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Article ; Online ; Conference proceedings: Special Issue on Cell Death: Murder, mystery (and a little bit of mayhem) in Manhattan.

Chipuk, Jerry E / Martin, Seamus J

2016 Volume 283, Issue 14, Page(s) 2565–2567

Abstract: This Special Issue on Cell Death comprises a series of 12 reviews that span a broad spectrum of topics within highly active research areas in the cell death field. We hope that you will find these pieces to be of interest; we certainly found them to be ... ...

Abstract	This Special Issue on Cell Death comprises a series of 12 reviews that span a broad spectrum of topics within highly active research areas in the cell death field. We hope that you will find these pieces to be of interest; we certainly found them to be fresh and engaging and we are grateful to their authors for taking the time to write for The FEBS Journal.
MeSH term(s)	Animals ; Cell Death ; Humans ; New York City ; Research
Language	English
Publishing date	2016-07
Publishing country	England
Document type	Congresses ; Introductory Journal Article
ZDB-ID	2173655-8
ISSN	1742-4658 ; 1742-464X
ISSN (online)	1742-4658
ISSN	1742-464X
DOI	10.1111/febs.13782
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Article: Special Issue on Cell Death: Murder, mystery (and a little bit of mayhem) in Manhattan

Chipuk, Jerry E / Seamus J. Martin

FEBS journal. 2016 July, v. 283, no. 14

2016

Abstract	This Special Issue on Cell Death comprises a series of 12 reviews that span a broad spectrum of topics within highly active research areas in the cell death field. We hope that you will find these pieces to be of interest; we certainly found them to be fresh and engaging and we are grateful to their authors for taking the time to write for The FEBS Journal.
Keywords	cell death ; cytotoxicity ; endoplasmic reticulum ; proteinases
Language	English
Dates of publication	2016-07
Size	p. 2565-2567.
Publishing place	John Wiley & Sons, Ltd
Document type	Article
Note	JOURNAL ARTICLE
ZDB-ID	2173655-8
ISSN	1742-4658 ; 1742-464X
ISSN (online)	1742-4658
ISSN	1742-464X
DOI	10.1111/febs.13782
Database	NAL-Catalogue (AGRICOLA)

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Article ; Online: Sustained CD28 costimulation is required for self-renewal and differentiation of TCF-1

Humblin, Etienne / Korpas, Isabel / Lu, Jiahua / Filipescu, Dan / van der Heide, Verena / Goldstein, Simon / Vaidya, Abishek / Soares-Schanoski, Alessandra / Casati, Beatrice / Selvan, Myvizhi E / Gümüş, Zeynep H / Wieland, Andreas / Corrado, Mauro / Cohen-Gould, Leona / Bernstein, Emily / Homann, Dirk / Chipuk, Jerry / Kamphorst, Alice O

Science immunology

2023 Volume 8, Issue 86, Page(s) eadg0878

Abstract: During persistent antigen stimulation, such as in chronic infections and cancer, CD8 T cells differentiate into a hypofunctional programmed death protein 1-positive (PD- ... ...

Abstract	During persistent antigen stimulation, such as in chronic infections and cancer, CD8 T cells differentiate into a hypofunctional programmed death protein 1-positive (PD-1
MeSH term(s)	T Cell Transcription Factor 1/genetics ; CD28 Antigens ; Programmed Cell Death 1 Receptor ; CD8-Positive T-Lymphocytes ; Cell Differentiation ; Transcription Factors
Chemical Substances	T Cell Transcription Factor 1 ; CD28 Antigens ; Programmed Cell Death 1 Receptor ; Transcription Factors
Language	English
Publishing date	2023-08-25
Publishing country	United States
Document type	Journal Article ; Research Support, N.I.H., Extramural ; Research Support, Non-U.S. Gov't
ISSN	2470-9468
ISSN (online)	2470-9468
DOI	10.1126/sciimmunol.adg0878
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Article ; Online ; Conference proceedings: From zero to sixty: cell death signaling in the city that never sleeps.

Gelles, J D / Elkholi, R / Serasinghe, M N / Luna-Vargas, M P A / Chipuk, J E

Oncogene

2016 Volume 35, Issue 11, Page(s) 1457–1460

MeSH term(s)	Animals ; Cell Death/physiology ; Humans ; Signal Transduction/physiology
Language	English
Publishing date	2016-03-17
Publishing country	England
Document type	Congresses ; Research Support, N.I.H., Extramural ; Research Support, Non-U.S. Gov't
ZDB-ID	639046-8
ISSN	1476-5594 ; 0950-9232
ISSN (online)	1476-5594
ISSN	0950-9232
DOI	10.1038/onc.2015.194
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Article ; Online: Examining BCL-2 family function with large unilamellar vesicles.

Asciolla, James J / Renault, Thibaud T / Chipuk, Jerry E

Journal of visualized experiments : JoVE

2012 , Issue 68

Abstract: ... that collaborate to either maintain cell survival or initiate apoptosis(1). Following cellular stress (e.g., DNA ... apoptotic proteins (e.g., cytochrome c) gain access to the cytoplasm, promote caspase activation, and ... proteins, such as BID (BH3-interacting domain agonist)(3-6). Anti-apoptotic BCL-2 family proteins (e.g ...

Abstract	The BCL-2 (B cell CLL/Lymphoma) family is comprised of approximately twenty proteins that collaborate to either maintain cell survival or initiate apoptosis(1). Following cellular stress (e.g., DNA damage), the pro-apoptotic BCL-2 family effectors BAK (BCL-2 antagonistic killer 1) and/or BAX (BCL-2 associated X protein) become activated and compromise the integrity of the outer mitochondrial membrane (OMM), though the process referred to as mitochondrial outer membrane permeabilization (MOMP)(1). After MOMP occurs, pro-apoptotic proteins (e.g., cytochrome c) gain access to the cytoplasm, promote caspase activation, and apoptosis rapidly ensues(2). In order for BAK/BAX to induce MOMP, they require transient interactions with members of another pro-apoptotic subset of the BCL-2 family, the BCL-2 homology domain 3 (BH3)-only proteins, such as BID (BH3-interacting domain agonist)(3-6). Anti-apoptotic BCL-2 family proteins (e.g., BCL-2 related gene, long isoform, BCL-xL; myeloid cell leukemia 1, MCL-1) regulate cellular survival by tightly controlling the interactions between BAK/BAX and the BH3-only proteins capable of directly inducing BAK/BAX activation(7,8). In addition, anti-apoptotic BCL-2 protein availability is also dictated by sensitizer/de-repressor BH3-only proteins, such as BAD (BCL-2 antagonist of cell death) or PUMA (p53 upregulated modulator of apoptosis), which bind and inhibit anti-apoptotic members(7,9). As most of the anti-apoptotic BCL-2 repertoire is localized to the OMM, the cellular decision to maintain survival or induce MOMP is dictated by multiple BCL-2 family interactions at this membrane. Large unilamellar vesicles (LUVs) are a biochemical model to explore relationships between BCL-2 family interactions and membrane permeabilization(10). LUVs are comprised of defined lipids that are assembled in ratios identified in lipid composition studies from solvent extracted Xenopus mitochondria (46.5% phosphatidylcholine, 28.5% phosphatidylethanoloamine, 9% phosphatidylinositol, 9% phosphatidylserine, and 7% cardiolipin)(10). This is a convenient model system to directly explore BCL-2 family function because the protein and lipid components are completely defined and tractable, which is not always the case with primary mitochondria. While cardiolipin is not usually this high throughout the OMM, this model does faithfully mimic the OMM to promote BCL-2 family function. Furthermore, a more recent modification of the above protocol allows for kinetic analyses of protein interactions and real-time measurements of membrane permeabilization, which is based on LUVs containing a polyanionic dye (ANTS: 8-aminonaphthalene-1,3,6-trisulfonic acid) and cationic quencher (DPX: p-xylene-bis-pyridinium bromide)(11). As the LUVs permeabilize, ANTS and DPX diffuse apart, and a gain in fluorescence is detected. Here, commonly used recombinant BCL-2 family protein combinations and controls using the LUVs containing ANTS/DPX are described.
MeSH term(s)	Animals ; BH3 Interacting Domain Death Agonist Protein/chemistry ; BH3 Interacting Domain Death Agonist Protein/metabolism ; Humans ; Liposomes/chemistry ; Liposomes/metabolism ; Naphthalenes/chemistry ; Naphthalenes/metabolism ; Proto-Oncogene Proteins c-bcl-2/chemistry ; Proto-Oncogene Proteins c-bcl-2/metabolism ; Pyridinium Compounds/chemistry ; Pyridinium Compounds/metabolism ; Xenopus ; bcl-2-Associated X Protein/chemistry ; bcl-2-Associated X Protein/metabolism
Chemical Substances	BAX protein, human ; BH3 Interacting Domain Death Agonist Protein ; BID protein, human ; Liposomes ; Naphthalenes ; Proto-Oncogene Proteins c-bcl-2 ; Pyridinium Compounds ; bcl-2-Associated X Protein ; N,N'-4-xylylenebis(pyridinium) (14208-10-7) ; 8-amino-1,3,6-naphthalenetrisulfonic acid (D33V8NB7KB)
Language	English
Publishing date	2012-10-05
Publishing country	United States
Document type	Journal Article ; Research Support, N.I.H., Extramural ; Research Support, Non-U.S. Gov't ; Video-Audio Media
ZDB-ID	2259946-0
ISSN	1940-087X ; 1940-087X
ISSN (online)	1940-087X
ISSN	1940-087X
DOI	10.3791/4291
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Article ; Online: Mitochondrial localization and moderated activity are key to murine erythroid enucleation.

Liang, Raymond / Menon, Vijay / Qiu, Jiajing / Arif, Tasleem / Renuse, Santosh / Lin, Miao / Nowak, Roberta / Hartmann, Boris / Tzavaras, Nikos / Benson, Deanna L / Chipuk, Jerry E / Fribourg, Miguel / Pandey, Akhilesh / Fowler, Velia / Ghaffari, Saghi

Blood advances

2021 Volume 5, Issue 10, Page(s) 2490–2504

Abstract: Mammalian red blood cells (RBCs), which primarily contain hemoglobin, exemplify an elaborate maturation process, with the terminal steps of RBC generation involving extensive cellular remodeling. This encompasses alterations of cellular content through ... ...

Abstract	Mammalian red blood cells (RBCs), which primarily contain hemoglobin, exemplify an elaborate maturation process, with the terminal steps of RBC generation involving extensive cellular remodeling. This encompasses alterations of cellular content through distinct stages of erythroblast maturation that result in the expulsion of the nucleus (enucleation) followed by the loss of mitochondria and all other organelles and a transition to anaerobic glycolysis. Whether there is any link between erythroid removal of the nucleus and the function of any other organelle, including mitochondria, remains unknown. Here we demonstrate that mitochondria are key to nuclear clearance. Using live and confocal microscopy and high-throughput single-cell imaging, we show that before nuclear polarization, mitochondria progressively move toward one side of maturing erythroblasts and aggregate near the nucleus as it extrudes from the cell, a prerequisite for enucleation to proceed. Although we found active mitochondrial respiration is required for nuclear expulsion, levels of mitochondrial activity identify distinct functional subpopulations, because terminally maturing erythroblasts with low relative to high mitochondrial membrane potential are at a later stage of maturation, contain greatly condensed nuclei with reduced open chromatin-associated acetylation histone marks, and exhibit higher enucleation rates. Lastly, to our surprise, we found that late-stage erythroblasts sustain mitochondrial metabolism and subsequent enucleation, primarily through pyruvate but independent of in situ glycolysis. These findings demonstrate the critical but unanticipated functions of mitochondria during the erythroblast enucleation process. They are also relevant to the in vitro production of RBCs as well as to disorders of the erythroid lineage.
MeSH term(s)	Animals ; Cell Nucleus/metabolism ; Chromatin/metabolism ; Erythroblasts/metabolism ; Erythrocytes ; Mice ; Mitochondria
Chemical Substances	Chromatin
Language	English
Publishing date	2021-05-24
Publishing country	United States
Document type	Journal Article ; Research Support, N.I.H., Extramural ; Research Support, Non-U.S. Gov't
ZDB-ID	2915908-8
ISSN	2473-9537 ; 2473-9529
ISSN (online)	2473-9537
ISSN	2473-9529
DOI	10.1182/bloodadvances.2021004259
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Article: Dissecting p53-dependent apoptosis.

Chipuk, J E / Green, D R

Cell death and differentiation

2006 Volume 13, Issue 6, Page(s) 994–1002

Abstract: The complexity of the p53 protein, coupled with the vast cellular responses to p53, is simply astonishing. As new isoforms, functional domains and protein-protein interactions are described; each morsel of information forces us to think (and re-think) ... ...

Abstract	The complexity of the p53 protein, coupled with the vast cellular responses to p53, is simply astonishing. As new isoforms, functional domains and protein-protein interactions are described; each morsel of information forces us to think (and re-think) about how it 'fits' into the current p53 paradigm. One aspect of p53 signaling that is under refinement is the mechanism(s) leading to apoptosis. Here we discuss what is known about p53-induced apoptosis, what proteins and protein-protein interactions are responsible for regulating apoptosis, how can this cascade be genetically dissected, and what pharmacological tools are available to modulate p53-dependent apoptosis. While everything may not comfortably fit into our understanding of p53, all of these data will certainly broaden our viewpoint on the complexity and significance of the p53-induced apoptotic pathway. Here, our discussion is primarily focused on the works presented at the 12th International p53 Workshop, except where appropriate background is required.
MeSH term(s)	Animals ; Antineoplastic Agents/pharmacology ; Apoptosis ; Aza Compounds/pharmacology ; Bridged Bicyclo Compounds, Heterocyclic/pharmacology ; Cell Transformation, Neoplastic/drug effects ; Cell Transformation, Neoplastic/genetics ; Cell Transformation, Neoplastic/metabolism ; Humans ; Imidazoles/pharmacology ; Mice ; Mice, Knockout ; Mutation ; Piperazines/pharmacology ; Proto-Oncogene Proteins c-bcl-2/genetics ; Proto-Oncogene Proteins c-bcl-2/metabolism ; Proto-Oncogene Proteins c-mdm2/antagonists & inhibitors ; Proto-Oncogene Proteins c-mdm2/metabolism ; Transcription, Genetic ; Tumor Suppressor Protein p53/genetics ; Tumor Suppressor Protein p53/metabolism
Chemical Substances	Antineoplastic Agents ; Aza Compounds ; Bridged Bicyclo Compounds, Heterocyclic ; Imidazoles ; Piperazines ; Proto-Oncogene Proteins c-bcl-2 ; Tumor Suppressor Protein p53 ; nutlin 1 ; Proto-Oncogene Proteins c-mdm2 (EC 2.3.2.27) ; 2,2-bis(hydroxymethyl)-1-azabicyclo(2,2,2,)octan-3-one (GHC34M30BG)
Language	English
Publishing date	2006-02-24
Publishing country	England
Document type	Journal Article ; Review
ZDB-ID	1225672-9
ISSN	1350-9047
ISSN	1350-9047
DOI	10.1038/sj.cdd.4401908
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Zs.A 4230: 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)
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Article: Born to be alive: a role for the BCL-2 family in melanoma tumor cell survival, apoptosis, and treatment.

Anvekar, Rina A / Asciolla, James J / Missert, Derek J / Chipuk, Jerry E

Frontiers in oncology

2012 Volume 1, Issue 34

Abstract: ... by the BCL-2 family of proteins.The BCL-2 family is comprised of anti-apoptotic proteins (e.g., BCL-2, BCL-xL ... and MCL-1) and pro-apoptotic proteins (e.g., BAK, BAX, and BIM), and their coordinated regulation and ...

Abstract	The global incidence of melanoma has dramatically increased during the recent decades, yet the advancement of primary and adjuvant therapies has not kept a similar pace. The development of melanoma is often centered on cellular signaling that hyper-activates survival pathways, while inducing a concomitant blockade to cell death. Aberrations in cell death signaling not only promote tumor survival and enhanced metastatic potential, but also create resistance to anti-tumor strategies. Chemotherapeutic agents target melanoma tumor cells by inducing a form of cell death called apoptosis, which is governed by the BCL-2 family of proteins.The BCL-2 family is comprised of anti-apoptotic proteins (e.g., BCL-2, BCL-xL, and MCL-1) and pro-apoptotic proteins (e.g., BAK, BAX, and BIM), and their coordinated regulation and function are essential for optimal responses to chemotherapeutics. Here we will discuss what is currently known about the mechanisms of BCL-2 family function with a focus on the signaling pathways that maintain melanoma tumor cell survival. Importantly, we will critically evaluate the literature regarding how chemotherapeutic strategies directly impact on BCL-2 family function and offer several suggestions for future regimens to target melanoma and enhance patient survival.
Language	English
Publishing date	2012-01-19
Publishing country	Switzerland
Document type	Journal Article
ZDB-ID	2649216-7
ISSN	2234-943X
ISSN	2234-943X
DOI	10.3389/fonc.2011.00034
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Article ; Online: Author Correction: A local tumor microenvironment acquired super-enhancer induces an oncogenic driver in colorectal carcinoma.

Zhou, Royce W / Xu, Jia / Martin, Tiphaine C / Zachem, Alexis L / He, John / Ozturk, Sait / Demircioglu, Deniz / Bansal, Ankita / Trotta, Andrew P / Giotti, Bruno / Gryder, Berkley / Shen, Yao / Wu, Xuewei / Carcamo, Saul / Bosch, Kaitlyn / Hopkins, Benjamin / Tsankov, Alexander / Steinhagen, Randolph / Jones, Drew R /

Asara, John / Chipuk, Jerry E / Brody, Rachel / Itzkowitz, Steven / Chio, Iok In Christine / Hasson, Dan / Bernstein, Emily / Parsons, Ramon E

Nature communications

2023 Volume 14, Issue 1, Page(s) 1923

Language	English
Publishing date	2023-04-06
Publishing country	England
Document type	Published Erratum
ZDB-ID	2553671-0
ISSN	2041-1723 ; 2041-1723
ISSN (online)	2041-1723
ISSN	2041-1723
DOI	10.1038/s41467-023-37640-4
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Article ; Online: Late-onset megaconial myopathy in mice lacking group I Paks.

Joseph, Giselle A / Hung, Margaret / Goel, Aviva J / Hong, Mingi / Rieder, Marysia-Kolbe / Beckmann, Noam D / Serasinghe, Madhavika N / Chipuk, Jerry E / Devarakonda, Parvathi M / Goldhamer, David J / Aldana-Hernandez, Paulina / Curtis, Jonathan / Jacobs, René L / Krauss, Robert S

Skeletal muscle

2019 Volume 9, Issue 1, Page(s) 5

Abstract: Background: Group I Paks are serine/threonine kinases that function as major effectors of the small GTPases Rac1 and Cdc42, and they regulate cytoskeletal dynamics, cell polarity, and transcription. We previously demonstrated that Pak1 and Pak2 function ...

Abstract	Background: Group I Paks are serine/threonine kinases that function as major effectors of the small GTPases Rac1 and Cdc42, and they regulate cytoskeletal dynamics, cell polarity, and transcription. We previously demonstrated that Pak1 and Pak2 function redundantly to promote skeletal myoblast differentiation during postnatal development and regeneration in mice. However, the roles of Pak1 and Pak2 in adult muscle homeostasis are unknown. Choline kinase β (Chk β) is important for adult muscle homeostasis, as autosomal recessive mutations in CHKβ are associated with two human muscle diseases, megaconial congenital muscular dystrophy and proximal myopathy with focal depletion of mitochondria. Methods: We analyzed mice conditionally lacking Pak1 and Pak2 in the skeletal muscle lineage (double knockout (dKO) mice) over 1 year of age. Muscle integrity in dKO mice was assessed with histological stains, immunofluorescence, electron microscopy, and western blotting. Assays for mitochondrial respiratory complex function were performed, as was mass spectrometric quantification of products of choline kinase. Mice and cultured myoblasts deficient for choline kinase β (Chk β) were analyzed for Pak1/2 phosphorylation. Results: dKO mice developed an age-related myopathy. By 10 months of age, dKO mouse muscles displayed centrally-nucleated myofibers, fibrosis, and signs of degeneration. Disease severity occurred in a rostrocaudal gradient, hindlimbs more strongly affected than forelimbs. A distinctive feature of this myopathy was elongated and branched intermyofibrillar (megaconial) mitochondria, accompanied by focal mitochondrial depletion in the central region of the fiber. dKO muscles showed reduced mitochondrial respiratory complex I and II activity. These phenotypes resemble those of rmd mice, which lack Chkβ and are a model for human diseases associated with CHKβ deficiency. Pak1/2 and Chkβ activities were not interdependent in mouse skeletal muscle, suggesting a more complex relationship in regulation of mitochondria and muscle homeostasis. Conclusions: Conditional loss of Pak1 and Pak2 in mice resulted in an age-dependent myopathy with similarity to mice and humans with CHKβ deficiency. Protein kinases are major regulators of most biological processes but few have been implicated in muscle maintenance or disease. Pak1/Pak2 dKO mice offer new insights into these processes.
MeSH term(s)	Animals ; Choline Kinase/metabolism ; Female ; Male ; Mice, Knockout ; Mitochondria/metabolism ; Mitochondria/ultrastructure ; Mitochondrial Myopathies/genetics ; Mitochondrial Myopathies/metabolism ; Mitochondrial Myopathies/pathology ; Mitochondrial Proteins/metabolism ; Muscle, Skeletal/metabolism ; Muscle, Skeletal/ultrastructure ; p21-Activated Kinases/genetics ; p21-Activated Kinases/metabolism
Chemical Substances	Mitochondrial Proteins ; Choline Kinase (EC 2.7.1.32) ; Pak1 protein, mouse (EC 2.7.11.1) ; Pak2 protein, mouse (EC 2.7.11.1) ; p21-Activated Kinases (EC 2.7.11.1)
Language	English
Publishing date	2019-02-21
Publishing country	England
Document type	Journal Article ; Research Support, N.I.H., Extramural ; Research Support, Non-U.S. Gov't
ZDB-ID	2595637-1
ISSN	2044-5040 ; 2044-5040
ISSN (online)	2044-5040
ISSN	2044-5040
DOI	10.1186/s13395-019-0191-4
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