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  1. Article ; Online: A tribute in memoriam: Michael C. Latham.

    Lawrence, Ruth A

    Breastfeeding medicine : the official journal of the Academy of Breastfeeding Medicine

    2011  Volume 6, Issue 4, Page(s) 163

    MeSH term(s) Breast Feeding ; Child Nutrition Sciences/history ; Famous Persons ; History, 20th Century ; Internationality
    Language English
    Publishing date 2011-08
    Publishing country United States
    Document type Biography ; Historical Article ; Journal Article
    ZDB-ID 2234680-6
    ISSN 1556-8342 ; 1556-8253
    ISSN (online) 1556-8342
    ISSN 1556-8253
    DOI 10.1089/bfm.2011.9987
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  2. Article ; Online: Reply to Gregory J. Nason, Michael A.S. Jewett, and Robert J. Hamilton's Letter to the Editor re: Adam C. Calaway, Lawrence H. Einhorn, Timothy A. Masterson, Richard S. Foster, Clint Cary. Adverse Surgical Outcomes Associated with Robotic Retroperitoneal Lymph Node Dissection Among Patients with Testicular Cancer. Eur Urol 2019;76:607-609: Adverse Surgical Outcomes Associated with Robotic Retroperitoneal Lymph Node Dissection Among Patients with Testicular Cancer.

    Calaway, Adam C / Einhorn, Lawrence H / Masterson, Timothy A / Foster, Richard S / Cary, Clint

    European urology

    2019  Volume 76, Issue 5, Page(s) e141

    MeSH term(s) Humans ; Lymph Node Excision ; Male ; Neoplasms, Germ Cell and Embryonal ; Robotic Surgical Procedures ; Robotics ; Testicular Neoplasms/surgery ; Treatment Outcome
    Language English
    Publishing date 2019-08-20
    Publishing country Switzerland
    Document type Letter ; Comment
    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.2019.08.004
    Database MEDical Literature Analysis and Retrieval System OnLINE

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    In stock of ZB MED Cologne/Königswinter

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

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  3. Book: Headache and facial pain

    Newman, Lawrence C. / Levin, Morris / Halker Singh, Rashmi B. / Michael, Rebecca L.

    (What do I do now?)

    2022  

    Author's details Lawrence C. Newman, Morris Levin, Rashmi B. Halker Singh, Rebecca L. Michael
    Series title What do I do now?
    Keywords Headache / diagnosis ; Headache / therapy ; Headache Disorders / diagnosis ; Headache Disorders / therapy ; Facial Pain / diagnosis ; Facial Pain / therapy ; Diagnosis, Differential
    Language English
    Size viii, 224 Seiten, Illustrationen
    Edition Second edition
    Publisher Oxford University Press
    Publishing place New York, NY
    Publishing country Great Britain
    Document type Book
    Note Includes bibliographical references and index
    HBZ-ID HT021479045
    ISBN 978-0-19-084213-0 ; 9780190842161 ; 9780190842147 ; 9780190842154 ; 0-19-084213-X ; 0190842164 ; 0190842148 ; 0190842156
    Database Catalogue ZB MED Medicine, Health

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    In stock of ZB MED Cologne/Königswinter

    Shelf markLoan statusLocation
    2022 A 1138 available for loan (reading room) Lesesaal EG

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  4. Article ; Online: Understanding insulin and its receptor from their three-dimensional structures.

    Lawrence, Michael C

    Molecular metabolism

    2021  Volume 52, Page(s) 101255

    Abstract: Background: Insulin's discovery 100 years ago and its ongoing use since that time to treat diabetes belies the molecular complexity of its structure and that of its receptor. Advances in single-particle cryo-electron microscopy have over the past three ... ...

    Abstract Background: Insulin's discovery 100 years ago and its ongoing use since that time to treat diabetes belies the molecular complexity of its structure and that of its receptor. Advances in single-particle cryo-electron microscopy have over the past three years revolutionized our understanding of the atomic detail of insulin-receptor interactions.
    Scope of review: This review describes the three-dimensional structure of insulin and its receptor and details on how they interact. This review also highlights the current gaps in our structural understanding of the system.
    Major conclusions: A near-complete picture has been obtained of the hormone receptor interactions, providing new insights into the kinetics of the interactions and necessitating a revision of the extant two-site cross-linking model of hormone receptor engagement. How insulin initially engages the receptor and the receptor's traversed trajectory as it undergoes conformational changes associated with activation remain areas for future investigation.
    MeSH term(s) Amino Acid Sequence ; Animals ; Cryoelectron Microscopy ; Crystallography, X-Ray ; Humans ; Insulin/chemistry ; Insulin/genetics ; Insulin/metabolism ; Protein Multimerization/genetics ; Protein Structure, Tertiary/genetics ; Receptor, Insulin/genetics ; Receptor, Insulin/metabolism ; Receptor, Insulin/ultrastructure
    Chemical Substances Insulin ; Receptor, Insulin (EC 2.7.10.1)
    Language English
    Publishing date 2021-05-13
    Publishing country Germany
    Document type Journal Article ; Research Support, N.I.H., Extramural ; Research Support, Non-U.S. Gov't ; Review
    ZDB-ID 2708735-9
    ISSN 2212-8778 ; 2212-8778
    ISSN (online) 2212-8778
    ISSN 2212-8778
    DOI 10.1016/j.molmet.2021.101255
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  5. Article: Insulin and its receptor: a grand challenge in structural biology.

    Lawrence, Michael C

    Biophysical reviews

    2019  , Page(s) 543–545

    Language English
    Publishing date 2019-06-27
    Publishing country Germany
    Document type Letter
    ZDB-ID 2486483-3
    ISSN 1867-2469 ; 1867-2450
    ISSN (online) 1867-2469
    ISSN 1867-2450
    DOI 10.1007/s12551-019-00559-6
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  6. Article ; Online: Understanding insulin and its receptor from their three-dimensional structures

    Michael C. Lawrence

    Molecular Metabolism, Vol 52, Iss , Pp 101255- (2021)

    2021  

    Abstract: Background: Insulin's discovery 100 years ago and its ongoing use since that time to treat diabetes belies the molecular complexity of its structure and that of its receptor. Advances in single-particle cryo-electron microscopy have over the past three ... ...

    Abstract Background: Insulin's discovery 100 years ago and its ongoing use since that time to treat diabetes belies the molecular complexity of its structure and that of its receptor. Advances in single-particle cryo-electron microscopy have over the past three years revolutionized our understanding of the atomic detail of insulin-receptor interactions. Scope of review: This review describes the three-dimensional structure of insulin and its receptor and details on how they interact. This review also highlights the current gaps in our structural understanding of the system. Major conclusions: A near-complete picture has been obtained of the hormone receptor interactions, providing new insights into the kinetics of the interactions and necessitating a revision of the extant two-site cross-linking model of hormone receptor engagement. How insulin initially engages the receptor and the receptor's traversed trajectory as it undergoes conformational changes associated with activation remain areas for future investigation.
    Keywords Insulin ; Insulin receptor ; Receptor tyrosine kinase ; Protein structure ; Cryo-electron microscopy ; X-ray crystallography ; Internal medicine ; RC31-1245
    Subject code 612
    Language English
    Publishing date 2021-10-01T00:00:00Z
    Publisher Elsevier
    Document type Article ; Online
    Database BASE - Bielefeld Academic Search Engine (life sciences selection)

    Full text online

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    Your chosen title can be delivered directly to ZB MED Cologne location if you are registered as a user at ZB MED Cologne.

  7. Article: Viruses of the

    Overton, Michael S / Manuel, Robert D / Lawrence, C Martin / Snyder, Jamie C

    Frontiers in microbiology

    2023  Volume 14, Page(s) 1258997

    Abstract: Viruses have played a central role in the evolution and ecology of cellular life since it first arose. Investigations into viral molecular biology and ecological dynamics have propelled abundant progress in our understanding of living systems, including ... ...

    Abstract Viruses have played a central role in the evolution and ecology of cellular life since it first arose. Investigations into viral molecular biology and ecological dynamics have propelled abundant progress in our understanding of living systems, including genetic inheritance, cellular signaling and trafficking, and organismal development. As well, the discovery of viral lineages that infect members of all three domains suggest that these lineages originated at the earliest stages of biological evolution. Research into these viruses is helping to elucidate the conditions under which life arose, and the dynamics that directed its early development. Archaeal viruses have only recently become a subject of intense study, but investigations have already produced intriguing and exciting results. STIV was originally discovered in Yellowstone National Park and has been the focus of concentrated research. Through this research, a viral genetic system was created, a novel lysis mechanism was discovered, and the interaction of the virus with cellular ESCRT machinery was revealed. This review will summarize the discoveries within this group of viruses and will also discuss future work.
    Language English
    Publishing date 2023-09-21
    Publishing country Switzerland
    Document type Journal Article ; Review
    ZDB-ID 2587354-4
    ISSN 1664-302X
    ISSN 1664-302X
    DOI 10.3389/fmicb.2023.1258997
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  8. Article ; Online: A thing of beauty: Structure and function of insulin's "aromatic triplet".

    Weiss, Michael A / Lawrence, Michael C

    Diabetes, obesity & metabolism

    2018  Volume 20 Suppl 2, Page(s) 51–63

    Abstract: The classical crystal structure of insulin was determined in 1969 by D.C. Hodgkin et al. following ...

    Abstract The classical crystal structure of insulin was determined in 1969 by D.C. Hodgkin et al. following a 35-year program of research. This structure depicted a hexamer remarkable for its self-assembly as a zinc-coordinated trimer of dimer. Prominent at the dimer interface was an "aromatic triplet" of conserved residues at consecutive positions in the B chain: Phe
    MeSH term(s) Humans ; Hydrocarbons, Aromatic/chemistry ; Insulin/chemistry ; Insulin/metabolism ; Protein Binding/physiology ; Protein Folding ; Protein Structural Elements ; Receptor, Insulin/chemistry ; Receptor, Insulin/physiology
    Chemical Substances Hydrocarbons, Aromatic ; Insulin ; Receptor, Insulin (EC 2.7.10.1)
    Language English
    Publishing date 2018-09-18
    Publishing country England
    Document type Journal Article ; Research Support, N.I.H., Extramural ; Research Support, Non-U.S. Gov't ; Review
    ZDB-ID 1454944-x
    ISSN 1463-1326 ; 1462-8902
    ISSN (online) 1463-1326
    ISSN 1462-8902
    DOI 10.1111/dom.13402
    Database MEDical Literature Analysis and Retrieval System OnLINE

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    In stock of ZB MED Cologne/Königswinter

    Zs.A 5442: Show issues Location:
    Je nach Verfügbarkeit (siehe Angabe bei Bestand)
    bis Jg. 1994: Bestellungen von Artikeln über das Online-Bestellformular
    Jg. 1995 - 2021: Lesesall (2.OG)
    ab Jg. 2022: Lesesaal (EG)

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  9. Article ; Online: Rituximab for Acquired Hemophilia A in the Setting of Bullous Pemphigoid.

    Bell, Maria C / Grove, Daniel C / Isaacs, Michael J / Mark, Lawrence A

    Cutis

    2022  Volume 110, Issue 1, Page(s) E23–E24

    MeSH term(s) Hemophilia A/complications ; Hemophilia A/drug therapy ; Humans ; Pemphigoid, Bullous/diagnosis ; Pemphigoid, Bullous/drug therapy ; Rituximab/therapeutic use
    Chemical Substances Rituximab (4F4X42SYQ6)
    Language English
    Publishing date 2022-09-30
    Publishing country United States
    Document type Letter
    ZDB-ID 391840-3
    ISSN 2326-6929 ; 0011-4162 ; 0151-9522
    ISSN (online) 2326-6929
    ISSN 0011-4162 ; 0151-9522
    DOI 10.12788/cutis.0585
    Database MEDical Literature Analysis and Retrieval System OnLINE

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    In stock of ZB MED Cologne/Königswinter

    Zs.B 1315: Show issues Location:
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    Zs.MG 44: Show issues

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  10. Article ; Online: Single-chain insulin analogs threaded by the insulin receptor αCT domain.

    Smith, Nicholas A / Menting, John G / Weiss, Michael A / Lawrence, Michael C / Smith, Brian J

    Biophysical journal

    2022  Volume 121, Issue 21, Page(s) 4063–4077

    Abstract: ... insulins (SCIs), whose C domains (foreshortened relative to proinsulin) resemble those of the single-chain ... the crystal structure of an ultrastable SCI (C-domain length 6; sequence EEGPRR) bound to modules ... of the insulin receptor (IR) ectodomain (N-terminal α-subunit domains L1-CR and C-terminal αCT peptide; "microreceptor ...

    Abstract Insulin is a mainstay of therapy for diabetes mellitus, yet its thermal stability complicates global transportation and storage. Cold-chain transport, coupled with optimized formulation and materials, prevents to some degree nucleation of amyloid and hence inactivation of hormonal activity. These issues hence motivate the design of analogs with increased stability, with a promising approach being single-chain insulins (SCIs), whose C domains (foreshortened relative to proinsulin) resemble those of the single-chain growth factors (IGFs). We have previously demonstrated that optimized SCIs can exhibit native-like hormonal activity with enhanced thermal stability and marked resistance to fibrillation. Here, we describe the crystal structure of an ultrastable SCI (C-domain length 6; sequence EEGPRR) bound to modules of the insulin receptor (IR) ectodomain (N-terminal α-subunit domains L1-CR and C-terminal αCT peptide; "microreceptor" [μIR]). The structure of the SCI-μIR complex, stabilized by an Fv module, was determined using diffraction data to a resolution of 2.6 Å. Remarkably, the αCT peptide (IR-A isoform) "threads" through a gap between the flexible C domain and the insulin core. To explore such threading, we undertook molecular dynamics simulations to 1) compare threaded with unthreaded binding modes and 2) evaluate effects of C-domain length on these alternate modes. The simulations (employing both conventional and enhanced sampling simulations) provide evidence that very short linkers (C-domain length of -1) would limit gap opening in the SCI and so impair threading. We envisage that analogous threading occurs in the intact SCI-IR complex-rationalizing why minimal C-domain lengths block complete activity-and might be exploited to design novel receptor-isoform-specific analogs.
    MeSH term(s) Receptor, Insulin/metabolism ; Insulin/metabolism ; Models, Molecular ; Protein Binding ; Peptides/chemistry
    Chemical Substances Receptor, Insulin (EC 2.7.10.1) ; Insulin ; Peptides
    Language English
    Publishing date 2022-09-30
    Publishing country United States
    Document type Journal Article ; Research Support, Non-U.S. Gov't ; Research Support, N.I.H., Extramural
    ZDB-ID 218078-9
    ISSN 1542-0086 ; 0006-3495
    ISSN (online) 1542-0086
    ISSN 0006-3495
    DOI 10.1016/j.bpj.2022.09.038
    Database MEDical Literature Analysis and Retrieval System OnLINE

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    In stock of ZB MED Cologne/Königswinter

    Zs.A 235: Show issues Location:
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    Zs.MO 2: Show issues

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