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Article ; Online: Retreatment of symptomatic chronic bronchitis with bronchial rheoplasty.

Klemm, Theresa / Krimsky, William / Welz, Kelly / Valipour, Arschang

BMJ case reports

2024 Volume 17, Issue 2

Abstract: A man in his early 70s with a long-standing history of chronic bronchitis presented to our department 3 years ago with debilitating chronic cough and excessive sputum production. He had no previous diagnosis of chronic obstructive pulmonary disease and ... ...

Abstract	A man in his early 70s with a long-standing history of chronic bronchitis presented to our department 3 years ago with debilitating chronic cough and excessive sputum production. He had no previous diagnosis of chronic obstructive pulmonary disease and without evidence of severe respiratory tract infections. Due to his symptom burden and impairments in daily activities, the patient was considered to be an appropriate candidate for bronchial rheoplasty, a novel endoscopic treatment for patients with chronic bronchitis. The patient responded well to bilateral treatment but then experienced symptom recurrence roughly 14 months after completing the initial treatment. In the absence of an alternative explanation for the return of these symptoms, he then underwent uneventful retreatment. The patient, again, reported significant symptom improvement and no adverse effects since retreatment. While further studies are necessary to assess the safety and efficacy of retreatment, the findings from this case are encouraging.
MeSH term(s)	Male ; Humans ; Bronchitis, Chronic/drug therapy ; Bronchitis, Chronic/surgery ; Pulmonary Disease, Chronic Obstructive ; Bronchi ; Retreatment ; Chronic Disease ; Bronchitis/complications ; Bronchitis/drug therapy ; Bronchitis/diagnosis
Language	English
Publishing date	2024-02-17
Publishing country	England
Document type	Case Reports ; Journal Article
ISSN	1757-790X
ISSN (online)	1757-790X
DOI	10.1136/bcr-2023-256764
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Article ; Online: Characterisation of the OTU domain deubiquitinase complement of

Wilde, Mary-Louise / Ruparel, Ushma / Klemm, Theresa / Lee, V Vern / Calleja, Dale J / Komander, David / Tonkin, Christopher J

Life science alliance

2023 Volume 6, Issue 6

Abstract: The phylum Apicomplexa contains several parasitic species of medical and agricultural importance. The ubiquitination machinery remains, for the most part, uncharacterised in apicomplexan parasites, despite the important roles that it plays in eukaryotic ... ...

Abstract	The phylum Apicomplexa contains several parasitic species of medical and agricultural importance. The ubiquitination machinery remains, for the most part, uncharacterised in apicomplexan parasites, despite the important roles that it plays in eukaryotic biology. Bioinformatic analysis of the ubiquitination machinery in apicomplexan parasites revealed an expanded ovarian tumour domain-containing (OTU) deubiquitinase (DUB) family in
MeSH term(s)	Toxoplasma/genetics ; Toxoplasma/metabolism ; Ubiquitin/genetics ; Ubiquitin/metabolism ; Ubiquitination ; Plasmodium ; Deubiquitinating Enzymes/genetics ; Deubiquitinating Enzymes/metabolism
Chemical Substances	Ubiquitin ; Deubiquitinating Enzymes (EC 3.4.19.12)
Language	English
Publishing date	2023-03-23
Publishing country	United States
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ISSN	2575-1077
ISSN (online)	2575-1077
DOI	10.26508/lsa.202201710
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Conference proceedings: Is student mentoring career-defining in surgical disciplines? A comparative survey among medical schools and medical students for mentoring programs

Hertling, Stefan Ferdinand / Loos, Franziska / Back, David / Klemm, Theresa / Wildemann, Britt / Graul, Isabel

2021 , Page(s) AB66–1385

Event/congress	Deutscher Kongress für Orthopädie und Unfallchirurgie (DKOU 2021); Berlin; ; Berufsverband für Orthopädie und Unfallchirurgie; 2021
Keywords	Medizin, Gesundheit ; mentoring ; medical students ; gender ; career ; surgery
Publishing date	2021-10-26
Publisher	German Medical Science GMS Publishing House; Düsseldorf
Document type	Conference proceedings
DOI	10.3205/21dkou409
Database	German Medical Science

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Article: Differential Oligomerization of the Deubiquitinases USP25 and USP28 Regulates Their Activities

Sauer, Florian / Kisker, Caroline / Klemm, Theresa / Kollampally, Ravi B / Nair, Radhika K / Popov, Nikita / Tessmer, Ingrid

Molecular cell. 2019 May 02, v. 74, no. 3

2019

Abstract: Deubiquitinases have emerged as promising drug targets for cancer therapy. The two DUBs USP25 and USP28 share high similarity but vary in their cellular functions. USP28 is known for its tumor-promoting role, whereas USP25 is a regulator of the innate ... ...

Abstract	Deubiquitinases have emerged as promising drug targets for cancer therapy. The two DUBs USP25 and USP28 share high similarity but vary in their cellular functions. USP28 is known for its tumor-promoting role, whereas USP25 is a regulator of the innate immune system and, recently, a role in tumorigenesis was proposed. We solved the structures of the catalytic domains of both proteins and established substantial differences in their activities. While USP28 is a constitutively active dimer, USP25 presents an auto-inhibited tetramer. Our data indicate that the activation of USP25 is not achieved through substrate or ubiquitin binding. USP25 cancer-associated mutations lead to activation in vitro and in vivo, thereby providing a functional link between auto-inhibition and the cancer-promoting role of the enzyme. Our work led to the identification of significant differences between USP25 and USP28 and provided the molecular basis for the development of new and highly specific anti-cancer drugs.
Keywords	active sites ; antineoplastic agents ; carcinogenesis ; innate immunity ; mutation ; neoplasms ; oligomerization ; therapeutics ; ubiquitin ; ubiquitinyl hydrolase 1
Language	English
Dates of publication	2019-0502
Size	p. 421-435.e10.
Publishing place	Elsevier Inc.
Document type	Article
ZDB-ID	1415236-8
ISSN	1097-4164 ; 1097-2765
ISSN (online)	1097-4164
ISSN	1097-2765
DOI	10.1016/j.molcel.2019.02.029
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Book ; Online ; Thesis: Minor differences cause major effects: How differential oligomerization regulates the activities of USP25 and USP28

Klemm, Theresa Antonia [Verfasser] / Kisker, Caroline [Gutachter] / Buchberger, Alexander [Gutachter] / Popov, Nikita [Gutachter]

2020

Author's details	Theresa Antonia Klemm ; Gutachter: Caroline Kisker, Alexander Buchberger, Nikita Popov
Keywords	Biowissenschaften, Biologie ; Life Science, Biology
Subject code	sg570
Language	English
Publisher	Universität Würzburg
Publishing place	Würzburg
Document type	Book ; Online ; Thesis
Database	Digital theses on the web

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Article ; Online: Differential Oligomerization of the Deubiquitinases USP25 and USP28 Regulates Their Activities.

Sauer, Florian / Klemm, Theresa / Kollampally, Ravi B / Tessmer, Ingrid / Nair, Radhika K / Popov, Nikita / Kisker, Caroline

Molecular cell

2019 Volume 74, Issue 3, Page(s) 421–435.e10

Abstract	Deubiquitinases have emerged as promising drug targets for cancer therapy. The two DUBs USP25 and USP28 share high similarity but vary in their cellular functions. USP28 is known for its tumor-promoting role, whereas USP25 is a regulator of the innate immune system and, recently, a role in tumorigenesis was proposed. We solved the structures of the catalytic domains of both proteins and established substantial differences in their activities. While USP28 is a constitutively active dimer, USP25 presents an auto-inhibited tetramer. Our data indicate that the activation of USP25 is not achieved through substrate or ubiquitin binding. USP25 cancer-associated mutations lead to activation in vitro and in vivo, thereby providing a functional link between auto-inhibition and the cancer-promoting role of the enzyme. Our work led to the identification of significant differences between USP25 and USP28 and provided the molecular basis for the development of new and highly specific anti-cancer drugs.
MeSH term(s)	Amino Acid Sequence/genetics ; Carcinogenesis/genetics ; Catalytic Domain/genetics ; Deubiquitinating Enzymes/chemistry ; Deubiquitinating Enzymes/genetics ; Humans ; Mutation/genetics ; Neoplasms/drug therapy ; Neoplasms/genetics ; Protein Binding/genetics ; Protein Conformation ; Protein Multimerization/genetics ; Ubiquitin/genetics ; Ubiquitin Thiolesterase/chemistry ; Ubiquitin Thiolesterase/genetics
Chemical Substances	USP25 protein, human ; USP28 protein, human ; Ubiquitin ; Deubiquitinating Enzymes (EC 3.4.19.12) ; Ubiquitin Thiolesterase (EC 3.4.19.12)
Language	English
Publishing date	2019-03-26
Publishing country	United States
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	1415236-8
ISSN	1097-4164 ; 1097-2765
ISSN (online)	1097-4164
ISSN	1097-2765
DOI	10.1016/j.molcel.2019.02.029
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Article ; Online: Structural Basis of Substrate Recognition and Covalent Inhibition of Cdu1 from Chlamydia trachomatis.

Ramirez, Yesid A / Adler, Thomas B / Altmann, Eva / Klemm, Theresa / Tiesmeyer, Christian / Sauer, Florian / Kathman, Stefan G / Statsyuk, Alexander V / Sotriffer, Christoph / Kisker, Caroline

ChemMedChem

2018 Volume 13, Issue 19, Page(s) 2014–2023

Abstract: Based on the similarity between the active sites of the deubiquitylating and deneddylating enzyme ChlaDub1 (Cdu1) and the evolutionarily related protease adenain, a target-hopping screening approach on a focused set of adenain inhibitors was investigated. ...

Abstract	Based on the similarity between the active sites of the deubiquitylating and deneddylating enzyme ChlaDub1 (Cdu1) and the evolutionarily related protease adenain, a target-hopping screening approach on a focused set of adenain inhibitors was investigated. The cyanopyrimidine-based inhibitors identified represent the first active-site-directed small-molecule inhibitors of Cdu1. High-resolution crystal structures of Cdu1 in complex with two covalently bound cyanopyrimidines, as well as with its substrate ubiquitin, were obtained. These structural data were complemented by enzymatic assays and covalent docking studies to provide insight into the substrate recognition of Cdu1, active-site pocket flexibility and potential hotspots for ligand interaction. Combined, these data provide a strong basis for future structure-guided medicinal chemistry optimization of this cyanopyrimidine scaffold into more potent and selective Cdu1 inhibitors.
MeSH term(s)	Amino Acid Sequence ; Catalytic Domain ; Chlamydia trachomatis/chemistry ; Chlamydia trachomatis/enzymology ; Cysteine Endopeptidases/chemistry ; Deubiquitinating Enzymes/antagonists & inhibitors ; Deubiquitinating Enzymes/chemistry ; Enzyme Inhibitors/chemistry ; Fungal Proteins/antagonists & inhibitors ; Fungal Proteins/chemistry ; Humans ; Molecular Docking Simulation ; Oligopeptides/chemistry ; Pyrimidines/chemistry ; Saccharomyces cerevisiae/enzymology ; Sequence Alignment ; Substrate Specificity
Chemical Substances	Enzyme Inhibitors ; Fungal Proteins ; Oligopeptides ; Pyrimidines ; Deubiquitinating Enzymes (EC 3.4.19.12) ; Cysteine Endopeptidases (EC 3.4.22.-) ; adenain (EC 3.4.22.39)
Language	English
Publishing date	2018-09-06
Publishing country	Germany
Document type	Journal Article ; Research Support, N.I.H., Extramural ; Research Support, Non-U.S. Gov't
ZDB-ID	2218496-X
ISSN	1860-7187 ; 1860-7179
ISSN (online)	1860-7187
ISSN	1860-7179
DOI	10.1002/cmdc.201800364
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Article: Insights Into Drug Repurposing, as Well as Specificity and Compound Properties of Piperidine-Based SARS-CoV-2 PLpro Inhibitors.

Calleja, Dale J / Kuchel, Nathan / Lu, Bernadine G C / Birkinshaw, Richard W / Klemm, Theresa / Doerflinger, Marcel / Cooney, James P / Mackiewicz, Liana / Au, Amanda E / Yap, Yu Q / Blackmore, Timothy R / Katneni, Kasiram / Crighton, Elly / Newman, Janet / Jarman, Kate E / Call, Melissa J / Lechtenberg, Bernhard C / Czabotar, Peter E / Pellegrini, Marc /

Charman, Susan A / Lowes, Kym N / Mitchell, Jeffrey P / Nachbur, Ueli / Lessene, Guillaume / Komander, David

Frontiers in chemistry

2022 Volume 10, Page(s) 861209

Abstract: The COVID-19 pandemic continues unabated, emphasizing the need for additional antiviral treatment options to prevent hospitalization and death of patients infected with SARS-CoV-2. The papain-like protease (PLpro) domain is part of the SARS-CoV-2 non- ... ...

Abstract	The COVID-19 pandemic continues unabated, emphasizing the need for additional antiviral treatment options to prevent hospitalization and death of patients infected with SARS-CoV-2. The papain-like protease (PLpro) domain is part of the SARS-CoV-2 non-structural protein (nsp)-3, and represents an essential protease and validated drug target for preventing viral replication. PLpro moonlights as a deubiquitinating (DUB) and deISGylating enzyme, enabling adaptation of a DUB high throughput (HTS) screen to identify PLpro inhibitors. Drug repurposing has been a major focus through the COVID-19 pandemic as it may provide a fast and efficient route for identifying clinic-ready, safe-in-human antivirals. We here report our effort to identify PLpro inhibitors by screening the ReFRAME library of 11,804 compounds, showing that none inhibit PLpro with any reasonable activity or specificity to justify further progression towards the clinic. We also report our latest efforts to improve piperidine-scaffold inhibitors,
Language	English
Publishing date	2022-04-12
Publishing country	Switzerland
Document type	Journal Article
ZDB-ID	2711776-5
ISSN	2296-2646
ISSN	2296-2646
DOI	10.3389/fchem.2022.861209
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Article ; Online: Global antibody response to Staphylococcus aureus live-cell vaccination.

Selle, Martina / Hertlein, Tobias / Oesterreich, Babett / Klemm, Theresa / Kloppot, Peggy / Müller, Elke / Ehricht, Ralf / Stentzel, Sebastian / Bröker, Barbara M / Engelmann, Susanne / Ohlsen, Knut

Scientific reports

2016 Volume 6, Page(s) 24754

Abstract: The pathogen Staphylococcus aureus causes a broad range of severe diseases and is feared for its ability to rapidly develop resistance to antibiotic substances. The increasing number of highly resistant S. aureus infections has accelerated the search for ...

Abstract	The pathogen Staphylococcus aureus causes a broad range of severe diseases and is feared for its ability to rapidly develop resistance to antibiotic substances. The increasing number of highly resistant S. aureus infections has accelerated the search for alternative treatment options to close the widening gap in anti-S. aureus therapy. This study analyses the humoral immune response to vaccination of Balb/c mice with sublethal doses of live S. aureus. The elicited antibody pattern in the sera of intravenously and intramuscularly vaccinated mice was determined using of a recently developed protein array. We observed a specific antibody response against a broad set of S. aureus antigens which was stronger following i.v. than i.m. vaccination. Intravenous but not intramuscular vaccination protected mice against an intramuscular challenge infection with a high bacterial dose. Vaccine protection was correlated with the strength of the anti-S. aureus antibody response. This study identified novel vaccine candidates by using protein microarrays as an effective tool and showed that successful vaccination against S. aureus relies on the optimal route of administration.
Language	English
Publishing date	2016--22
Publishing country	England
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	2615211-3
ISSN	2045-2322 ; 2045-2322
ISSN (online)	2045-2322
ISSN	2045-2322
DOI	10.1038/srep24754
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Article ; Online: Mechanism and inhibition of the papain-like protease, PLpro, of SARS-CoV-2.

Klemm, Theresa / Ebert, Gregor / Calleja, Dale J / Allison, Cody C / Richardson, Lachlan W / Bernardini, Jonathan P / Lu, Bernadine Gc / Kuchel, Nathan W / Grohmann, Christoph / Shibata, Yuri / Gan, Zhong Yan / Cooney, James P / Doerflinger, Marcel / Au, Amanda E / Blackmore, Timothy R / van der Heden van Noort, Gerbrand J / Geurink, Paul P / Ovaa, Huib / Newman, Janet /

Riboldi-Tunnicliffe, Alan / Czabotar, Peter E / Mitchell, Jeffrey P / Feltham, Rebecca / Lechtenberg, Bernhard C / Lowes, Kym N / Dewson, Grant / Pellegrini, Marc / Lessene, Guillaume / Komander, David

The EMBO journal

2020 Volume 39, Issue 18, Page(s) e106275

Abstract: The SARS-CoV-2 coronavirus encodes an essential papain-like protease domain as part of its non-structural protein (nsp)-3, namely SARS2 PLpro, that cleaves the viral polyprotein, but also removes ubiquitin-like ISG15 protein modifications as well as, ... ...

Abstract	The SARS-CoV-2 coronavirus encodes an essential papain-like protease domain as part of its non-structural protein (nsp)-3, namely SARS2 PLpro, that cleaves the viral polyprotein, but also removes ubiquitin-like ISG15 protein modifications as well as, with lower activity, Lys48-linked polyubiquitin. Structures of PLpro bound to ubiquitin and ISG15 reveal that the S1 ubiquitin-binding site is responsible for high ISG15 activity, while the S2 binding site provides Lys48 chain specificity and cleavage efficiency. To identify PLpro inhibitors in a repurposing approach, screening of 3,727 unique approved drugs and clinical compounds against SARS2 PLpro identified no compounds that inhibited PLpro consistently or that could be validated in counterscreens. More promisingly, non-covalent small molecule SARS PLpro inhibitors also target SARS2 PLpro, prevent self-processing of nsp3 in cells and display high potency and excellent antiviral activity in a SARS-CoV-2 infection model.
MeSH term(s)	Animals ; Antiviral Agents/pharmacology ; Binding Sites ; Chlorocebus aethiops ; Coronavirus 3C Proteases/antagonists & inhibitors ; Coronavirus 3C Proteases/chemistry ; Coronavirus 3C Proteases/genetics ; Coronavirus 3C Proteases/metabolism ; Crystallography, X-Ray ; Cytokines/genetics ; Drug Evaluation, Preclinical/methods ; Drug Repositioning ; Fluorescence Polarization ; HEK293 Cells ; Humans ; Kinetics ; Models, Molecular ; Protease Inhibitors/pharmacology ; Protein Conformation ; SARS-CoV-2/chemistry ; SARS-CoV-2/genetics ; SARS-CoV-2/metabolism ; Ubiquitin/metabolism ; Ubiquitins/genetics ; Vero Cells
Chemical Substances	Antiviral Agents ; Cytokines ; Protease Inhibitors ; Ubiquitin ; Ubiquitins ; ISG15 protein, human (60267-61-0) ; 3C-like proteinase, SARS-CoV-2 (EC 3.4.22.-) ; Coronavirus 3C Proteases (EC 3.4.22.28)
Keywords	covid19
Language	English
Publishing date	2020-08-26
Publishing country	England
Document type	Journal Article
ZDB-ID	586044-1
ISSN	1460-2075 ; 0261-4189
ISSN (online)	1460-2075
ISSN	0261-4189
DOI	10.15252/embj.2020106275
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