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Article: Fatal Puumala Hantavirus Infection in a Patient with Common Variable Immunodeficiency (CVID).

Steininger, Philipp / Herbst, Larissa / Bihlmaier, Karl / Willam, Carsten / Körper, Sixten / Schrezenmeier, Hubert / Klüter, Harald / Pfister, Frederick / Amann, Kerstin / Weiss, Sabrina / Krüger, Detlev H / Zimmermann, Robert / Korn, Klaus / Hofmann, Jörg / Harrer, Thomas

Microorganisms

2023 Volume 11, Issue 2

Abstract: Puumala hantavirus (PUUV) infections usually show a mild or moderate clinical course, but may sometimes also lead to life-threatening disease. Here, we report on a 60-year-old female patient with common variable immunodeficiency (CVID) who developed a ... ...

Abstract	Puumala hantavirus (PUUV) infections usually show a mild or moderate clinical course, but may sometimes also lead to life-threatening disease. Here, we report on a 60-year-old female patient with common variable immunodeficiency (CVID) who developed a fatal PUUV infection with persistent renal failure, thrombocytopenia, and CNS infection with impaired consciousness and tetraparesis. Hantavirus-specific antibodies could not be detected due to the humoral immunodeficiency. Diagnosis and virological monitoring were based on the quantitative detection of PUUV RNA in blood, cerebrospinal fluid, bronchial lavage, and urine, where viral RNA was found over an unusually extended period of one month. Due to clinical deterioration and virus persistence, treatment with ribavirin was initiated. Additionally, fresh frozen plasma (FFP) from convalescent donors with a history of PUUV infection was administered. Despite viral clearance, the clinical condition of the patient did not improve and the patient died on day 81 of hospitalization. This case underlines the importance of the humoral immune response for the course of PUUV disease and illustrates the need for PCR-based virus diagnostics in those patients. Due to its potential antiviral activity, convalescent plasma should be considered in the therapy of severe hantavirus diseases.
Language	English
Publishing date	2023-01-21
Publishing country	Switzerland
Document type	Case Reports
ZDB-ID	2720891-6
ISSN	2076-2607
ISSN	2076-2607
DOI	10.3390/microorganisms11020283
Database	MEDical Literature Analysis and Retrieval System OnLINE

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Book ; Online ; Thesis: The disulfide relay system of mitochondria is connected to the respiratory chain

Bihlmaier, Karl

2010

Author's details	vorgelegt von Karl Bihlmaier
Language	English
Size	Online-Ressource
Document type	Book ; Online ; Thesis
Thesis / German Habilitation thesis	Kaiserslautern, Techn. Univ., Diss., 2009
Database	Library catalogue of the German National Library of Science and Technology (TIB), Hannover

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Article ; Online: β-(1→3)-D-glucan- and mannan-guided early termination of antifungal therapy in ICU patients: a randomized controlled study.

Erb, Timothy / Mihai, Sidonia / Strauß, Richard / Herbst, Larissa / Castellanos, Ixchel / Diesch, Katharina / Cipa, Franziska / Bihlmaier, Karl / Lang, Anne-Katharina / Ganslmayer, Marion / Willam, Carsten / Bremer, Frank / Fürst, Julia / Beyer, Christian / Bogdan, Christian / Rath, Anca / Held, Jürgen

Antimicrobial agents and chemotherapy

2023 Volume 67, Issue 11, Page(s) e0072523

Abstract: ... ...

Abstract	Candida
MeSH term(s)	Adult ; Humans ; Antifungal Agents/therapeutic use ; Mannans ; Glucans ; Prospective Studies ; beta-Glucans ; Candidiasis, Invasive/drug therapy ; Intensive Care Units ; Biomarkers
Chemical Substances	Antifungal Agents ; Mannans ; Glucans ; beta-Glucans ; Biomarkers
Language	English
Publishing date	2023-10-12
Publishing country	United States
Document type	Randomized Controlled Trial ; Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	217602-6
ISSN	1098-6596 ; 0066-4804
ISSN (online)	1098-6596
ISSN	0066-4804
DOI	10.1128/aac.00725-23
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Book ; Online ; Thesis: The disulfide relay system of mitochondria is connected to the respiratory chain

Bihlmaier, Karl [Verfasser]

2010

Author's details	vorgelegt von Karl Bihlmaier
Keywords	Biowissenschaften, Biologie ; Life Science, Biology
Subject code	sg570
Language	English
Document type	Book ; Online ; Thesis
Database	Digital theses on the web

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Article ; Online: Disseminated Multifocal Intracerebral Bleeding Events in Three Coronavirus Disease 2019 Patients on Extracorporeal Membrane Oxygenation As Rescue Therapy.

Bihlmaier, Karl / Coras, Roland / Willam, Carsten / Grampp, Steffen / Jabari, Samir / Eichhorn, Philip / Haller, Florian / Kuramatsu, Joji / Schwab, Stefan / Castellanos, Ixchel / Birkholz, Torsten / Schüttler, Jürgen / Altmeppen, Jürgen / Schiffer, Mario / Herbst, Larissa

Critical care explorations

2020 Volume 2, Issue 9, Page(s) e0218

Abstract: Objectives: To describe three coronavirus disease 2019 patients suffering from acute respiratory distress syndrome under venovenous extracorporeal membrane oxygenation therapy and tight anticoagulation monitoring presenting a novel pattern of multifocal ...

Abstract	Objectives: To describe three coronavirus disease 2019 patients suffering from acute respiratory distress syndrome under venovenous extracorporeal membrane oxygenation therapy and tight anticoagulation monitoring presenting a novel pattern of multifocal brain hemorrhage in various degrees in all cerebral and cerebellar lobes. Design: Clinical observation of three patients. Post mortem examinations. Setting: Two ICUs at the University Hospital Erlangen. Patients: Three patients (medium age 56.6 yr, two male with hypertension and diabetes, one female with no medical history) developed severe acute respiratory distress syndrome on the basis of a severe acute respiratory syndrome coronavirus 2 infection. All required mechanical ventilation and venovenous extracorporeal membrane oxygenation support. Interventions: Clinical observation, CT, data extraction from electronic medical records, and post mortem examinations. Main results: We report on an unusual multifocal bleeding pattern in the white matter in three cases with severe acute respiratory distress syndrome due to coronavirus disease 2019 undergoing venovenous extracorporeal membrane oxygenation therapy. Bleeding pattern with consecutive herniation was found in CT scans as well as in neuropathologic post mortem examinations. Frequency for this unusual brain hemorrhage in coronavirus disease 2019 patients with extracorporeal membrane oxygenation therapy at our hospital is currently 50%, whereas bleeding events in extracorporeal membrane oxygenation patients generally occur at 10-15%. Conclusions: Multifocality and high frequency of the unusual white matter hemorrhage pattern suggest a coherence to coronavirus disease 2019. Neuropathological analyses showed circumscribed thrombotic cerebrovascular occlusions, which eventually led to microvascular and later on macrovascular disseminated bleeding events. However, signs of cerebrovascular inflammation could not be detected. Polymerase chain reaction analyses of brain tissue or cerebrospinal fluid remained negative. Increased susceptibility for fatal bleeding events should be taken into consideration in terms of systemic anticoagulation strategies in coronavirus disease 2019.
Keywords	covid19
Language	English
Publishing date	2020-09-15
Publishing country	United States
Document type	Journal Article
ISSN	2639-8028
ISSN (online)	2639-8028
DOI	10.1097/CCE.0000000000000218
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Article: In vitro import of proteins into isolated mitochondria.

Bihlmaier, Karl / Bien, Melanie / Herrmann, Johannes M

Methods in molecular biology (Clifton, N.J.)

2008 Volume 457, Page(s) 85–94

Abstract: Import of proteins is of vital importance for the biogenesis of mitochondria. The vast majority of mitochondrial proteins is encoded within the nuclear genome and translocated into various mitochondrial compartments after translation in the cytosol as ... ...

Abstract	Import of proteins is of vital importance for the biogenesis of mitochondria. The vast majority of mitochondrial proteins is encoded within the nuclear genome and translocated into various mitochondrial compartments after translation in the cytosol as preproteins. Even in rather primitive eukaryotes like yeasts, these are 700 to 1,000 different proteins, whereas only a handful of proteins is encoded in the mitochondrial DNA. In vitro import studies are important tools to understand import mechanisms and pathways. Using isolated mitochondria and radioactively labeled precursor proteins, it was possible to identify several import machineries and pathways consisting of a large number of components during the last decades.
MeSH term(s)	Mitochondria/metabolism ; Mitochondrial Proteins/biosynthesis ; Mitochondrial Proteins/metabolism ; Molecular Biology/methods ; Protein Biosynthesis ; Protein Precursors/metabolism ; Protein Transport ; Saccharomyces cerevisiae/metabolism
Chemical Substances	Mitochondrial Proteins ; Protein Precursors
Language	English
Publishing date	2008-11-18
Publishing country	United States
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ISSN	1064-3745
ISSN	1064-3745
DOI	10.1007/978-1-59745-261-8_6
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Article ; Online: The disulfide relay of the intermembrane space of mitochondria: an oxygen-sensing system?

Bihlmaier, Karl / Mesecke, Nikola / Kloeppel, Christine / Herrmann, Johannes M

Annals of the New York Academy of Sciences

2008 Volume 1147, Page(s) 293–302

Abstract: The intermembrane space of mitochondria contains many proteins that lack classical mitochondrial targeting sequences. Instead, these proteins often show characteristic patterns of cysteine residues that are critical for their accumulation in the ... ...

Abstract	The intermembrane space of mitochondria contains many proteins that lack classical mitochondrial targeting sequences. Instead, these proteins often show characteristic patterns of cysteine residues that are critical for their accumulation in the organelle. Import of these proteins is catalyzed by two essential components, Mia40 and Erv1. Mia40 is a protein in the intermembrane space that directly binds newly imported proteins via disulfide bonds. By reorganization of these bonds, intramolecular disulfide bonds are formed in the imported proteins, which are thereby released from Mia40 into the intermembrane space. Because folded proteins are unable to traverse the import pore of the outer membrane, this leads to a permanent location of these proteins within the mitochondria. During this reaction, Mia40 becomes reduced and needs to be re-oxidized to regain its activity. Oxidation of Mia40 is carried out by Erv1, a conserved flavine adenine dinucleotide (FAD)-binding sulfhydryl oxidase. Erv1 directly interacts with Mia40 and shuttles electrons from reduced Mia40 to oxidized cytochrome c, from whence they flow through cytochrome oxidase to molecular oxygen. The connection of the disulfide relay with the respiratory chain not only significantly increases the efficiency of the oxidase activity, but also prevents the formation of potentially deleterious hydrogen peroxide. The oxidative activity of Erv1 strongly depends on the oxygen concentration in mitochondria. Erv1, therefore, may function as a molecular switch that adapts mitochondrial activities to the oxygen levels in the cell.
MeSH term(s)	Animals ; Cytosol/metabolism ; Disulfides/metabolism ; Humans ; Mitochondria/metabolism ; Oxygen/metabolism ; Protein Transport
Chemical Substances	Disulfides ; Oxygen (S88TT14065)
Language	English
Publishing date	2008-12
Publishing country	United States
Document type	Journal Article ; Research Support, Non-U.S. Gov't ; Review
ZDB-ID	211003-9
ISSN	1749-6632 ; 0077-8923
ISSN (online)	1749-6632
ISSN	0077-8923
DOI	10.1196/annals.1427.005
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Article ; Online: Inaccurately assembled cytochrome c oxidase can lead to oxidative stress-induced growth arrest.

Bode, Manuela / Longen, Sebastian / Morgan, Bruce / Peleh, Valentina / Dick, Tobias P / Bihlmaier, Karl / Herrmann, Johannes M

Antioxidants & redox signaling

2013 Volume 18, Issue 13, Page(s) 1597–1612

Abstract: Aims: To identify yeast mutants that show a strong redox dependence of the ability to respire, we systematically screened a yeast deletion library for mutants that require the presence of reductants for growth on nonfermentable carbon sources.: ... ...

Abstract	Aims: To identify yeast mutants that show a strong redox dependence of the ability to respire, we systematically screened a yeast deletion library for mutants that require the presence of reductants for growth on nonfermentable carbon sources. Results: Respirative growth of 44 yeast mutants was significantly improved by the addition of dithiothreitol or glutathione. Two mutants that were strongly stimulated by reductants lacked the proteins Cmc1 and Coa4. Both proteins belong to the family of "twin Cx(9)C" proteins present in the intermembrane space of mitochondria. Deletion of CMC1 or COA4 leads to assembly defects of cytochrome c oxidase, in particular to the lack of Cox1 and rapid degradation of Cox2 and Cox3. Interestingly, the presence of the reductants does not suppress these assembly defects and the levels of cytochrome c oxidase remain reduced. Reductants and antioxidants such as ascorbic acid rather counteract the effects of hydrogen peroxide that is produced from partially assembled cytochrome c oxidase intermediates. Innovation: Here we show that oxidative stress generated by the accumulation of partially assembled respiratory chain complexes prevents growth on carbon sources that force cells to respire. Conclusion: Defects in the assembly of cytochrome c oxidase can lead to increased production of hydrogen peroxide, which is sensed in cells and blocks their proliferation. We propose that this redox-regulated feedback regulation specifically slows down the propagation of cells carrying respiratory chain mutations in order to select for cells of high mitochondrial fitness.
MeSH term(s)	Carbon/metabolism ; Catalase/genetics ; Catalase/metabolism ; Cell Cycle Checkpoints ; Cytosol/metabolism ; Electron Transport Complex IV/metabolism ; Energy Metabolism ; Fungal Proteins/genetics ; Fungal Proteins/metabolism ; Gene Expression ; Glycerol/metabolism ; Hydrogen Peroxide/metabolism ; Mitochondria/genetics ; Mitochondria/metabolism ; Mitochondrial Proteins/genetics ; Mitochondrial Proteins/metabolism ; Mutation ; Oxidative Stress ; Reducing Agents/pharmacology ; Yeasts/drug effects ; Yeasts/genetics ; Yeasts/growth & development ; Yeasts/metabolism
Chemical Substances	Fungal Proteins ; Mitochondrial Proteins ; Reducing Agents ; Carbon (7440-44-0) ; Hydrogen Peroxide (BBX060AN9V) ; Catalase (EC 1.11.1.6) ; Electron Transport Complex IV (EC 1.9.3.1) ; Glycerol (PDC6A3C0OX)
Language	English
Publishing date	2013-01-15
Publishing country	United States
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	1483836-9
ISSN	1557-7716 ; 1523-0864
ISSN (online)	1557-7716
ISSN	1523-0864
DOI	10.1089/ars.2012.4685
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Article: The disulfide relay system of mitochondria is connected to the respiratory chain

Bihlmaier, Karl / Mesecke, Nikola / Terziyska, Nadia / Bien, Melanie / Hell, Kai / Herrmann, Johannes M

Journal of cell biology. 2007 Nov. 5, v. 179, no. 3

2007

Abstract: All proteins of the intermembrane space of mitochondria are encoded by nuclear genes and synthesized in the cytosol. Many of these proteins lack presequences but are imported into mitochondria in an oxidation-driven process that relies on the activity of ...

Abstract	All proteins of the intermembrane space of mitochondria are encoded by nuclear genes and synthesized in the cytosol. Many of these proteins lack presequences but are imported into mitochondria in an oxidation-driven process that relies on the activity of Mia40 and Erv1. Both factors form a disulfide relay system in which Mia40 functions as a receptor that transiently interacts with incoming polypeptides via disulfide bonds. Erv1 is a sulfhydryl oxidase that oxidizes and activates Mia40, but it has remained unclear how Erv1 itself is oxidized. Here, we show that Erv1 passes its electrons on to molecular oxygen via interaction with cytochrome c and cytochrome c oxidase. This connection to the respiratory chain increases the efficient oxidation of the relay system in mitochondria and prevents the formation of toxic hydrogen peroxide. Thus, analogous to the system in the bacterial periplasm, the disulfide relay in the intermembrane space is connected to the electron transport chain of the inner membrane.
Language	English
Dates of publication	2007-1105
Size	p. 389-395.
Publishing place	The Rockefeller University Press
Document type	Article
ZDB-ID	218154-x
ISSN	1540-8140 ; 0021-9525
ISSN (online)	1540-8140
ISSN	0021-9525
Database	NAL-Catalogue (AGRICOLA)

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Article: The disulfide relay system of mitochondria is connected to the respiratory chain.

Bihlmaier, Karl / Mesecke, Nikola / Terziyska, Nadia / Bien, Melanie / Hell, Kai / Herrmann, Johannes M

The Journal of cell biology

2007 Volume 179, Issue 3, Page(s) 389–395

Abstract	All proteins of the intermembrane space of mitochondria are encoded by nuclear genes and synthesized in the cytosol. Many of these proteins lack presequences but are imported into mitochondria in an oxidation-driven process that relies on the activity of Mia40 and Erv1. Both factors form a disulfide relay system in which Mia40 functions as a receptor that transiently interacts with incoming polypeptides via disulfide bonds. Erv1 is a sulfhydryl oxidase that oxidizes and activates Mia40, but it has remained unclear how Erv1 itself is oxidized. Here, we show that Erv1 passes its electrons on to molecular oxygen via interaction with cytochrome c and cytochrome c oxidase. This connection to the respiratory chain increases the efficient oxidation of the relay system in mitochondria and prevents the formation of toxic hydrogen peroxide. Thus, analogous to the system in the bacterial periplasm, the disulfide relay in the intermembrane space is connected to the electron transport chain of the inner membrane.
MeSH term(s)	Animals ; Cytochrome Reductases/metabolism ; Disulfides/metabolism ; Dose-Response Relationship, Drug ; Electron Transport ; Electron Transport Complex IV/metabolism ; Horses ; Humans ; Mitochondrial Membrane Transport Proteins/metabolism ; Mitochondrial Proteins/metabolism ; Models, Biological ; Oxidoreductases Acting on Sulfur Group Donors ; Oxygen/chemistry ; Oxygen/metabolism ; Reactive Oxygen Species ; Saccharomyces cerevisiae/metabolism ; Saccharomyces cerevisiae Proteins/metabolism
Chemical Substances	CHCHD4 protein, human ; Disulfides ; MIA40 protein, S cerevisiae ; Mitochondrial Membrane Transport Proteins ; Mitochondrial Proteins ; Reactive Oxygen Species ; Saccharomyces cerevisiae Proteins ; Cytochrome Reductases (EC 1.6.2.-) ; GFER protein, human (EC 1.8.-) ; Oxidoreductases Acting on Sulfur Group Donors (EC 1.8.-) ; ERV1 protein, S cerevisiae (EC 1.8.3.2) ; Electron Transport Complex IV (EC 1.9.3.1) ; Oxygen (S88TT14065)
Language	English
Publishing date	2007-10-29
Publishing country	United States
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	218154-x
ISSN	1540-8140 ; 0021-9525
ISSN (online)	1540-8140
ISSN	0021-9525
DOI	10.1083/jcb.200707123
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