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  1. Article ; Online: Brain changes after COVID-19 - how concerned should we be?

    Kremer, Stéphane / Jäger, H Rolf

    Nature reviews. Neurology

    2022  Volume 18, Issue 6, Page(s) 321–322

    MeSH term(s) Brain ; COVID-19 ; Humans ; SARS-CoV-2
    Language English
    Publishing date 2022-04-04
    Publishing country England
    Document type Journal Article ; Comment
    ZDB-ID 2491514-2
    ISSN 1759-4766 ; 1759-4758
    ISSN (online) 1759-4766
    ISSN 1759-4758
    DOI 10.1038/s41582-022-00661-6
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    In stock of ZB MED Cologne/Königswinter

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  2. Article ; Online: Meningeal inflammation and cerebral vasculitis during acute COVID-19 with spontaneous regression.

    Lersy, François / Kremer, Stéphane

    Intensive care medicine

    2021  Volume 48, Issue 2, Page(s) 233–235

    MeSH term(s) COVID-19 ; Humans ; Inflammation ; SARS-CoV-2 ; Vasculitis, Central Nervous System/complications ; Vasculitis, Central Nervous System/diagnostic imaging
    Language English
    Publishing date 2021-12-16
    Publishing country United States
    Document type Journal Article
    ZDB-ID 80387-x
    ISSN 1432-1238 ; 0340-0964 ; 0342-4642 ; 0935-1701
    ISSN (online) 1432-1238
    ISSN 0340-0964 ; 0342-4642 ; 0935-1701
    DOI 10.1007/s00134-021-06592-y
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  3. Article: Editorial 49

    Kremer, Stéphane / Beaujeux, Remy / Cotton, François

    Journal of neuroradiology = Journal de neuroradiologie

    2022  Volume 49, Issue 2, Page(s) 103

    Language English
    Publishing date 2022-03-29
    Publishing country France
    Document type Editorial
    ZDB-ID 131763-5
    ISSN 1773-0406 ; 0150-9861
    ISSN (online) 1773-0406
    ISSN 0150-9861
    DOI 10.1016/j.neurad.2022.02.005
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  4. Article ; Online: Intrabacterial lipid inclusion-associated proteins: a core machinery conserved from saprophyte Actinobacteria to the human pathogen Mycobacterium tuberculosis.

    Dargham, Tonia / Mallick, Ivy / Kremer, Laurent / Santucci, Pierre / Canaan, Stéphane

    FEBS open bio

    2023  Volume 13, Issue 12, Page(s) 2306–2323

    Abstract: Mycobacterium tuberculosis (Mtb), the aetiologic agent of tuberculosis (TB), stores triacylglycerol (TAG) in the form of intrabacterial lipid inclusions (ILI) to survive and chronically persist within its host. These highly energetic molecules represent ... ...

    Abstract Mycobacterium tuberculosis (Mtb), the aetiologic agent of tuberculosis (TB), stores triacylglycerol (TAG) in the form of intrabacterial lipid inclusions (ILI) to survive and chronically persist within its host. These highly energetic molecules represent a major source of carbon to support bacterial persistence and reactivation, thus playing a leading role in TB pathogenesis. However, despite its physiological and clinical relevance, ILI metabolism in Mtb remains poorly understood. Recent discoveries have suggested that several ILI-associated proteins might be widely conserved across TAG-producing prokaryotes, but still very little is known regarding the nature and the biological functions of these proteins. Herein, we performed an in silico analysis of three independent ILI-associated proteomes previously reported to computationally define a potential core ILI-associated proteome, referred to as ILIome. Our investigation revealed the presence of 70 orthologous proteins that were strictly conserved, thereby defining a minimal ILIome core. We further narrowed our analysis to proteins involved in lipid metabolism and discuss here their putative biological functions, along with their molecular interactions and dynamics at the surface of these bacterial organelles. We also highlight the experimental limitations of the original proteomic investigations and of the present bioinformatic analysis, while describing new technological approaches and presenting biological perspectives in the field. The in silico investigation presented here aims at providing useful datasets that could constitute a scientific resource of broad interest for the mycobacterial community, with the ultimate goal of enlightening ILI metabolism in prokaryotes with a special emphasis on Mtb pathogenesis.
    MeSH term(s) Humans ; Mycobacterium tuberculosis ; Proteomics ; Actinobacteria ; Lipid Metabolism ; Triglycerides/metabolism
    Chemical Substances Triglycerides
    Language English
    Publishing date 2023-11-15
    Publishing country England
    Document type Journal Article ; Research Support, Non-U.S. Gov't
    ZDB-ID 2651702-4
    ISSN 2211-5463 ; 2211-5463
    ISSN (online) 2211-5463
    ISSN 2211-5463
    DOI 10.1002/2211-5463.13721
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  5. Article ; Online: A unified framework for focal intensity change detection and deformable image registration. Application to the monitoring of multiple sclerosis lesions in longitudinal 3D brain MRI.

    Dufresne, Eléonore / Fortun, Denis / Kremer, Stéphane / Noblet, Vincent

    Frontiers in neuroimaging

    2022  Volume 1, Page(s) 1008128

    Abstract: Registration is a crucial step in the design of automatic change detection methods dedicated to longitudinal brain MRI. Even small registration inaccuracies can significantly deteriorate the detection performance by introducing numerous spurious ... ...

    Abstract Registration is a crucial step in the design of automatic change detection methods dedicated to longitudinal brain MRI. Even small registration inaccuracies can significantly deteriorate the detection performance by introducing numerous spurious detections. Rigid or affine registration are usually considered to align baseline and follow-up scans, as a pre-processing step before applying a change detection method. In the context of multiple sclerosis, using deformable registration can be required to capture the complex deformations due to brain atrophy. However, non-rigid registration can alter the shape of appearing and evolving lesions while minimizing the dissimilarity between the two images. To overcome this issue, we consider registration and change detection as intertwined problems that should be solved jointly. To this end, we formulate these two separate tasks as a single optimization problem involving a unique energy that models their coupling. We focus on intensity-based change detection and registration, but the approach is versatile and could be extended to other modeling choices. We show experimentally on synthetic and real data that the proposed joint approach overcomes the limitations of the sequential scheme.
    Language English
    Publishing date 2022-12-22
    Publishing country Switzerland
    Document type Journal Article
    ZDB-ID 3123824-5
    ISSN 2813-1193 ; 2813-1193
    ISSN (online) 2813-1193
    ISSN 2813-1193
    DOI 10.3389/fnimg.2022.1008128
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  6. Article ; Online: Intrabacterial lipid inclusion‐associated proteins

    Tonia Dargham / Ivy Mallick / Laurent Kremer / Pierre Santucci / Stéphane Canaan

    FEBS Open Bio, Vol 13, Iss 12, Pp 2306-

    a core machinery conserved from saprophyte Actinobacteria to the human pathogen Mycobacterium tuberculosis

    2023  Volume 2323

    Abstract: Mycobacterium tuberculosis (Mtb), the aetiologic agent of tuberculosis (TB), stores triacylglycerol (TAG) in the form of intrabacterial lipid inclusions (ILI) to survive and chronically persist within its host. These highly energetic molecules represent ... ...

    Abstract Mycobacterium tuberculosis (Mtb), the aetiologic agent of tuberculosis (TB), stores triacylglycerol (TAG) in the form of intrabacterial lipid inclusions (ILI) to survive and chronically persist within its host. These highly energetic molecules represent a major source of carbon to support bacterial persistence and reactivation, thus playing a leading role in TB pathogenesis. However, despite its physiological and clinical relevance, ILI metabolism in Mtb remains poorly understood. Recent discoveries have suggested that several ILI‐associated proteins might be widely conserved across TAG‐producing prokaryotes, but still very little is known regarding the nature and the biological functions of these proteins. Herein, we performed an in silico analysis of three independent ILI‐associated proteomes previously reported to computationally define a potential core ILI‐associated proteome, referred to as ILIome. Our investigation revealed the presence of 70 orthologous proteins that were strictly conserved, thereby defining a minimal ILIome core. We further narrowed our analysis to proteins involved in lipid metabolism and discuss here their putative biological functions, along with their molecular interactions and dynamics at the surface of these bacterial organelles. We also highlight the experimental limitations of the original proteomic investigations and of the present bioinformatic analysis, while describing new technological approaches and presenting biological perspectives in the field. The in silico investigation presented here aims at providing useful datasets that could constitute a scientific resource of broad interest for the mycobacterial community, with the ultimate goal of enlightening ILI metabolism in prokaryotes with a special emphasis on Mtb pathogenesis.
    Keywords bacterial lipid droplets ; lipid metabolism ; pathogenesis ; triacylglycerol ; Biology (General) ; QH301-705.5
    Subject code 612
    Language English
    Publishing date 2023-12-01T00:00:00Z
    Publisher Wiley
    Document type Article ; Online
    Database BASE - Bielefeld Academic Search Engine (life sciences selection)

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  7. Article: A case of acute disseminate encephalomyelitis after SARS-CoV-2 related acute respiratory distress syndrome.

    Fitouchi, Simon / Heger, Bob / Kremer, Laurent / Kremer, Stéphane / Ohlmann, Patrick

    Journal of neuroradiology = Journal de neuroradiologie

    2020  Volume 48, Issue 6, Page(s) 464–465

    MeSH term(s) COVID-19 ; Encephalomyelitis ; Humans ; Respiratory Distress Syndrome/diagnostic imaging ; Respiratory Distress Syndrome/etiology ; SARS-CoV-2
    Keywords covid19
    Language English
    Publishing date 2020-11-18
    Publishing country France
    Document type Case Reports ; Letter
    ZDB-ID 131763-5
    ISSN 1773-0406 ; 0150-9861
    ISSN (online) 1773-0406
    ISSN 0150-9861
    DOI 10.1016/j.neurad.2020.11.001
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    In stock of ZB MED Cologne/Königswinter

    Zs.A 1062: Show issues Location:
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  8. Article ; Online: Ocular MRI Findings in Patients with Severe COVID-19: A Retrospective Multicenter Observational Study.

    Lecler, Augustin / Cotton, François / Lersy, François / Kremer, Stéphane / Héran, Françoise

    Radiology

    2021  Volume 302, Issue 1, Page(s) E4

    Language English
    Publishing date 2021-12-20
    Publishing country United States
    Document type Published Erratum
    ZDB-ID 80324-8
    ISSN 1527-1315 ; 0033-8419
    ISSN (online) 1527-1315
    ISSN 0033-8419
    DOI 10.1148/radiol.2021219025
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  9. Article ; Online: More on Neurologic Features in Severe SARS-CoV-2 Infection. Reply.

    Helms, Julie / Kremer, Stéphane / Meziani, Ferhat

    The New England journal of medicine

    2020  Volume 382, Issue 26, Page(s) e110

    MeSH term(s) Betacoronavirus ; COVID-19 ; Coronavirus Infections ; Humans ; Nervous System Diseases/virology ; Pandemics ; Pneumonia, Viral ; SARS-CoV-2 ; Severe Acute Respiratory Syndrome
    Keywords covid19
    Language English
    Publishing date 2020-05-26
    Publishing country United States
    Document type Letter ; Comment
    ZDB-ID 207154-x
    ISSN 1533-4406 ; 0028-4793
    ISSN (online) 1533-4406
    ISSN 0028-4793
    DOI 10.1056/NEJMc2015132
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  10. Article ; Online: The roles of tetraspanins in bacterial infections.

    Karam, Jona / Méresse, Stéphane / Kremer, Laurent / Daher, Wassim

    Cellular microbiology

    2020  Volume 22, Issue 12, Page(s) e13260

    Abstract: Tetraspanins, a wide family composed of 33 transmembrane proteins, are associated with different types of proteins through which they arbitrate important cellular processes such as fusion, adhesion, invasion, tissue differentiation and immunological ... ...

    Abstract Tetraspanins, a wide family composed of 33 transmembrane proteins, are associated with different types of proteins through which they arbitrate important cellular processes such as fusion, adhesion, invasion, tissue differentiation and immunological responses. Tetraspanins share a comparable structural design, which consists of four hydrophobic transmembrane domains with cytoplasmic and extracellular loops. They cooperate with different proteins, including other tetraspanins, receptors or signalling proteins to compose functional complexes at the cell surface, designated tetraspanin-enriched microdomains (TEM). Increasing evidences establish that tetraspanins are exploited by numerous intracellular pathogens as a doorway for entering and replicating within human cells. Although previous surveys focused mainly on viruses and parasites, it is now becoming clear that bacteria interact with tetraspanins, using TEM as a "gateway" to infection. In this review, we examine the biological functions of tetraspanins that are relevant to bacterial infective procedures and consider the available data that reveal how different bacteria benefit from host cell tetraspanins in infection and in the pathogenesis of diseases. We will also emphasise the stimulating potentials of targeting tetraspanins for preventing bacterial infectious diseases, using specific neutralising antibodies or anti-adhesion peptide-based therapies. Such innovative therapeutic opportunities may deliver alternatives for fighting difficult-to-manage and drug-resistant bacterial pathogens.
    MeSH term(s) Animals ; Bacterial Infections/microbiology ; Cell Membrane/metabolism ; Humans ; Membrane Proteins/metabolism ; Mice ; Tetraspanins/chemistry ; Tetraspanins/metabolism
    Chemical Substances Membrane Proteins ; Tetraspanins
    Language English
    Publishing date 2020-10-02
    Publishing country England
    Document type Journal Article ; Research Support, Non-U.S. Gov't ; Review
    ZDB-ID 1468320-9
    ISSN 1462-5822 ; 1462-5814
    ISSN (online) 1462-5822
    ISSN 1462-5814
    DOI 10.1111/cmi.13260
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