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  1. Book ; Online: Field guide to the difficult patient interview

    Platt, Frederic W. / Gordon, Geoffrey H.

    (Field guide series)

    2004  

    Author's details Frederic W. Platt, Geoffrey H. Gordon
    Series title Field guide series
    Keywords Physician-patient relations ; Communication ; Medical history taking - methods
    Language English
    Size 1 Online-Ressource (xx, 297 Seiten), Illustrationen
    Edition 2nd ed.
    Publisher Lippincott Williams & Wilkins
    Publishing place Philadelphia
    Document type Book ; Online
    Note Includes bibliographical references and index
    Remark Zugriff für angemeldete ZB MED-Nutzerinnen und -Nutzer
    ISBN 978-0-7817-4774-5 ; 0-7817-4774-0
    Database ZB MED Catalogue: Medicine, Health, Nutrition, Environment, Agriculture

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  2. Book: Field guide to the difficult patient interview

    Platt, Frederic W. / Gordon, Geoffrey H.

    (Field guide)

    1999  

    Author's details Frederic W. Platt ; Geoffrey H. Gordon
    Series title Field guide
    Keywords Physician-Patient Relations ; Communication ; Medical History Taking / methods
    Language English
    Size XVIII, 201 S. : Ill.
    Publisher Lippincott Williams & Wilkins
    Publishing place Philadelphia u.a.
    Publishing country United States
    Document type Book
    HBZ-ID HT010734594
    ISBN 0-7817-2044-3 ; 978-0-7817-2044-1
    Database Catalogue ZB MED Medicine, Health

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    In stock of ZB MED Cologne/Königswinter

    Shelf markLoan statusLocation
    1999 A 4282 order for loan Magazin

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  3. Article ; Online: Can self-awareness be taught? Monkeys pass the mirror test-again.

    Huttunen, Annamarie W / Adams, Geoffrey K / Platt, Michael L

    Proceedings of the National Academy of Sciences of the United States of America

    2017  Volume 114, Issue 13, Page(s) 3281–3283

    Language English
    Publishing date 2017-03-28
    Publishing country United States
    Document type Journal Article
    ZDB-ID 209104-5
    ISSN 1091-6490 ; 0027-8424
    ISSN (online) 1091-6490
    ISSN 0027-8424
    DOI 10.1073/pnas.1701676114
    Database MEDical Literature Analysis and Retrieval System OnLINE

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    In stock of ZB MED Cologne/Königswinter

    Zs.A 1148: Show issues Location:
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  4. Article ; Online: Glimpses of the molecular mechanisms of beta2-microglobulin fibril formation in vitro: aggregation on a complex energy landscape.

    Platt, Geoffrey W / Radford, Sheena E

    FEBS letters

    2009  Volume 583, Issue 16, Page(s) 2623–2629

    Abstract: Beta(2)-microglobulin (beta(2)m) is a 99-residue protein that aggregates to form amyloid fibrils in dialysis-related amyloidosis. The protein provides a powerful model for exploration of the structural molecular mechanisms of fibril formation from a full- ...

    Abstract Beta(2)-microglobulin (beta(2)m) is a 99-residue protein that aggregates to form amyloid fibrils in dialysis-related amyloidosis. The protein provides a powerful model for exploration of the structural molecular mechanisms of fibril formation from a full-length protein in vitro. Fibrils have been assembled from beta(2)m under both low pH conditions, where the precursor is disordered, and at neutral pH where the protein is initially natively folded. Here we discuss the roles of sequence and structure in amyloid formation, the current understanding of the structural mechanisms of the early stages of aggregation of beta(2)m at both low and neutral pH, and the common and distinct features of these assembly pathways.
    MeSH term(s) Amino Acid Sequence ; Amyloid/chemistry ; Entropy ; Humans ; Hydrogen-Ion Concentration ; Protein Conformation ; beta 2-Microglobulin/chemistry
    Chemical Substances Amyloid ; beta 2-Microglobulin
    Language English
    Publishing date 2009-05-09
    Publishing country England
    Document type Journal Article ; Research Support, Non-U.S. Gov't ; Review
    ZDB-ID 212746-5
    ISSN 1873-3468 ; 0014-5793
    ISSN (online) 1873-3468
    ISSN 0014-5793
    DOI 10.1016/j.febslet.2009.05.005
    Database MEDical Literature Analysis and Retrieval System OnLINE

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    Zs.B 282: Show issues Location:
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  5. Article ; Online: Mapping the Aggregation Kinetics of a Therapeutic Antibody Fragment.

    Chakroun, Nesrine / Hilton, David / Ahmad, Shahina S / Platt, Geoffrey W / Dalby, Paul A

    Molecular pharmaceutics

    2016  Volume 13, Issue 2, Page(s) 307–319

    Abstract: The analytical characterization of biopharmaceuticals is a fundamental step in the early stages of development and prediction of their behavior in bioprocesses. Protein aggregation in particular is a common issue as it affects all stages of product ... ...

    Abstract The analytical characterization of biopharmaceuticals is a fundamental step in the early stages of development and prediction of their behavior in bioprocesses. Protein aggregation in particular is a common issue as it affects all stages of product development. In the present work, we investigate the stability and the aggregation kinetics of A33Fab, a therapeutically relevant humanized antibody fragment at a wide range of pH, ionic strength, and temperature. We show that the propensity of A33Fab to aggregate under thermally accelerated conditions is pH and ionic-strength dependent with a stronger destabilizing effect of ionic strength at low pH. In the absence of added salts, A33Fab molecules appear to be protected from aggregation due to electrostatic colloidal repulsion at low pH. Analysis by transmission electron microscopy identified significantly different aggregate species formed at low and high pH. The correlations between apparent midpoints of thermal transitions (Tm,app values), or unfolded mole fractions, and aggregation rates are reported here to be significant only at the elevated incubation temperature of 65 °C, where aggregation from the unfolded state predominates. At all other conditions, particularly at 4-45 °C, aggregation of A33 Fab was predominantly from a native-like state, and the kinetics obeyed Arrhenius behavior. Despite this, the rank order of aggregation rates observed at 45 °C, 23 and 4 °C still did not correlate well to each other, indicating that forced degradation at elevated temperatures was not a good screen for predicting behavior at low temperature.
    MeSH term(s) Antibodies, Monoclonal/chemistry ; Calorimetry, Differential Scanning ; Circular Dichroism ; Humans ; Hydrogen-Ion Concentration ; Immunoglobulin Fragments/chemistry ; Kinetics ; Membrane Glycoproteins/chemistry ; Protein Aggregates ; Protein Conformation ; Protein Multimerization ; Protein Stability
    Chemical Substances Antibodies, Monoclonal ; GPA33 protein, human ; Immunoglobulin Fragments ; Membrane Glycoproteins ; Protein Aggregates
    Language English
    Publishing date 2016-02-01
    Publishing country United States
    Document type Journal Article ; Research Support, Non-U.S. Gov't
    ZDB-ID 2138405-8
    ISSN 1543-8392 ; 1543-8384
    ISSN (online) 1543-8392
    ISSN 1543-8384
    DOI 10.1021/acs.molpharmaceut.5b00387
    Database MEDical Literature Analysis and Retrieval System OnLINE

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    In stock of ZB MED Cologne/Königswinter

    Zs.A 6250: Show issues Location:
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  6. Article ; Online: Probing dynamics within amyloid fibrils using a novel capping method.

    Platt, Geoffrey W / Xue, Wei-Feng / Homans, Steve W / Radford, Sheena E

    Angewandte Chemie (International ed. in English)

    2009  Volume 48, Issue 31, Page(s) 5705–5707

    MeSH term(s) Amino Acid Sequence ; Amyloid/chemistry ; Magnetic Resonance Spectroscopy ; Microscopy, Electron, Transmission ; Molecular Sequence Data ; Peptide Hydrolases/metabolism ; beta 2-Microglobulin/chemistry
    Chemical Substances Amyloid ; beta 2-Microglobulin ; Peptide Hydrolases (EC 3.4.-)
    Language English
    Publishing date 2009
    Publishing country Germany
    Document type Journal Article ; Research Support, Non-U.S. Gov't
    ZDB-ID 2011836-3
    ISSN 1521-3773 ; 1433-7851
    ISSN (online) 1521-3773
    ISSN 1433-7851
    DOI 10.1002/anie.200901343
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  7. Article ; Online: Superchiral Plasmonic Phase Sensitivity for Fingerprinting of Protein Interface Structure.

    Tullius, Ryan / Platt, Geoffrey W / Khosravi Khorashad, Larousse / Gadegaard, Nikolaj / Lapthorn, Adrian J / Rotello, Vincent M / Cooke, Graeme / Barron, Laurence D / Govorov, Alexander O / Karimullah, Affar S / Kadodwala, Malcolm

    ACS nano

    2017  Volume 11, Issue 12, Page(s) 12049–12056

    Abstract: The structure adopted by biomaterials, such as proteins, at interfaces is a crucial parameter in a range of important biological problems. It is a critical property in defining the functionality of cell/bacterial membranes and biofilms (i.e., in ... ...

    Abstract The structure adopted by biomaterials, such as proteins, at interfaces is a crucial parameter in a range of important biological problems. It is a critical property in defining the functionality of cell/bacterial membranes and biofilms (i.e., in antibiotic-resistant infections) and the exploitation of immobilized enzymes in biocatalysis. The intrinsically small quantities of materials at interfaces precludes the application of conventional spectroscopic phenomena routinely used for (bio)structural analysis due to a lack of sensitivity. We show that the interaction of proteins with superchiral fields induces asymmetric changes in retardation phase effects of excited bright and dark modes of a chiral plasmonic nanostructure. Phase retardations are obtained by a simple procedure, which involves fitting the line shape of resonances in the reflectance spectra. These interference effects provide fingerprints that are an incisive probe of the structure of interfacial biomolecules. Using these fingerprints, layers composed of structurally related proteins with differing geometries can be discriminated. Thus, we demonstrate a powerful tool for the bioanalytical toolbox.
    MeSH term(s) Nanostructures/chemistry ; Optical Imaging ; Protein Conformation ; Proteins/chemistry ; Silicon/chemistry
    Chemical Substances Proteins ; Silicon (Z4152N8IUI)
    Language English
    Publishing date 2017-12-15
    Publishing country United States
    Document type Journal Article ; Research Support, Non-U.S. Gov't
    ISSN 1936-086X
    ISSN (online) 1936-086X
    DOI 10.1021/acsnano.7b04698
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  8. Article: Probing Dynamics within Amyloid Fibrils Using a Novel Capping Method

    Platt, Geoffrey W / Xue, Wei-Feng / Homans, Steve W / Radford, Sheena E

    Angewandte Chemie. 2009 July 20, v. 48, no. 31

    2009  

    Language English
    Dates of publication 2009-0720
    Size p. 5705-5707.
    Publishing place Wiley-VCH Verlag
    Document type Article
    ZDB-ID 2011836-3
    ISSN 1521-3773 ; 1433-7851
    ISSN (online) 1521-3773
    ISSN 1433-7851
    DOI 10.1002/anie.200901343
    Database NAL-Catalogue (AGRICOLA)

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  9. Article: Allergen immobilisation and signal amplification by quantum dots for use in a biosensor assay of IgE in serum

    Platt, Geoffrey W / Francesco Damin / Gilbert Skorski / Isabelle Metton / Marcella Chiari / Marcus J. Swann / Marina Cretich

    Biosensors & bioelectronics. 2014 Feb. 15, v. 52

    2014  

    Abstract: The production of biosensors for point of care diagnostics usually requires the immobilisation and storage of protein (for example, antigen or antibody) on a sensor surface, in a manner that retains a high degree of activity and low levels of non- ... ...

    Abstract The production of biosensors for point of care diagnostics usually requires the immobilisation and storage of protein (for example, antigen or antibody) on a sensor surface, in a manner that retains a high degree of activity and low levels of non-specific binding. These characteristics have been assessed for polymer immobilised antigens (allergens) using an IgG binding assay and demonstrated further by assay with serum containing reactive IgEs.The activity of allergens immobilised on sensor chips using copoly(DMA–NAS–MAPS) and a spotting technique, as well as the specificity of their binding interactions with cognate immunoglobulins was assessed using Dual Polarisation Interferometry (DPI). The data obtained indicate that the allergens studied remain stable over long periods of time (at least 114 days). This performance compared favourably with other immobilisation methods. Allergen coated chips were tested in an anti-casein IgE assay using human serum from allergic and non-allergic donors. Detection of both total Ig and specific IgE was demonstrated using a secondary anti-IgE antibody. Furthermore, optical signal enhancement with streptavidin conjugated quantum dots was shown to yield responses for samples below 0.84ng/mL (0.35KU/L) of IgE, which overlap with the industrial quasi-standard ImmunoCAP® and is the clinically relevant threshold used to classify serum samples from allergic individuals.
    Keywords allergens ; antibodies ; biosensors ; blood serum ; diagnostic techniques ; humans ; immunoglobulin E ; immunoglobulin G ; interferometry ; polymers ; quantum dots ; streptavidin
    Language English
    Dates of publication 2014-0215
    Size p. 82-88.
    Publishing place Elsevier B.V.
    Document type Article
    ZDB-ID 1011023-9
    ISSN 1873-4235 ; 0956-5663
    ISSN (online) 1873-4235
    ISSN 0956-5663
    DOI 10.1016/j.bios.2013.08.019
    Database NAL-Catalogue (AGRICOLA)

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    In stock of ZB MED Cologne/Königswinter

    Zs.A 2275: Show issues Location:
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  10. Book: Field guide to the difficult patient interview

    Platt, Frederic W / Gordon, Geoffrey H

    (Field guide series)

    2004  

    Author's details Frederic W. Platt, Geoffrey H. Gordon
    Series title Field guide series
    MeSH term(s) Physician-Patient Relations ; Communication ; Medical History Taking/methods
    Language English
    Size xx, 297 p. :, ill.
    Edition 2nd ed.
    Publisher Lippincott Williams & Wilkins
    Publishing place Philadelphia
    Document type Book
    ISBN 9780781747745 ; 0781747740
    Database Catalogue of the US National Library of Medicine (NLM)

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