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  1. Article ; Online: Reply from Authors re: Declan G. Murphy, Anthony J. Costello. How Can the Autonomic Nervous System Contribute to Urinary Continence Following Radical Prostatectomy? A "Boson-like" Conundrum. Eur Urol 2013;63:445-7: Sparing of the Neurovascular Bundle Leads to Improved Rates of Continence.

    Tewari, Ashutosh / Ludwig, Wesley / Takenaka, Atsushi / Srivastava, Abhishek / Chopra, Sameer / Pham, Anthony / Sooriakumaran, Prasanna / Durand, Matthieu / Chughtai, Bilal / Gruschow, Siobhan / Peyser, Alexandra / Harneja, Niyati / Leung, Robert / Lee, Richard / Herman, Michael / Robinson, Brian / Shevchuk, Maria

    publication RETRACTED

    European urology

    2013  Volume 63, Issue 3, Page(s) 447–449

    MeSH term(s) Autonomic Nervous System/surgery ; Humans ; Male ; Postoperative Complications/etiology ; Postoperative Complications/prevention & control ; Prostate/innervation ; Prostate/surgery ; Prostatectomy/adverse effects ; Prostatic Neoplasms/surgery ; Urinary Incontinence/etiology ; Urinary Incontinence/prevention & control
    Language English
    Publishing date 2013-03
    Publishing country Switzerland
    Document type Editorial ; Retracted Publication
    ZDB-ID 193790-x
    ISSN 1873-7560 ; 1421-993X ; 0302-2838
    ISSN (online) 1873-7560 ; 1421-993X
    ISSN 0302-2838
    DOI 10.1016/j.eururo.2012.09.021
    Database MEDical Literature Analysis and Retrieval System OnLINE

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    Zs.A 1247: Show issues Location:
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    Zs.MO 294: Show issues

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  2. Article ; Online: The role of cholesterol binding in the control of cholesterol by the Scap-Insig system.

    Lee, Anthony G

    European biophysics journal : EBJ

    2022  Volume 51, Issue 4-5, Page(s) 385–399

    Abstract: Scap and Insig, two proteins embedded in the membrane of the endoplasmic reticulum (ER), regulate the synthesis of cholesterol in animal cells by forming a dimer in the presence of high concentrations of cholesterol. Cryo-electron microscopic structures ... ...

    Abstract Scap and Insig, two proteins embedded in the membrane of the endoplasmic reticulum (ER), regulate the synthesis of cholesterol in animal cells by forming a dimer in the presence of high concentrations of cholesterol. Cryo-electron microscopic structures for the Scap-Insig dimer show a sterol-binding site at the dimer interface, but none of the structures include cholesterol itself. Here, a molecular docking approach developed to characterise cholesterol binding to the transmembrane (TM) regions of membrane proteins is used to characterise cholesterol binding to sites on the TM surface of the dimer and to the interfacial binding site. Binding of cholesterol is also observed at sites on the extra-membranous luminal domains of Scap, but the properties of these sites suggest that they will be unoccupied in vivo. Comparing the structure of Scap in the dimer with that predicted by AlphaFold for monomeric Scap suggests that dimer formation could result in relocation of TM helix 7 of Scap and of the loop between TM6 and 7, and that this could be the key change on Scap that signals that there is a high concentration of cholesterol in the ER.
    MeSH term(s) Animals ; Cholesterol/metabolism ; Endoplasmic Reticulum/metabolism ; Intracellular Signaling Peptides and Proteins/metabolism ; Membrane Proteins/metabolism ; Molecular Docking Simulation
    Chemical Substances Intracellular Signaling Peptides and Proteins ; Membrane Proteins ; Cholesterol (97C5T2UQ7J)
    Language English
    Publishing date 2022-06-19
    Publishing country Germany
    Document type Journal Article
    ZDB-ID 283671-3
    ISSN 1432-1017 ; 0175-7571
    ISSN (online) 1432-1017
    ISSN 0175-7571
    DOI 10.1007/s00249-022-01606-z
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  3. Article ; Online: Interfacial binding sites for cholesterol on GABA

    Lee, Anthony G

    Biophysical journal

    2021  Volume 120, Issue 13, Page(s) 2710–2722

    Abstract: γ-Aminobutyric acid type A ( ... ...

    Abstract γ-Aminobutyric acid type A (GABA
    MeSH term(s) Binding Sites ; Cholesterol ; Molecular Docking Simulation ; Neurosteroids ; Receptors, GABA-A/metabolism ; gamma-Aminobutyric Acid
    Chemical Substances Neurosteroids ; Receptors, GABA-A ; gamma-Aminobutyric Acid (56-12-2) ; Cholesterol (97C5T2UQ7J)
    Language English
    Publishing date 2021-05-20
    Publishing country United States
    Document type Journal Article
    ZDB-ID 218078-9
    ISSN 1542-0086 ; 0006-3495
    ISSN (online) 1542-0086
    ISSN 0006-3495
    DOI 10.1016/j.bpj.2021.05.009
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  4. Article ; Online: Interfacial Binding Sites for Cholesterol on Kir, Kv, K

    Lee, Anthony G

    Biophysical journal

    2020  Volume 119, Issue 1, Page(s) 35–47

    Abstract: Inwardly rectifying, voltage-gated, two-pore domain, and related ... ...

    Abstract Inwardly rectifying, voltage-gated, two-pore domain, and related K
    MeSH term(s) Binding Sites ; Cholesterol ; Molecular Docking Simulation ; Potassium Channels/metabolism ; Protein Binding
    Chemical Substances Potassium Channels ; Cholesterol (97C5T2UQ7J)
    Language English
    Publishing date 2020-06-04
    Publishing country United States
    Document type Journal Article
    ZDB-ID 218078-9
    ISSN 1542-0086 ; 0006-3495
    ISSN (online) 1542-0086
    ISSN 0006-3495
    DOI 10.1016/j.bpj.2020.05.028
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  5. Article ; Online: Interfacial Binding Sites for Cholesterol on G Protein-Coupled Receptors.

    Lee, Anthony G

    Biophysical journal

    2019  Volume 116, Issue 9, Page(s) 1586–1597

    Abstract: A docking procedure is described that allows the transmembrane surface of a G protein-coupled ...

    Abstract A docking procedure is described that allows the transmembrane surface of a G protein-coupled receptor (GPCR) to be swept rapidly for potential binding sites for cholesterol at the bilayer interfaces on the two sides of the membrane. The procedure matches 89% of the cholesterols resolved in published GPCR crystal structures, when cholesterols likely to be crystal packing artifacts are excluded. Docking poses are shown to form distinct clusters on the protein surface, the clusters corresponding to "greasy hollows" between protein ridges. Docking poses depend on the angle of tilt of the GPCR in the surrounding lipid bilayer. It is suggested that thermal motion could alter the optimal binding pose for a cholesterol molecule, with the range of binding poses within a cluster providing a guide to the range of thermal motions likely for a cholesterol within a binding site.
    MeSH term(s) Binding Sites ; Cholesterol/metabolism ; Crystallography, X-Ray ; Molecular Docking Simulation ; Molecular Dynamics Simulation ; Protein Binding ; Protein Conformation ; Receptors, G-Protein-Coupled/chemistry ; Receptors, G-Protein-Coupled/metabolism
    Chemical Substances Receptors, G-Protein-Coupled ; Cholesterol (97C5T2UQ7J)
    Language English
    Publishing date 2019-04-02
    Publishing country United States
    Document type Journal Article
    ZDB-ID 218078-9
    ISSN 1542-0086 ; 0006-3495
    ISSN (online) 1542-0086
    ISSN 0006-3495
    DOI 10.1016/j.bpj.2019.03.025
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  6. Article ; Online: Interfacial Binding Sites for Cholesterol on TRP Ion Channels.

    Lee, Anthony G

    Biophysical journal

    2019  Volume 117, Issue 10, Page(s) 2020–2033

    Abstract: Transient receptor potential (TRP) channels are members of a large family of ion channels located in membranes rich in cholesterol, some of whose functions are affected by the cholesterol content of the membrane. Here, cholesterol binding to TRPs is ... ...

    Abstract Transient receptor potential (TRP) channels are members of a large family of ion channels located in membranes rich in cholesterol, some of whose functions are affected by the cholesterol content of the membrane. Here, cholesterol binding to TRPs is studied using a docking procedure that allows the transmembrane surface of a TRP to be swept rapidly for potential binding sites at the interfaces on the two sides of the membrane. Cholesterol docking poses determined in this way match 89% of the cholesterol hemisuccinate molecules in published TRP structures when cholesterol hemisuccinate molecules unlikely to represent typical bound cholesterols are excluded. TRPs are tetrameric, with large clefts at the interfaces between subunits; cholesterol poses are located in hollows, largely within these clefts. Comparison of cholesterol poses with phospholipid binding sites suggests that binding of cholesterol to a TRP need not result in displacement of phospholipid molecules from the TRP surface.
    MeSH term(s) Animals ; Binding Sites ; Cholesterol/metabolism ; Cluster Analysis ; Humans ; Mice ; Molecular Docking Simulation ; Phospholipids/metabolism ; Transient Receptor Potential Channels/metabolism
    Chemical Substances Phospholipids ; Transient Receptor Potential Channels ; Cholesterol (97C5T2UQ7J)
    Language English
    Publishing date 2019-10-18
    Publishing country United States
    Document type Journal Article
    ZDB-ID 218078-9
    ISSN 1542-0086 ; 0006-3495
    ISSN (online) 1542-0086
    ISSN 0006-3495
    DOI 10.1016/j.bpj.2019.10.011
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  7. Article ; Online: Superficial X-ray in the treatment of nonaggressive basal and squamous cell carcinoma in the elderly: A 22-year retrospective analysis.

    Mattia, Alexzandra / Thompson, Anthony / Lee, Sang Kyu / Hong, Hyokyoung G / Green, William Harris / Cognetta, Armand B

    Journal of the American Academy of Dermatology

    2024  Volume 90, Issue 5, Page(s) 1052–1054

    MeSH term(s) Humans ; Aged ; Retrospective Studies ; X-Rays ; Carcinoma, Squamous Cell/diagnostic imaging ; Skin Neoplasms/diagnostic imaging ; Skin Neoplasms/pathology ; Radiography ; Carcinoma, Basal Cell/diagnostic imaging ; Carcinoma, Basal Cell/surgery
    Language English
    Publishing date 2024-01-13
    Publishing country United States
    Document type Journal Article
    ZDB-ID 603641-7
    ISSN 1097-6787 ; 0190-9622
    ISSN (online) 1097-6787
    ISSN 0190-9622
    DOI 10.1016/j.jaad.2024.01.010
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  8. Article ; Online: A Database of Predicted Binding Sites for Cholesterol on Membrane Proteins, Deep in the Membrane.

    Lee, Anthony G

    Biophysical journal

    2018  Volume 115, Issue 3, Page(s) 522–532

    Abstract: ... structures. The database includes sites on the transmembrane surfaces of many G-protein coupled receptors ...

    Abstract The outer membranes of animal cells contain high concentrations of cholesterol, of which a small proportion is located deep within the hydrophobic core of the membrane. An automated docking procedure is described that allows the characterization of binding sites for these deep cholesterol molecules on the membrane-spanning surfaces of membrane proteins and in protein cavities or pores, driven by hydrogen bond formation. A database of this class of predicted binding site is described, covering 397 high-resolution structures. The database includes sites on the transmembrane surfaces of many G-protein coupled receptors; within the fenestrations of two-pore K
    MeSH term(s) Binding Sites ; Cholesterol/metabolism ; Databases, Protein ; Membrane Proteins/chemistry ; Membrane Proteins/metabolism ; Molecular Docking Simulation ; Potassium Channels/metabolism ; Protein Binding ; Protein Conformation
    Chemical Substances Membrane Proteins ; Potassium Channels ; Cholesterol (97C5T2UQ7J)
    Language English
    Publishing date 2018-06-26
    Publishing country United States
    Document type Journal Article
    ZDB-ID 218078-9
    ISSN 1542-0086 ; 0006-3495
    ISSN (online) 1542-0086
    ISSN 0006-3495
    DOI 10.1016/j.bpj.2018.06.022
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  9. Book: ATPases

    Lee, Anthony G.

    (Biomembranes ; 5)

    1996  

    Author's details ed.: A. G. Lee
    Series title Biomembranes ; 5
    Collection
    Keywords Adenosinetriphosphatase
    Language English
    Size XII, 428 S. : Ill., graph. Darst.
    Publisher JAI Press
    Publishing place Greenwich, Conn
    Document type Book
    HBZ-ID HT007476610
    ISBN 1-55938-662-2 ; 978-1-55938-662-3
    Database Catalogue ZB MED Medicine, Health

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    Shelf markLoan statusLocation
    1996 A 6349 -5- order for loan Magazin

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  10. Book: Biomembranes / 1

    Lee, Anthony G.

    a multi-volume treatise

    1995  

    Author's details ed.: A. G. Lee
    Collection Biomembranes
    Language English
    Size IX, 279 S. : Ill., graph. Darst.
    Publisher JAI Press
    Publishing place Greenwich, Conn. u.a.
    Publishing country United States
    Document type Book
    HBZ-ID HT007189167
    ISBN 1-55938-658-4 ; 978-1-55938-658-6
    Database Catalogue ZB MED Medicine, Health

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