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  1. Article ; Online: DPP-IV Inhibitor-Associated Angioedema in Patient With Known History of ACE Inhibitor Angioedema.

    Ejikeme, Chidinma / Nwachukwu, Chinedu / Viechweg, John Luis / Ejikeme, Ifunanya / Brescia, Micheal

    Journal of investigative medicine high impact case reports

    2021  Volume 9, Page(s) 23247096211033049

    Abstract: The patient is a 69-year-old male with a past medical history of intellectual disability, hypertension, type 2 diabetes mellitus, and angiotensin-converting enzyme (ACE) inhibitor-associated angioedema who presented to the emergency department with ... ...

    Abstract The patient is a 69-year-old male with a past medical history of intellectual disability, hypertension, type 2 diabetes mellitus, and angiotensin-converting enzyme (ACE) inhibitor-associated angioedema who presented to the emergency department with difficulty breathing. On physical examination, the patient had significant facial edema. Nasal fiber-optic visualization revealed extensive airway edema involving the supraglottic region and the arytenoids. The patient was successfully intubated through the collective teamwork of ENT, anesthesia, and critical care teams. He was managed in the intensive care unit until recovery. Workup for markers for allergic causes of angioedema were within normal limits. Further investigation revealed that symptoms developed following the initiation of a dipeptidyl peptidase 4 (DPP-IV) inhibitor. The angiotensin-converting enzyme and DPP-IV play a significant role in the metabolism of bradykinin and substance P to their inactive metabolites. The complex interplay between the enzymes in the high-molecular-weight kininogen (HWMK) system may increase the risk of angioedema in patients with a known history of ACE inhibitor-associated angioedema when placed on a DPP-IV inhibitor. This case report highlights the pathophysiology involved.
    MeSH term(s) Aged ; Angioedema/chemically induced ; Angioedema/diagnosis ; Angiotensin-Converting Enzyme Inhibitors/adverse effects ; Bradykinin ; Diabetes Mellitus, Type 2 ; Dipeptidyl-Peptidase IV Inhibitors/adverse effects ; Humans ; Male
    Chemical Substances Angiotensin-Converting Enzyme Inhibitors ; Dipeptidyl-Peptidase IV Inhibitors ; Bradykinin (S8TIM42R2W)
    Language English
    Publishing date 2021-07-08
    Publishing country United States
    Document type Case Reports ; Journal Article
    ZDB-ID 2710326-2
    ISSN 2324-7096 ; 2324-7096
    ISSN (online) 2324-7096
    ISSN 2324-7096
    DOI 10.1177/23247096211033049
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  2. Article ; Online: Hepatosplenic Abscess From

    Ejikeme, Chidinma / Nwachukwu, Onyeka / Ayad, Sarah / Rath, Payal / Ejikeme, Ifunanya / Salamera, Julius

    Journal of investigative medicine high impact case reports

    2021  Volume 9, Page(s) 23247096211033046

    Abstract: ... ...

    Abstract Invasive
    MeSH term(s) Bacteremia ; Diabetes Mellitus/epidemiology ; Female ; Humans ; Klebsiella Infections/complications ; Klebsiella Infections/drug therapy ; Klebsiella pneumoniae ; Liver Abscess, Pyogenic/epidemiology ; Middle Aged
    Language English
    Publishing date 2021-07-20
    Publishing country United States
    Document type Case Reports ; Journal Article
    ZDB-ID 2710326-2
    ISSN 2324-7096 ; 2324-7096
    ISSN (online) 2324-7096
    ISSN 2324-7096
    DOI 10.1177/23247096211033046
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  3. Article: Mechanics of the Microtubule Seam Interface Probed by Molecular Simulations and in Vitro Severing Experiments

    Szatkowski, Lukasz / Belonogov, Liudmila / Dima, Ruxandra I / Ejikeme, Ifunanya / Jiang, Nan / Merz, Dale R / Ross, Jennifer L

    Journal of physical chemistry. 2019 May 22, v. 123, no. 23

    2019  

    Abstract: Microtubules (MTs) are structural components essential for cell morphology and organization. It has recently been shown that defects in the filament’s lattice structure can be healed to create stronger filaments in a local area and ultimately cause ... ...

    Abstract Microtubules (MTs) are structural components essential for cell morphology and organization. It has recently been shown that defects in the filament’s lattice structure can be healed to create stronger filaments in a local area and ultimately cause global changes in MT organization and cell mobility. The ability to break, causing a defect, and heal appears to be a physiologically relevant and important feature of the MT structure. Defects can be created by MT severing enzymes and are target sites for complete severing or for healing by newly incorporated dimers. One particular lattice defect, the MT lattice ‘‘seam” interface, is a location often speculated to be a weak site, a site of disassembly, or a target site for MT binding proteins. Despite seams existing in many MT structures, very little is known about the seam’s role in MT function and dynamics. In this study, we probed the mechanical stability of the seam interface by applying coarse-grained indenting molecular dynamics. We found that the seam interface is as structurally robust as the typical lattice structure of MTs. Our results suggest that, unlike prior results that claim the seam is a weak site, it is just as strong as any other location on the MT, corroborating recent mechanical measurements.
    Keywords binding proteins ; enzymes ; mechanics ; microtubules ; molecular dynamics
    Language English
    Dates of publication 2019-0522
    Size p. 4888-4900.
    Publishing place American Chemical Society
    Document type Article
    ISSN 1520-5207
    DOI 10.1021/acs.jpcb.9b03059
    Database NAL-Catalogue (AGRICOLA)

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  4. Article ; Online: Mechanics of the Microtubule Seam Interface Probed by Molecular Simulations and in Vitro Severing Experiments.

    Szatkowski, Lukasz / Merz, Dale R / Jiang, Nan / Ejikeme, Ifunanya / Belonogov, Liudmila / Ross, Jennifer L / Dima, Ruxandra I

    The journal of physical chemistry. B

    2019  Volume 123, Issue 23, Page(s) 4888–4900

    Abstract: Microtubules (MTs) are structural components essential for cell morphology and organization. It has recently been shown that defects in the filament's lattice structure can be healed to create stronger filaments in a local area and ultimately cause ... ...

    Abstract Microtubules (MTs) are structural components essential for cell morphology and organization. It has recently been shown that defects in the filament's lattice structure can be healed to create stronger filaments in a local area and ultimately cause global changes in MT organization and cell mobility. The ability to break, causing a defect, and heal appears to be a physiologically relevant and important feature of the MT structure. Defects can be created by MT severing enzymes and are target sites for complete severing or for healing by newly incorporated dimers. One particular lattice defect, the MT lattice ''seam" interface, is a location often speculated to be a weak site, a site of disassembly, or a target site for MT binding proteins. Despite seams existing in many MT structures, very little is known about the seam's role in MT function and dynamics. In this study, we probed the mechanical stability of the seam interface by applying coarse-grained indenting molecular dynamics. We found that the seam interface is as structurally robust as the typical lattice structure of MTs. Our results suggest that, unlike prior results that claim the seam is a weak site, it is just as strong as any other location on the MT, corroborating recent mechanical measurements.
    MeSH term(s) Microtubules/chemistry ; Molecular Dynamics Simulation ; Polymerization
    Language English
    Publishing date 2019-06-03
    Publishing country United States
    Document type Journal Article ; Research Support, U.S. Gov't, Non-P.H.S.
    ISSN 1520-5207
    ISSN (online) 1520-5207
    DOI 10.1021/acs.jpcb.9b03059
    Database MEDical Literature Analysis and Retrieval System OnLINE

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    Order via subito

    This service is chargeable due to the Delivery terms set by subito. Orders including an article and supplementary material will be classified as separate orders. In these cases, fees will be demanded for each order.

    Inter-library loan at ZB MED

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

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