture-to-physis distance [FPD], physis alteration). The reference standard was the final fracture diagnosis determined by expert panel. The primary outcome was the diagnostic accuracy of secondary signs for cortical breach and physeal fractures. Diagnostic statistics were reported for each relevant secondary sign.
    Results: A total of 135 participants were enrolled. The expert panel diagnosed 48 "no" fracture, 52 "buckle" fracture and 35 "other" fracture. All "other" fractures were cortical breach fractures and included 15 Salter-Harris II fractures. The PQH sign demonstrated high sensitivity and moderate specificity to diagnose cortical breach fractures (91%, 95% Confidence Interval [CI] 78%-97% and 82%, 73%-88%). Poor sensitivity but high specificity was observed for the visible angulation and periosteal hematoma secondary signs. FPD <1cm showed perfect sensitivity and moderate specificity (100%, 80%-100% and 85%, 78%-90%) for diagnosis of Salter-Harris II fracture. Conversely, physis alteration showed poor sensitivity but excellent specificity (40%, 20%-64% and 99%, 95%-100%) for the diagnosis of Salter-Harris II fractures.
    Conclusion: Ultrasound secondary signs showed good diagnostic accuracy for both cortical breach fractures and Salter-Harris II fractures. Future research should consider optimal use of secondary signs to improve diagnostic accuracy.
    MeSH term(s) Humans ; Child ; Female ; Male ; Ultrasonography/methods ; Adolescent ; Child, Preschool ; Sensitivity and Specificity ; Forearm Injuries/diagnostic imaging ; Ulna Fractures/diagnostic imaging ; Reproducibility of Results ; Prospective Studies ; Radius Fractures/diagnostic imaging ; Wrist Fractures
    Language English
    Publishing date 2024-03-21
    Publishing country England
    Document type Journal Article ; Research Support, Non-U.S. Gov't
    ZDB-ID 186150-5
    ISSN 1879-291X ; 0301-5629
    ISSN (online) 1879-291X
    ISSN 0301-5629
    DOI 10.1016/j.ultrasmedbio.2024.02.015
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  6. Article ; Online: Cy3-ATP labeling of unfixed, permeabilized mouse hair cells

    Itallia V. Pacentine / Peter G. Barr-Gillespie

    Scientific Reports, Vol 11, Iss 1, Pp 1-

    2021  Volume 13

    Abstract: Abstract ATP-utilizing enzymes play key roles in hair bundles, the mechanically sensitive organelles of sensory hair cells in the inner ear. We used a fluorescent ATP analog, EDA-ATP-Cy3 (Cy3-ATP), to label ATP-binding proteins in two different ... ...

    Abstract Abstract ATP-utilizing enzymes play key roles in hair bundles, the mechanically sensitive organelles of sensory hair cells in the inner ear. We used a fluorescent ATP analog, EDA-ATP-Cy3 (Cy3-ATP), to label ATP-binding proteins in two different preparations of unfixed hair-cell stereocilia of the mouse. In the first preparation, we lightly permeabilized dissected cochleas, then labeled them with Cy3-ATP. Hair cells and their stereocilia remained intact, and stereocilia tips in rows 1 and 2 were labeled particularly strongly with Cy3-ATP. In many cases, vanadate (Vi) traps nucleotides at the active site of myosin isoforms and presents nucleotide dissociation. Co-application with Vi enhanced the tip labeling, which is consistent with myosin isoforms being responsible. By contrast, the actin polymerization inhibitors latrunculin A and cytochalasin D had no effect, suggesting that actin turnover at stereocilia tips was not involved. Cy3-ATP labeling was substantially reduced—but did not disappear altogether—in mutant cochleas lacking MYO15A; by contrast, labeling remained robust in cochleas lacking MYO7A. In the second preparation, used to quantify Cy3-ATP labeling, we labeled vestibular stereocilia that had been adsorbed to glass, which demonstrated that tip labeling was higher in longer stereocilia. We found that tip signal was reduced by ~ 50% in Myo15a sh2/sh2 stereocilia as compared to Myo15a sh2 /+stereocilia. These results suggest that MYO15A accounts for a substantial fraction of the Cy3-ATP tip labeling in vestibular hair cells, and so this novel preparation could be utilized to examine the control of MYO15A ATPase activity in situ.
    Keywords Medicine ; R ; Science ; Q
    Subject code 570
    Language English
    Publishing date 2021-12-01T00:00:00Z
    Publisher Nature Portfolio
    Document type Article ; Online
    Database BASE - Bielefeld Academic Search Engine (life sciences selection)

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  7. Article: GIPC3 couples to MYO6 and PDZ domain proteins and shapes the hair cell apical region.

    Chatterjee, Paroma / Morgan, Clive P / Krey, Jocelyn F / Benson, Connor / Goldsmith, Jennifer / Bateschell, Michael / Ricci, Anthony J / Barr-Gillespie, Peter G

    bioRxiv : the preprint server for biology

    2023  

    Abstract: GIPC3 has been implicated in auditory function. Initially localized to the cytoplasm of inner and outer hair cells of the cochlea, GIPC3 increasingly concentrated in cuticular plates and at cell junctions during postnatal development. Early postnatal : ...

    Abstract GIPC3 has been implicated in auditory function. Initially localized to the cytoplasm of inner and outer hair cells of the cochlea, GIPC3 increasingly concentrated in cuticular plates and at cell junctions during postnatal development. Early postnatal
    Summary statement: The PDZ-domain protein GIPC3 couples the molecular motors MYO6 and MYO18A to actin cytoskeleton structures in hair cells. GIPC3 is necessary for shaping the hair cell’s cuticular plate and hence the arrangement of the stereocilia in the hair bundle.
    Language English
    Publishing date 2023-03-01
    Publishing country United States
    Document type Preprint
    DOI 10.1101/2023.02.28.530466
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  8. Article ; Online: Stereocilia Rootlets: Actin-Based Structures That Are Essential for Structural Stability of the Hair Bundle.

    Pacentine, Itallia / Chatterjee, Paroma / Barr-Gillespie, Peter G

    International journal of molecular sciences

    2020  Volume 21, Issue 1

    Abstract: Sensory hair cells of the inner ear rely on the hair bundle, a cluster of actin-filled stereocilia, to transduce auditory and vestibular stimuli into electrical impulses. Because they are long and thin projections, stereocilia are most prone to damage at ...

    Abstract Sensory hair cells of the inner ear rely on the hair bundle, a cluster of actin-filled stereocilia, to transduce auditory and vestibular stimuli into electrical impulses. Because they are long and thin projections, stereocilia are most prone to damage at the point where they insert into the hair cell's soma. Moreover, this is the site of stereocilia pivoting, the mechanical movement that induces transduction, which additionally weakens this area mechanically. To bolster this fragile area, hair cells construct a dense core called the rootlet at the base of each stereocilium, which extends down into the actin meshwork of the cuticular plate and firmly anchors the stereocilium. Rootlets are constructed with tightly packed actin filaments that extend from stereocilia actin filaments which are wrapped with TRIOBP; in addition, many other proteins contribute to the rootlet and its associated structures. Rootlets allow stereocilia to sustain innumerable deflections over their lifetimes and exemplify the unique manner in which sensory hair cells exploit actin and its associated proteins to carry out the function of mechanotransduction.
    MeSH term(s) Actins/analysis ; Actins/metabolism ; Animals ; Hair Cells, Auditory/chemistry ; Hair Cells, Auditory/cytology ; Hair Cells, Auditory/metabolism ; Hair Cells, Auditory/ultrastructure ; Hair Cells, Vestibular/chemistry ; Hair Cells, Vestibular/cytology ; Hair Cells, Vestibular/metabolism ; Hair Cells, Vestibular/ultrastructure ; Hearing ; Humans ; Mechanotransduction, Cellular ; Postural Balance ; Stereocilia/chemistry ; Stereocilia/metabolism ; Stereocilia/ultrastructure
    Chemical Substances Actins
    Language English
    Publishing date 2020-01-03
    Publishing country Switzerland
    Document type Journal Article ; Review
    ZDB-ID 2019364-6
    ISSN 1422-0067 ; 1422-0067 ; 1661-6596
    ISSN (online) 1422-0067
    ISSN 1422-0067 ; 1661-6596
    DOI 10.3390/ijms21010324
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  9. Article ; Online: GIPC3 couples to MYO6 and PDZ domain proteins, and shapes the hair cell apical region.

    Chatterjee, Paroma / Morgan, Clive P / Krey, Jocelyn F / Benson, Connor / Goldsmith, Jennifer / Bateschell, Michael / Ricci, Anthony J / Barr-Gillespie, Peter G

    Journal of cell science

    2023  Volume 136, Issue 10

    Abstract: GIPC3 has been implicated in auditory function. Here, we establish that GIPC3 is initially localized to the cytoplasm of inner and outer hair cells of the cochlea and then is increasingly concentrated in cuticular plates and at cell junctions during ... ...

    Abstract GIPC3 has been implicated in auditory function. Here, we establish that GIPC3 is initially localized to the cytoplasm of inner and outer hair cells of the cochlea and then is increasingly concentrated in cuticular plates and at cell junctions during postnatal development. Early postnatal Gipc3KO/KO mice had mostly normal mechanotransduction currents, but had no auditory brainstem response at 1 month of age. Cuticular plates of Gipc3KO/KO hair cells did not flatten during development as did those of controls; moreover, hair bundles were squeezed along the cochlear axis in mutant hair cells. Junctions between inner hair cells and adjacent inner phalangeal cells were also severely disrupted in Gipc3KO/KO cochleas. GIPC3 bound directly to MYO6, and the loss of MYO6 led to altered distribution of GIPC3. Immunoaffinity purification of GIPC3 from chicken inner ear extracts identified co-precipitating proteins associated with adherens junctions, intermediate filament networks and the cuticular plate. Several of immunoprecipitated proteins contained GIPC family consensus PDZ-binding motifs (PBMs), including MYO18A, which bound directly to the PDZ domain of GIPC3. We propose that GIPC3 and MYO6 couple to PBMs of cytoskeletal and cell junction proteins to shape the cuticular plate.
    MeSH term(s) Mice ; Animals ; Mechanotransduction, Cellular ; PDZ Domains ; Hair Cells, Auditory, Inner/metabolism ; Cytoskeleton/metabolism ; Hair Cells, Auditory, Outer/metabolism ; Adaptor Proteins, Signal Transducing/metabolism ; Myosins/genetics ; Myosins/metabolism
    Chemical Substances Gipc3 protein, mouse ; Adaptor Proteins, Signal Transducing ; Myo18a protein, mouse ; Myosins (EC 3.6.4.1)
    Language English
    Publishing date 2023-05-25
    Publishing country England
    Document type Journal Article ; Research Support, N.I.H., Extramural ; Research Support, Non-U.S. Gov't
    ZDB-ID 2993-2
    ISSN 1477-9137 ; 0021-9533
    ISSN (online) 1477-9137
    ISSN 0021-9533
    DOI 10.1242/jcs.261100
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  10. Article ; Online: Assembly of hair bundles, an amazing problem for cell biology.

    Barr-Gillespie, Peter-G

    Molecular biology of the cell

    2015  Volume 26, Issue 15, Page(s) 2727–2732

    Abstract: The hair bundle--the sensory organelle of inner-ear hair cells of vertebrates--exemplifies the ability of a cell to assemble complex, elegant structures. Proper construction of the bundle is required for proper mechanotransduction in response to external ...

    Abstract The hair bundle--the sensory organelle of inner-ear hair cells of vertebrates--exemplifies the ability of a cell to assemble complex, elegant structures. Proper construction of the bundle is required for proper mechanotransduction in response to external forces and to transmit information about sound and movement. Bundles contain tightly controlled numbers of actin-filled stereocilia, which are arranged in defined rows of precise heights. Indeed, many deafness mutations that disable hair-cell cytoskeletal proteins also disrupt bundles. Bundle assembly is a tractable problem in molecular and cellular systems biology; the sequence of structural changes in stereocilia is known, and a modest number of proteins may be involved.
    MeSH term(s) Actins/metabolism ; Animals ; Cell Biology ; Deafness/metabolism ; Deafness/pathology ; Hair Cells, Auditory, Inner/cytology ; Hair Cells, Auditory, Inner/metabolism ; Hair Cells, Auditory, Inner/pathology ; Hair Cells, Auditory, Inner/physiology ; Humans ; Stereocilia/metabolism ; Stereocilia/pathology
    Chemical Substances Actins
    Language English
    Publishing date 2015-08-01
    Publishing country United States
    Document type Journal Article ; Research Support, N.I.H., Extramural ; Review
    ZDB-ID 1098979-1
    ISSN 1939-4586 ; 1059-1524
    ISSN (online) 1939-4586
    ISSN 1059-1524
    DOI 10.1091/mbc.E14-04-0940
    Database MEDical Literature Analysis and Retrieval System OnLINE

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