LIVIVO - Search results -

Search results

Result 1 - 10 of total 20

Search options

Article ; Online: Disruption of mitochondrial quality control genes promotes caspase-resistant cell survival following apoptotic stimuli.

Kushnareva, Yulia / Moraes, Vivian / Suess, Julian / Peters, Bjoern / Newmeyer, Donald D / Kuwana, Tomomi

2022 Volume 298, Issue 4, Page(s) 101835

Abstract: In cells undergoing cell-intrinsic apoptosis, mitochondrial outer membrane permeabilization (MOMP) typically marks an irreversible step in the cell death process. However, in some cases, a subpopulation of treated cells can exhibit a sublethal response, ... ...

Abstract	In cells undergoing cell-intrinsic apoptosis, mitochondrial outer membrane permeabilization (MOMP) typically marks an irreversible step in the cell death process. However, in some cases, a subpopulation of treated cells can exhibit a sublethal response, termed "minority MOMP." In this phenomenon, the affected cells survive, despite a low level of caspase activation and subsequent limited activation of the endonuclease caspase-activated DNase (DNA fragmentation factor subunit beta). Consequently, these cells can experience DNA damage, increasing the probability of oncogenesis. However, little is known about the minority MOMP response. To discover genes that affect the MOMP response in individual cells, we conducted an imaging-based phenotypic siRNA screen. We identified multiple candidate genes whose downregulation increased the heterogeneity of MOMP within single cells, among which were genes related to mitochondrial dynamics and mitophagy that participate in the mitochondrial quality control (MQC) system. Furthermore, to test the hypothesis that functional MQC is important for reducing the frequency of minority MOMP, we developed an assay to measure the clonogenic survival of caspase-engaged cells. We found that cells deficient in various MQC genes were indeed prone to aberrant post-MOMP survival. Our data highlight the important role of proteins involved in mitochondrial dynamics and mitophagy in preventing apoptotic dysregulation and oncogenesis.
MeSH term(s)	Apoptosis/physiology ; Carcinogenesis/genetics ; Carcinogenesis/metabolism ; Caspases/metabolism ; Cell Survival/genetics ; Humans ; Mitochondria/genetics ; Mitochondria/metabolism ; Mitochondrial Membranes/metabolism
Chemical Substances	Caspases (EC 3.4.22.-)
Language	English
Publishing date	2022-03-16
Publishing country	United States
Document type	Journal Article
ZDB-ID	2997-x
ISSN	1083-351X ; 0021-9258
ISSN (online)	1083-351X
ISSN	0021-9258
DOI	10.1016/j.jbc.2022.101835
Database	MEDical Literature Analysis and Retrieval System OnLINE

In stock of ZB MED Cologne/Königswinter

Uc I Zs.108: Show issues

Location:
Je nach Verfügbarkeit (siehe Angabe bei Bestand)
bis Jg. 2021: Bestellungen von Artikeln über das Online-Bestellformular
ab Jg. 2022: Lesesaal (EG)

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.

Details ▾
- See ZB MED holdings
- Order with fees

Article ; Online: HIV-1 Fusion with CD4+ T cells Is Promoted by Proteins Involved in Endocytosis and Intracellular Membrane Trafficking.

Marin, Mariana / Kushnareva, Yulia / Mason, Caleb S / Chanda, Sumit K / Melikyan, Gregory B

Viruses

2019 Volume 11, Issue 2

Abstract: The HIV-1 entry pathway into permissive cells has been a subject of debate. Accumulating evidence, including our previous single virus tracking results, suggests that HIV-1 can enter different cell types via endocytosis and CD4/coreceptor-dependent ... ...

Abstract	The HIV-1 entry pathway into permissive cells has been a subject of debate. Accumulating evidence, including our previous single virus tracking results, suggests that HIV-1 can enter different cell types via endocytosis and CD4/coreceptor-dependent fusion with endosomes. However, recent studies that employed indirect techniques to infer the sites of HIV-1 entry into CD4+ T cells have concluded that endocytosis does not contribute to infection. To assess whether HIV-1 enters these cells via endocytosis, we probed the role of intracellular trafficking in HIV-1 entry/fusion by a targeted shRNA screen in a CD4+ T cell line. We performed a screen utilizing a direct virus-cell fusion assay as readout and identified several host proteins involved in endosomal trafficking/maturation, including Rab5A and sorting nexins, as factors regulating HIV-1 fusion and infection. Knockdown of these proteins inhibited HIV-1 fusion irrespective of coreceptor tropism, without altering the CD4 or coreceptor expression, or compromising the virus' ability to mediate fusion of two adjacent cells initiated by virus-plasma membrane fusion. Ectopic expression of Rab5A in non-permissive cells harboring Rab5A shRNAs partially restored the HIV-cell fusion. Together, these results implicate endocytic machinery in productive HIV-1 entry into CD4+ T cells.
MeSH term(s)	CD4-Positive T-Lymphocytes/virology ; Cell Line ; Endocytosis ; HIV-1/physiology ; Humans ; Intracellular Membranes/virology ; RNA, Small Interfering/genetics ; Sorting Nexins/genetics ; Virus Internalization ; Virus Replication ; rab5 GTP-Binding Proteins/genetics
Chemical Substances	RNA, Small Interfering ; Sorting Nexins ; RAB5C protein, human (EC 3.6.1.-) ; rab5 GTP-Binding Proteins (EC 3.6.5.2)
Language	English
Publishing date	2019-01-25
Publishing country	Switzerland
Document type	Journal Article ; Research Support, N.I.H., Extramural ; Research Support, Non-U.S. Gov't
ZDB-ID	2516098-9
ISSN	1999-4915 ; 1999-4915
ISSN (online)	1999-4915
ISSN	1999-4915
DOI	10.3390/v11020100
Database	MEDical Literature Analysis and Retrieval System OnLINE

Order via subito

Article ; Online: Functional Analysis of Immune Signature Genes in Th1* Memory Cells Links ISOC1 and Pyrimidine Metabolism to IFN-γ and IL-17 Production.

Kushnareva, Yulia / Mathews, Ian T / Andreyev, Alexander Y / Altay, Gokmen / Lindestam Arlehamn, Cecilia S / Pandurangan, Vijayanand / Nilsson, Roland / Jain, Mohit / Sette, Alessandro / Peters, Bjoern / Sharma, Sonia

Journal of immunology (Baltimore, Md. : 1950)

2021 Volume 206, Issue 6, Page(s) 1181–1193

Abstract: ... ...

Abstract	CCR6
MeSH term(s)	Gene Expression Regulation/immunology ; Gene Knockdown Techniques ; HEK293 Cells ; Healthy Volunteers ; Humans ; Hydrolases/genetics ; Hydrolases/metabolism ; Immunologic Memory/genetics ; Interferon-gamma/genetics ; Interleukin-17/genetics ; Primary Cell Culture ; Pyrimidines/metabolism ; RNA, Small Interfering/metabolism ; Signal Transduction/genetics ; Signal Transduction/immunology ; Th1 Cells/immunology ; Th1 Cells/metabolism
Chemical Substances	IFNG protein, human ; Interleukin-17 ; Pyrimidines ; RNA, Small Interfering ; Interferon-gamma (82115-62-6) ; Hydrolases (EC 3.-) ; ISOC1 protein, human (EC 3.-)
Language	English
Publishing date	2021-02-05
Publishing country	United States
Document type	Journal Article ; Research Support, N.I.H., Extramural ; Research Support, Non-U.S. Gov't
ZDB-ID	3056-9
ISSN	1550-6606 ; 0022-1767 ; 1048-3233 ; 1047-7381
ISSN (online)	1550-6606
ISSN	0022-1767 ; 1048-3233 ; 1047-7381
DOI	10.4049/jimmunol.2000672
Database	MEDical Literature Analysis and Retrieval System OnLINE

In stock of ZB MED Cologne/Königswinter

Ud II Zs.37: Show issues			Location: Je nach Verfügbarkeit (siehe Angabe bei Bestand) bis Jg. 2021: Bestellungen von Artikeln über das Online-Bestellformular ab Jg. 2022: Lesesaal (EG)
Zs.MG 28: Show issues

Order via subito

Details ▾
- See ZB MED holdings
- Order with fees

Article ; Online: Olgotrelvir, a dual inhibitor of SARS-CoV-2 M

Mao, Long / Shaabani, Namir / Zhang, Xiaoying / Jin, Can / Xu, Wanhong / Argent, Christopher / Kushnareva, Yulia / Powers, Colin / Stegman, Karen / Liu, Jia / Xie, Hui / Xu, Changxu / Bao, Yimei / Xu, Lijun / Zhang, Yuren / Yang, Haigang / Qian, Shengdian / Hu, Yong / Shao, Jianping /

Zhang, Can / Li, Tingting / Li, Yi / Liu, Na / Lin, Zhenhao / Wang, Shanbo / Wang, Chao / Shen, Wei / Lin, Yuanlong / Shu, Dan / Zhu, Zhenhong / Kotoi, Olivia / Kerwin, Lisa / Han, Qing / Chumakova, Ludmila / Teijaro, John / Royal, Mike / Brunswick, Mark / Allen, Robert / Ji, Henry / Lu, Hongzhou / Xu, Xiao

Med (New York, N.Y.)

2024 Volume 5, Issue 2, Page(s) 169–171

Language	English
Publishing date	2024-02-02
Publishing country	United States
Document type	Published Erratum
ISSN	2666-6340
ISSN (online)	2666-6340
DOI	10.1016/j.medj.2024.01.013
Database	MEDical Literature Analysis and Retrieval System OnLINE

Order via subito

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.

Article ; Online: Role and significance of asprosin in feeding behaviour and metabolism

Rustam H. Salimkhanov / Vladislav R. Sharifullin / Yulia R. Kushnareva / Azamat Kh. Kade / Pavel P. Polyakov

Кубанский научный медицинский вестник, Vol 27, Iss 1, Pp 96-

2020 Volume 104

Abstract: This article presents a review of available information on asprosin — a hormone of white adipose tissue discovered in 2016. The history of its discovery, as well as its action mechanisms and main targets are examined. Changes in the plasma level of ... ...

Abstract	This article presents a review of available information on asprosin — a hormone of white adipose tissue discovered in 2016. The history of its discovery, as well as its action mechanisms and main targets are examined. Changes in the plasma level of asprosin under some pathological conditions are analysed. The importance of studying asprosin is determined by its functions: asprosin regulates physiological processes during fasting and plays an important role in the development of metabolic disorders, such as insulin resistance. There are relatively few studies concerned with asprosin; however, this hormone can already be considered as a diagnostic marker and a potential target in the treatment of certain metabolic disorders, e.g. diabetes mellitus and obesity.
Keywords	fbn1 ; marfanoid-progeroid-lipodystrophy syndrome ; white adipose tissue ; insulin resistance ; Medicine ; R
Language	Russian
Publishing date	2020-02-01T00:00:00Z
Publisher	Ministry of Healthcare of the Russian Federation. “Kuban State Medical University”
Document type	Article ; Online
Database	BASE - Bielefeld Academic Search Engine (life sciences selection)

Full text online

Full text

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.

Article ; Online: Bioenergetics and cell death.

Kushnareva, Yulia / Newmeyer, Donald D

Annals of the New York Academy of Sciences

2010 Volume 1201, Page(s) 50–57

Abstract: Mitochondrial bioenergetic function is a key to cell life and death. Cells need energy not only to support their vital functions but also to die gracefully. Execution of an apoptotic program includes energy-dependent steps, including kinase signaling, ... ...

Abstract	Mitochondrial bioenergetic function is a key to cell life and death. Cells need energy not only to support their vital functions but also to die gracefully. Execution of an apoptotic program includes energy-dependent steps, including kinase signaling, formation of the apoptosome, and effector caspase activation. Under conditions of bioenergetic collapse, cells are diverted toward necrotic demise. Mitochondrial outer membrane permeabilization (MOMP) is a decisive event in the execution of apoptosis. It is also causally linked to a decline in bioenergetic function via different mechanisms, not merely due to cytochrome c dispersion. MOMP-induced bioenergetic deficiency is usually irreversible and commits cells to die, even when caspases are inactive. Here, we discuss the mechanisms by which MOMP impacts bioenergetics in different cell death paradigms.
MeSH term(s)	Apoptosis ; Caspases/metabolism ; Cell Death/physiology ; Cell Survival ; Cytochromes c/metabolism ; Energy Metabolism ; Enzyme Activation ; HeLa Cells ; Humans ; Mitochondria/metabolism ; Mitochondrial Membranes/metabolism ; NAD/metabolism ; Necrosis ; Oxygen/chemistry ; bcl-2-Associated X Protein/metabolism
Chemical Substances	bcl-2-Associated X Protein ; NAD (0U46U6E8UK) ; Cytochromes c (9007-43-6) ; Caspases (EC 3.4.22.-) ; Oxygen (S88TT14065)
Language	English
Publishing date	2010-10-25
Publishing country	United States
Document type	Journal Article ; Research Support, N.I.H., Extramural ; Review
ZDB-ID	211003-9
ISSN	1749-6632 ; 0077-8923
ISSN (online)	1749-6632
ISSN	0077-8923
DOI	10.1111/j.1749-6632.2010.05633.x
Database	MEDical Literature Analysis and Retrieval System OnLINE

Full text online

Accessible to users with ZB MED library card

In stock of ZB MED Cologne/Königswinter

Se 110: Show issues

Location:
Je nach Verfügbarkeit (siehe Angabe bei Bestand)
bis Jg. 2021: Bestellungen von Artikeln über das Online-Bestellformular
ab Jg. 2022: Lesesaal (EG)

Order via subito

Details ▾

Article ; Online: Olgotrelvir, a dual inhibitor of SARS-CoV-2 M

Med (New York, N.Y.)

2024 Volume 5, Issue 1, Page(s) 42–61.e23

Abstract: Background: Oral antiviral drugs with improved antiviral potency and safety are needed to address current challenges in clinical practice for treatment of COVID-19, including the risks of rebound, drug-drug interactions, and emerging resistance.: ... ...

Abstract	Background: Oral antiviral drugs with improved antiviral potency and safety are needed to address current challenges in clinical practice for treatment of COVID-19, including the risks of rebound, drug-drug interactions, and emerging resistance. Methods: Olgotrelvir (STI-1558) is designed as a next-generation antiviral targeting the SARS-CoV-2 main protease (M Findings: Olgotrelvir is a highly bioavailable oral prodrug that is converted in plasma to its active form, AC1115. The dual mechanism of action of olgotrelvir and AC1115 was confirmed by enzyme activity inhibition assays and co-crystal structures of AC1115 with SARS-CoV-2 M Conclusions: Olgotrelvir is an oral inhibitor targeting M Funding: Funded by Sorrento Therapeutics.
MeSH term(s)	Animals ; Humans ; Mice ; Antiviral Agents/pharmacology ; Antiviral Agents/therapeutic use ; Cathepsin L/antagonists & inhibitors ; COVID-19/prevention & control ; Disease Models, Animal ; Mice, Transgenic ; SARS-CoV-2 ; Coronavirus Protease Inhibitors/chemistry ; Coronavirus Protease Inhibitors/pharmacology ; Coronavirus 3C Proteases/antagonists & inhibitors ; COVID-19 Drug Treatment/methods
Chemical Substances	Antiviral Agents ; Cathepsin L (EC 3.4.22.15) ; STI-1558 ; Coronavirus Protease Inhibitors ; Coronavirus 3C Proteases (EC 3.4.22.28)
Language	English
Publishing date	2024-01-04
Publishing country	United States
Document type	Journal Article
ISSN	2666-6340
ISSN (online)	2666-6340
DOI	10.1016/j.medj.2023.12.004
Database	MEDical Literature Analysis and Retrieval System OnLINE

Order via subito

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.

Article ; Online: Bax activation initiates the assembly of a multimeric catalyst that facilitates Bax pore formation in mitochondrial outer membranes.

Kushnareva, Yulia / Andreyev, Alexander Y / Kuwana, Tomomi / Newmeyer, Donald D

PLoS biology

2012 Volume 10, Issue 9, Page(s) e1001394

Abstract: Bax/Bak-mediated mitochondrial outer membrane permeabilization (MOMP) is essential for "intrinsic" apoptotic cell death. Published studies used synthetic liposomes to reveal an intrinsic pore-forming activity of Bax, but it is unclear how other ... ...

Abstract	Bax/Bak-mediated mitochondrial outer membrane permeabilization (MOMP) is essential for "intrinsic" apoptotic cell death. Published studies used synthetic liposomes to reveal an intrinsic pore-forming activity of Bax, but it is unclear how other mitochondrial outer membrane (MOM) proteins might facilitate this function. We carefully analyzed the kinetics of Bax-mediated pore formation in isolated MOMs, with some unexpected results. Native MOMs were more sensitive than liposomes to added Bax, and MOMs displayed a lag phase not observed with liposomes. Heat-labile MOM proteins were required for this enhanced response. A two-tiered mathematical model closely fit the kinetic data: first, Bax activation promotes the assembly of a multimeric complex, which then catalyzes the second reaction, Bax-dependent pore formation. Bax insertion occurred immediately upon Bax addition, prior to the end of the lag phase. Permeabilization kinetics were affected in a reciprocal manner by [cBid] and [Bax], confirming the "hit-and-run" hypothesis of cBid-induced direct Bax activation. Surprisingly, MOMP rate constants were linearly related to [Bax], implying that Bax acts non-cooperatively. Thus, the oligomeric catalyst is distinct from Bax. Moreover, contrary to common assumption, pore formation kinetics depend on Bax monomers, not oligomers. Catalyst formation exhibited a sharp transition in activation energy at ∼28°C, suggesting a role for membrane lipid packing. Furthermore, catalyst formation was strongly inhibited by chemical antagonists of the yeast mitochondrial fission protein, Dnm1. However, the mammalian ortholog, Drp1, was undetectable in mitochondrial outer membranes. Moreover, ATP and GTP were dispensable for MOMP. Thus, the data argue that oligomerization of a catalyst protein, distinct from Bax and Drp1, facilitates MOMP, possibly through a membrane-remodeling event.
MeSH term(s)	Animals ; BH3 Interacting Domain Death Agonist Protein/metabolism ; Biocatalysis/drug effects ; Dynamin I/metabolism ; Humans ; Kinetics ; Liposomes/metabolism ; Male ; Mitochondria, Liver/drug effects ; Mitochondria, Liver/metabolism ; Mitochondrial Membrane Transport Proteins/metabolism ; Mitochondrial Membranes/metabolism ; Mitochondrial Permeability Transition Pore ; Models, Biological ; Permeability/drug effects ; Protein Multimerization/drug effects ; Quinazolinones/pharmacology ; Rats ; Rats, Sprague-Dawley ; Thermodynamics ; bcl-2-Associated X Protein/metabolism
Chemical Substances	3-(2,4-dichloro-5-methoxyphenyl)-2-sulfanyl-4(3H)-quinazolinone ; BH3 Interacting Domain Death Agonist Protein ; Liposomes ; Mitochondrial Membrane Transport Proteins ; Mitochondrial Permeability Transition Pore ; Quinazolinones ; bcl-2-Associated X Protein ; Dynamin I (EC 3.5.1.50)
Language	English
Publishing date	2012-09-25
Publishing country	United States
Document type	Journal Article ; Research Support, N.I.H., Extramural
ZDB-ID	2126776-5
ISSN	1545-7885 ; 1544-9173
ISSN (online)	1545-7885
ISSN	1544-9173
DOI	10.1371/journal.pbio.1001394
Database	MEDical Literature Analysis and Retrieval System OnLINE

In stock of ZB MED Cologne/Königswinter

Zs.A 6193: Show issues

Location:
Je nach Verfügbarkeit (siehe Angabe bei Bestand)
bis Jg. 2021: Bestellungen von Artikeln über das Online-Bestellformular
ab Jg. 2022: Lesesaal (EG)

Order via subito

Details ▾
- See ZB MED holdings
- Order with fees

Article ; Online: Bax activation initiates the assembly of a multimeric catalyst that facilitates Bax pore formation in mitochondrial outer membranes.

Yulia Kushnareva / Alexander Y Andreyev / Tomomi Kuwana / Donald D Newmeyer

PLoS Biology, Vol 10, Iss 9, p e

2012 Volume 1001394

Abstract	Bax/Bak-mediated mitochondrial outer membrane permeabilization (MOMP) is essential for "intrinsic" apoptotic cell death. Published studies used synthetic liposomes to reveal an intrinsic pore-forming activity of Bax, but it is unclear how other mitochondrial outer membrane (MOM) proteins might facilitate this function. We carefully analyzed the kinetics of Bax-mediated pore formation in isolated MOMs, with some unexpected results. Native MOMs were more sensitive than liposomes to added Bax, and MOMs displayed a lag phase not observed with liposomes. Heat-labile MOM proteins were required for this enhanced response. A two-tiered mathematical model closely fit the kinetic data: first, Bax activation promotes the assembly of a multimeric complex, which then catalyzes the second reaction, Bax-dependent pore formation. Bax insertion occurred immediately upon Bax addition, prior to the end of the lag phase. Permeabilization kinetics were affected in a reciprocal manner by [cBid] and [Bax], confirming the "hit-and-run" hypothesis of cBid-induced direct Bax activation. Surprisingly, MOMP rate constants were linearly related to [Bax], implying that Bax acts non-cooperatively. Thus, the oligomeric catalyst is distinct from Bax. Moreover, contrary to common assumption, pore formation kinetics depend on Bax monomers, not oligomers. Catalyst formation exhibited a sharp transition in activation energy at ∼28°C, suggesting a role for membrane lipid packing. Furthermore, catalyst formation was strongly inhibited by chemical antagonists of the yeast mitochondrial fission protein, Dnm1. However, the mammalian ortholog, Drp1, was undetectable in mitochondrial outer membranes. Moreover, ATP and GTP were dispensable for MOMP. Thus, the data argue that oligomerization of a catalyst protein, distinct from Bax and Drp1, facilitates MOMP, possibly through a membrane-remodeling event.
Keywords	Biology (General) ; QH301-705.5
Subject code	570
Language	English
Publishing date	2012-01-01T00:00:00Z
Publisher	Public Library of Science (PLoS)
Document type	Article ; Online
Database	BASE - Bielefeld Academic Search Engine (life sciences selection)

Full text online

Full text

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.

Article ; Online: Caspase-independent mitochondrial cell death results from loss of respiration, not cytotoxic protein release.

Lartigue, Lydia / Kushnareva, Yulia / Seong, Youngmo / Lin, Helen / Faustin, Benjamin / Newmeyer, Donald D

Molecular biology of the cell

2009 Volume 20, Issue 23, Page(s) 4871–4884

Abstract: In apoptosis, mitochondrial outer membrane permeabilization (MOMP) triggers caspase-dependent death. However, cells undergo clonogenic death even if caspases are blocked. One proposed mechanism involved the release of cytotoxic proteins (e.g., AIF and ... ...

Abstract	In apoptosis, mitochondrial outer membrane permeabilization (MOMP) triggers caspase-dependent death. However, cells undergo clonogenic death even if caspases are blocked. One proposed mechanism involved the release of cytotoxic proteins (e.g., AIF and endoG) from mitochondria. To initiate MOMP directly without side effects, we created a tamoxifen-switchable BimS fusion protein. Surprisingly, even after MOMP, caspase-inhibited cells replicated DNA and divided for approximately 48 h before undergoing proliferation arrest. AIF and endoG remained in mitochondria. However, cells gradually lost mitochondrial membrane potential and ATP content, and DNA synthesis slowed to a halt by 72 h. These defects resulted from a partial loss of respiratory function, occurring 4-8 h after MOMP, that was not merely due to dispersion of cytochrome c. In particular, Complex I activity was completely lost, and Complex IV activity was reduced by approximately 70%, whereas Complex II was unaffected. Later, cells exhibited a more profound loss of mitochondrial protein constituents. Thus, under caspase inhibition, MOMP-induced clonogenic death results from a progressive loss of mitochondrial function, rather than the release of cytotoxic proteins from mitochondria.
MeSH term(s)	Amino Acid Chloromethyl Ketones/metabolism ; Animals ; Apoptosis Inducing Factor/metabolism ; Apoptosis Regulatory Proteins/genetics ; Apoptosis Regulatory Proteins/metabolism ; Bcl-2-Like Protein 11 ; Caspases/metabolism ; Cell Death/physiology ; Cell Line ; Cell Proliferation ; Cell Respiration/physiology ; Cysteine Proteinase Inhibitors/metabolism ; Cytochromes c/metabolism ; Enzyme Activation ; Glucose/metabolism ; Glycolysis/physiology ; Humans ; Intracellular Membranes/metabolism ; Membrane Proteins/genetics ; Membrane Proteins/metabolism ; Mitochondria/drug effects ; Mitochondria/metabolism ; Mitochondria/ultrastructure ; Mitochondrial Proteins/metabolism ; Oxygen Consumption ; Proto-Oncogene Proteins/genetics ; Proto-Oncogene Proteins/metabolism ; Recombinant Fusion Proteins/genetics ; Recombinant Fusion Proteins/metabolism ; Uncoupling Agents/metabolism ; bcl-2-Associated X Protein/metabolism
Chemical Substances	Amino Acid Chloromethyl Ketones ; Apoptosis Inducing Factor ; Apoptosis Regulatory Proteins ; BCL2L11 protein, human ; Bcl-2-Like Protein 11 ; Cysteine Proteinase Inhibitors ; Membrane Proteins ; Mitochondrial Proteins ; Proto-Oncogene Proteins ; Recombinant Fusion Proteins ; Uncoupling Agents ; bcl-2-Associated X Protein ; benzyloxycarbonylvalyl-alanyl-aspartyl fluoromethyl ketone ; Cytochromes c (9007-43-6) ; Caspases (EC 3.4.22.-) ; Glucose (IY9XDZ35W2)
Language	English
Publishing date	2009-09-30
Publishing country	United States
Document type	Journal Article ; Research Support, N.I.H., Extramural
ZDB-ID	1098979-1
ISSN	1939-4586 ; 1059-1524
ISSN (online)	1939-4586
ISSN	1059-1524
DOI	10.1091/mbc.E09-07-0649
Database	MEDical Literature Analysis and Retrieval System OnLINE

Full text online

Accessible to users with ZB MED library card

In stock of ZB MED Cologne/Königswinter

Zs.A 2853: 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)
Zs.MO 410: Show issues

Order via subito

Details ▾

To top

More links

Kategorien

In stock of ZB MED Cologne/Königswinter

Order via subito

More links

Kategorien

Order via subito

More links

Kategorien

In stock of ZB MED Cologne/Königswinter

Order via subito

More links

Kategorien

Order via subito

Inter-library loan at ZB MED

Full text online

More links

Kategorien

Inter-library loan at ZB MED

Full text online

More links

Kategorien

In stock of ZB MED Cologne/Königswinter

Order via subito

More links

Kategorien

Order via subito

Inter-library loan at ZB MED

More links

Kategorien

In stock of ZB MED Cologne/Königswinter

Order via subito

Full text online

More links

Kategorien

Inter-library loan at ZB MED

Full text online

More links

Kategorien

In stock of ZB MED Cologne/Königswinter

Order via subito