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  1. Article: Francis Barr.

    Barr, Francis

    Current biology : CB

    2005  Volume 15, Issue 9, Page(s) R314–5

    MeSH term(s) Career Choice ; Cell Growth Processes/physiology ; Membranes/physiology ; Publishing
    Language English
    Publishing date 2005-03-22
    Publishing country England
    Document type Interview
    ZDB-ID 1071731-6
    ISSN 1879-0445 ; 0960-9822
    ISSN (online) 1879-0445
    ISSN 0960-9822
    DOI 10.1016/j.cub.2005.04.040
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  2. Article: Drake, Francis

    Barr, C. Bernard L

    Oxford dictionary of national biography v.16

    2004  

    Author's details C. Bernard L. Barr
    MeSH term(s) General Surgery ; History of Medicine ; History, 18th Century
    Keywords England
    Language English
    Size p. 870-873.
    Publisher Oxford University Press
    Publishing place Oxford ; New York
    Document type Article
    ISBN 019861411X ; 9780198614111
    Database Catalogue of the US National Library of Medicine (NLM)

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  3. Article ; Online: Membrane Traffic: Trans-Golgi Tethers Leave a Surprisingly Small GAP.

    Barr, Francis A

    Current biology : CB

    2017  Volume 27, Issue 22, Page(s) R1222–R1225

    Abstract: Activation and inactivation of Rab GTPases by GEFs and GAPs promotes or terminates vesicle tethering to organelles, respectively. This simple model is challenged by new evidence revealing that a catalytically inactive Rab GAP promotes rather than ... ...

    Abstract Activation and inactivation of Rab GTPases by GEFs and GAPs promotes or terminates vesicle tethering to organelles, respectively. This simple model is challenged by new evidence revealing that a catalytically inactive Rab GAP promotes rather than terminates vesicle tethering at the trans-Golgi.
    MeSH term(s) Endosomes ; Golgi Apparatus ; Golgi Matrix Proteins ; Protein Transport ; rab GTP-Binding Proteins
    Chemical Substances Golgi Matrix Proteins ; rab GTP-Binding Proteins (EC 3.6.5.2)
    Language English
    Publishing date 2017-11-17
    Publishing country England
    Document type Journal Article ; Comment
    ZDB-ID 1071731-6
    ISSN 1879-0445 ; 0960-9822
    ISSN (online) 1879-0445
    ISSN 0960-9822
    DOI 10.1016/j.cub.2017.10.003
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  4. Book ; Online: Polaris

    Barr, William / Bessels, Emil

    2016  

    Abstract: Emil Bessels was chief scientist and medical officer on George Francis Halls ill-fated American ... during the first winter, and Bessels is widely suspected of having poisoned him. Bill Barr has uncovered ...

    Abstract Emil Bessels was chief scientist and medical officer on George Francis Halls ill-fated American North Pole Expedition of 1871-73 on board the ship Polaris. Bessels book, translated from the German in its entirety for the first time, is one of only two first-hand accounts of the voyage, and it is the only first-hand account of the experiences of the group which stayed with the ship after it ran afoul of arctic ice, leaving some of its crew stranded on an ice floe. Bessels and the others spent a second winter on shore in Northwest Greenland, where the drifting, disabled ship ran aground. Hall died suspiciously during the first winter, and Bessels is widely suspected of having poisoned him. Bill Barr has uncovered new evidence of a possible motive. Essential reading for researchers and students of arctic exploration history, this book is also a compelling read for the interested general reader
    Size 1 electronic resource (672 p.)
    Publisher University of Calgary Press
    Document type Book ; Online
    Note English ; Open Access
    HBZ-ID HT020092212
    ISBN 9781552388754 ; 9781552388761 ; 1552388751 ; 155238876X
    Database ZB MED Catalogue: Medicine, Health, Nutrition, Environment, Agriculture

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  5. Article ; Online: Molecular basis for pH sensing in the KDEL trafficking receptor.

    Wu, Zhiyi / Smith, Kathryn / Gerondopoulos, Andreas / Sobajima, Tomoaki / Parker, Joanne L / Barr, Francis A / Newstead, Simon / Biggin, Philip C

    Structure (London, England : 1993)

    2024  

    Abstract: Trafficking receptors control protein localization through the recognition of specific signal sequences that specify unique cellular locations. Differences in luminal pH are important for the vectorial trafficking of cargo receptors. The KDEL receptor is ...

    Abstract Trafficking receptors control protein localization through the recognition of specific signal sequences that specify unique cellular locations. Differences in luminal pH are important for the vectorial trafficking of cargo receptors. The KDEL receptor is responsible for maintaining the integrity of the ER by retrieving luminally localized folding chaperones in a pH-dependent mechanism. Structural studies have revealed the end states of KDEL receptor activation and the mechanism of selective cargo binding. However, precisely how the KDEL receptor responds to changes in luminal pH remains unclear. To explain the mechanism of pH sensing, we combine analysis of X-ray crystal structures of the KDEL receptor at neutral and acidic pH with advanced computational methods and cell-based assays. We show a critical role for ordered water molecules that allows us to infer a direct connection between protonation in different cellular compartments and the consequent changes in the affinity of the receptor for cargo.
    Language English
    Publishing date 2024-04-12
    Publishing country United States
    Document type Journal Article
    ZDB-ID 1213087-4
    ISSN 1878-4186 ; 0969-2126
    ISSN (online) 1878-4186
    ISSN 0969-2126
    DOI 10.1016/j.str.2024.03.013
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  6. Article ; Online: Facilitators and Barriers to Pediatric Nurse Practitioner Practice in the United States: A Systematic Review.

    Courtwright, Suzanne E / Turi, Eleanor / Barr, Emily A / Burns, Jade C / Gigli, Kristin Hittle / Bennett, C Robert / Sonney, Jennifer / Francis, Lucine / Poghosyan, Lusine

    Journal of pediatric health care : official publication of National Association of Pediatric Nurse Associates & Practitioners

    2024  

    Abstract: Introduction: The pediatric nurse practitioner (PNP) workforce was designed to improve child health equity. We aimed to systematically review the evidence on facilitators and barriers to PNP practice.: Method: We included empirical studies on PNP ... ...

    Abstract Introduction: The pediatric nurse practitioner (PNP) workforce was designed to improve child health equity. We aimed to systematically review the evidence on facilitators and barriers to PNP practice.
    Method: We included empirical studies on PNP practice in the United States and excluded studies with non-identifiable PNP data. We applied Joanna Briggs Institute tools to appraise studies and applied critical interpretive synthesis principles to synthesize.
    Results: The final sample is 26 studies, mostly published before 2013 and observational. Prescriptive privileges, training program availability, organizational climate, and telehealth are facilitators. Mandated physician supervision, reduced pediatric curricula, geographically disparate training programs, and poor data infrastructure are barriers. The sample is limited by a moderate to high risk of bias.
    Discussion: Evidence suggests modifiable factors impact PNP practice and could have important implications for child health equity. We offer a theoretical model to guide robust research studying the PNP workforce and health equity.
    Language English
    Publishing date 2024-01-29
    Publishing country United States
    Document type Journal Article
    ZDB-ID 1036356-7
    ISSN 1532-656X ; 0891-5245
    ISSN (online) 1532-656X
    ISSN 0891-5245
    DOI 10.1016/j.pedhc.2023.12.003
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  7. Article ; Online: Ordered dephosphorylation initiated by the selective proteolysis of cyclin B drives mitotic exit.

    Holder, James / Mohammed, Shabaz / Barr, Francis A

    eLife

    2020  Volume 9

    Abstract: APC/C-mediated proteolysis of cyclin B and securin promotes anaphase entry, inactivating CDK1 and permitting chromosome segregation, respectively. Reduction of CDK1 activity relieves inhibition of the CDK1-counteracting phosphatases PP1 and PP2A-B55, ... ...

    Abstract APC/C-mediated proteolysis of cyclin B and securin promotes anaphase entry, inactivating CDK1 and permitting chromosome segregation, respectively. Reduction of CDK1 activity relieves inhibition of the CDK1-counteracting phosphatases PP1 and PP2A-B55, allowing wide-spread dephosphorylation of substrates. Meanwhile, continued APC/C activity promotes proteolysis of other mitotic regulators. Together, these activities orchestrate a complex series of events during mitotic exit. However, the relative importance of regulated proteolysis and dephosphorylation in dictating the order and timing of these events remains unclear. Using high temporal-resolution proteomics, we compare the relative extent of proteolysis and protein dephosphorylation. This reveals highly-selective rapid proteolysis of cyclin B, securin and geminin at the metaphase-anaphase transition, followed by slow proteolysis of other substrates. Dephosphorylation requires APC/C-dependent destruction of cyclin B and was resolved into PP1-dependent categories with unique sequence motifs. We conclude that dephosphorylation initiated by selective proteolysis of cyclin B drives the bulk of changes observed during mitotic exit.
    MeSH term(s) CDC2 Protein Kinase/metabolism ; Cyclin B/metabolism ; HeLa Cells ; Humans ; Mitosis/physiology ; Phosphorylation/physiology ; Protein Phosphatase 1/metabolism ; Protein Phosphatase 2/metabolism ; Proteolysis
    Chemical Substances Cyclin B ; CDC2 Protein Kinase (EC 2.7.11.22) ; CDK1 protein, human (EC 2.7.11.22) ; Protein Phosphatase 1 (EC 3.1.3.16) ; Protein Phosphatase 2 (EC 3.1.3.16)
    Language English
    Publishing date 2020-09-01
    Publishing country England
    Document type Journal Article ; Research Support, Non-U.S. Gov't
    ZDB-ID 2687154-3
    ISSN 2050-084X ; 2050-084X
    ISSN (online) 2050-084X
    ISSN 2050-084X
    DOI 10.7554/eLife.59885
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  8. Article ; Online: Review series: Rab GTPases and membrane identity: causal or inconsequential?

    Barr, Francis A

    The Journal of cell biology

    2013  Volume 202, Issue 2, Page(s) 191–199

    Abstract: Rab GTPases are highly conserved components of vesicle trafficking pathways that help to ensure the fusion of a vesicle with a specific target organelle membrane. Specific regulatory pathways promote kinetic proofreading of membrane surfaces by Rab ... ...

    Abstract Rab GTPases are highly conserved components of vesicle trafficking pathways that help to ensure the fusion of a vesicle with a specific target organelle membrane. Specific regulatory pathways promote kinetic proofreading of membrane surfaces by Rab GTPases, and permit accumulation of active Rabs only at the required sites. Emerging evidence indicates that Rab activation and inactivation are under complex feedback control, suggesting that ultrasensitivity and bistability, principles established for other cellular regulatory networks, may also apply to Rab regulation. Such systems can promote the rapid membrane accumulation and removal of Rabs to create time-limited membrane domains with a unique composition, and can explain how Rabs define the identity of vesicle and organelle membranes.
    MeSH term(s) Cell Membrane/enzymology ; Endoplasmic Reticulum/enzymology ; Enzyme Activation ; Feedback, Physiological ; Golgi Apparatus/enzymology ; Guanine Nucleotide Exchange Factors/metabolism ; Humans ; Multiprotein Complexes/metabolism ; Protein Transport ; Transport Vesicles/enzymology ; rab GTP-Binding Proteins/metabolism
    Chemical Substances Guanine Nucleotide Exchange Factors ; Multiprotein Complexes ; rab GTP-Binding Proteins (EC 3.6.5.2)
    Language English
    Publishing date 2013-07-22
    Publishing country United States
    Document type Journal Article ; Research Support, Non-U.S. Gov't ; Review
    ZDB-ID 218154-x
    ISSN 1540-8140 ; 0021-9525
    ISSN (online) 1540-8140
    ISSN 0021-9525
    DOI 10.1083/jcb.201306010
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  9. Article ; Online: Ordered dephosphorylation initiated by the selective proteolysis of cyclin B drives mitotic exit

    James Holder / Shabaz Mohammed / Francis A Barr

    eLife, Vol

    2020  Volume 9

    Abstract: APC/C-mediated proteolysis of cyclin B and securin promotes anaphase entry, inactivating CDK1 and permitting chromosome segregation, respectively. Reduction of CDK1 activity relieves inhibition of the CDK1-counteracting phosphatases PP1 and PP2A-B55, ... ...

    Abstract APC/C-mediated proteolysis of cyclin B and securin promotes anaphase entry, inactivating CDK1 and permitting chromosome segregation, respectively. Reduction of CDK1 activity relieves inhibition of the CDK1-counteracting phosphatases PP1 and PP2A-B55, allowing wide-spread dephosphorylation of substrates. Meanwhile, continued APC/C activity promotes proteolysis of other mitotic regulators. Together, these activities orchestrate a complex series of events during mitotic exit. However, the relative importance of regulated proteolysis and dephosphorylation in dictating the order and timing of these events remains unclear. Using high temporal-resolution proteomics, we compare the relative extent of proteolysis and protein dephosphorylation. This reveals highly-selective rapid proteolysis of cyclin B, securin and geminin at the metaphase-anaphase transition, followed by slow proteolysis of other substrates. Dephosphorylation requires APC/C-dependent destruction of cyclin B and was resolved into PP1-dependent categories with unique sequence motifs. We conclude that dephosphorylation initiated by selective proteolysis of cyclin B drives the bulk of changes observed during mitotic exit.
    Keywords dephosphorylation ; proteolysis ; APC/C ; PP1 ; mitotic exit ; cell cycle ; Medicine ; R ; Science ; Q ; Biology (General) ; QH301-705.5
    Subject code 572
    Language English
    Publishing date 2020-09-01T00:00:00Z
    Publisher eLife Sciences Publications Ltd
    Document type Article ; Online
    Database BASE - Bielefeld Academic Search Engine (life sciences selection)

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  10. Article ; Online: Rab regulation by GEFs and GAPs during membrane traffic.

    Lamber, Ekaterina P / Siedenburg, Ann-Christin / Barr, Francis A

    Current opinion in cell biology

    2019  Volume 59, Page(s) 34–39

    Abstract: Rab GTPases and their regulatory proteins play a crucial role in vesicle-mediated membrane trafficking. During vesicle membrane tethering Rab GTPases are activated by GEFs (guanine nucleotide exchange factors) and then inactivated by GAPs (GTPase ... ...

    Abstract Rab GTPases and their regulatory proteins play a crucial role in vesicle-mediated membrane trafficking. During vesicle membrane tethering Rab GTPases are activated by GEFs (guanine nucleotide exchange factors) and then inactivated by GAPs (GTPase activating proteins). Recent evidence shows that in addition to activating and inactivating Rab GTPases, both Rab GEFs and GAPs directly contribute to membrane tethering events during vesicle traffic. Other studies have extended the range of processes, in which Rabs function, and revealed roles for Rabs and their GAPs in the regulation of autophagy. Here, we will discuss these advances and the emerging relationship between the domain architectures of Rab GEFs and vesicle coat protein complexes linked with GTPases of the Sar, ARF and Arl families in animal cells.
    MeSH term(s) GTPase-Activating Proteins/metabolism ; Guanine Nucleotide Exchange Factors/metabolism ; Humans ; Protein Transport/genetics ; rab GTP-Binding Proteins/genetics
    Chemical Substances GTPase-Activating Proteins ; Guanine Nucleotide Exchange Factors ; rab GTP-Binding Proteins (EC 3.6.5.2)
    Language English
    Publishing date 2019-04-10
    Publishing country England
    Document type Journal Article ; Research Support, Non-U.S. Gov't ; Review
    ZDB-ID 1026381-0
    ISSN 1879-0410 ; 0955-0674
    ISSN (online) 1879-0410
    ISSN 0955-0674
    DOI 10.1016/j.ceb.2019.03.004
    Database MEDical Literature Analysis and Retrieval System OnLINE

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