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Article ; Online: Connecting autoimmune disease to Bardet-Biedl syndrome and primary cilia.

Kanie, Tomoharu / Jackson, Peter K

2021 Volume 22, Issue 2, Page(s) e52180

Abstract: Bardet-Biedl syndrome (BBS) is a genetic disorder caused by the dysfunction of the primary cilium. To date, immunological defects in the disease have not been systematically assessed. In this issue, Tsyklauri and colleagues find, through detailed ... ...

Abstract	Bardet-Biedl syndrome (BBS) is a genetic disorder caused by the dysfunction of the primary cilium. To date, immunological defects in the disease have not been systematically assessed. In this issue, Tsyklauri and colleagues find, through detailed analysis of BBS mutant animals, that B-cell development is altered in mutant mice (Tsyklauri et al, 2021). The authors further report that BBS patients are more susceptible to autoimmune disorders. This study sheds new light on the potential role of primary cilia in controlling immune function in disease.
MeSH term(s)	Animals ; Autoimmune Diseases/genetics ; Bardet-Biedl Syndrome/genetics ; Cilia ; Hematopoiesis ; Humans ; Mice
Language	English
Publishing date	2021-01-28
Publishing country	England
Document type	Journal Article ; Comment
ZDB-ID	2020896-0
ISSN	1469-3178 ; 1469-221X
ISSN (online)	1469-3178
ISSN	1469-221X
DOI	10.15252/embr.202052180
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Article: Myristoylated Neuronal Calcium Sensor-1 captures the ciliary vesicle at distal appendages.

Kanie, Tomoharu / Ng, Roy / Abbott, Keene L / Pongs, Olaf / Jackson, Peter K

bioRxiv : the preprint server for biology

2023

Abstract: The primary cilium is a microtubule-based organelle that cycles through assembly and disassembly. In many cell types, formation of the cilium is initiated by recruitment of ciliary vesicles to the distal appendage of the mother centriole. However, the ... ...

Abstract	The primary cilium is a microtubule-based organelle that cycles through assembly and disassembly. In many cell types, formation of the cilium is initiated by recruitment of ciliary vesicles to the distal appendage of the mother centriole. However, the distal appendage mechanism that directly captures ciliary vesicles is yet to be identified. In an accompanying paper, we show that the distal appendage protein, CEP89, is important for thef ciliary vesicle recruitment, but not for other steps of cilium formation (Tomoharu Kanie, Love, Fisher, Gustavsson, & Jackson, 2023). The lack of a membrane binding motif in CEP89 suggests that it may indirectly recruit ciliary vesicles via another binding partner. Here, we identify Neuronal Calcium Sensor-1 (NCS1) as a stoichiometric interactor of CEP89. NCS1 localizes to the position between CEP89 and a ciliary vesicle marker, RAB34, at the distal appendage. This localization was completely abolished in CEP89 knockouts, suggesting that CEP89 recruits NCS1 to the distal appendage. Similarly to CEP89 knockouts, ciliary vesicle recruitment as well as subsequent cilium formation was perturbed in NCS1 knockout cells. The ability of NCS1 to recruit the ciliary vesicle is dependent on its myristoylation motif and NCS1 knockout cells expressing myristoylation defective mutant failed to rescue the vesicle recruitment defect despite localizing proper localization to the centriole. In sum, our analysis reveals the first known mechanism for how the distal appendage recruits the ciliary vesicles.
Language	English
Publishing date	2023-01-10
Publishing country	United States
Document type	Preprint
DOI	10.1101/2023.01.06.523037
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Article: A hierarchical pathway for assembly of the distal appendages that organize primary cilia.

Kanie, Tomoharu / Love, Julia F / Fisher, Saxton D / Gustavsson, Anna-Karin / Jackson, Peter K

bioRxiv : the preprint server for biology

2023

Abstract: Distal appendages are nine-fold symmetric blade-like structures attached to the distal end of the mother centriole. These structures are critical for formation of the primary cilium, by regulating at least four critical steps: ciliary vesicle recruitment, ...

Abstract	Distal appendages are nine-fold symmetric blade-like structures attached to the distal end of the mother centriole. These structures are critical for formation of the primary cilium, by regulating at least four critical steps: ciliary vesicle recruitment, recruitment and initiation of intraflagellar transport (IFT), and removal of CP110. While specific proteins that localize to the distal appendages have been identified, how exactly each protein functions to achieve the multiple roles of the distal appendages is poorly understood. Here we comprehensively analyze known and newly discovered distal appendage proteins (CEP83, SCLT1, CEP164, TTBK2, FBF1, CEP89, KIZ, ANKRD26, PIDD1, LRRC45, NCS1, C3ORF14) for their precise localization, order of recruitment, and their roles in each step of cilia formation. Using CRISPR-Cas9 knockouts, we show that the order of the recruitment of the distal appendage proteins is highly interconnected and a more complex hierarchy. Our analysis highlights two protein modules, CEP83-SCLT1 and CEP164-TTBK2, as critical for structural assembly of distal appendages. Functional assay revealed that CEP89 selectively functions in RAB34
Language	English
Publishing date	2023-01-10
Publishing country	United States
Document type	Preprint
DOI	10.1101/2023.01.06.522944
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Article: Guanine Nucleotide Exchange Assay Using Fluorescent MANT-GDP.

Kanie, Tomoharu / Jackson, Peter K

Bio-protocol

2018 Volume 8, Issue 7

Abstract: GTPases are molecular switches that cycle between the inactive GDP-bound state and the active GTP-bound state. GTPases exchange nucleotides either by its intrinsic nucleotide exchange or by interaction with guanine nucleotide exchange factors (GEFs). ... ...

Abstract	GTPases are molecular switches that cycle between the inactive GDP-bound state and the active GTP-bound state. GTPases exchange nucleotides either by its intrinsic nucleotide exchange or by interaction with guanine nucleotide exchange factors (GEFs). Monitoring the nucleotide exchange
Language	English
Publishing date	2018-06-27
Publishing country	United States
Document type	Journal Article
ZDB-ID	2833269-6
ISSN	2331-8325
ISSN	2331-8325
DOI	10.21769/BioProtoc.2795
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Article: Single-molecule imaging in the primary cilium.

Weiss, Lucien E / Love, Julia F / Yoon, Joshua / Comerci, Colin J / Milenkovic, Ljiljana / Kanie, Tomoharu / Jackson, Peter K / Stearns, Tim / Gustavsson, Anna-Karin

Methods in cell biology

2023 Volume 176, Page(s) 59–83

Abstract: The primary cilium is an important signaling organelle critical for normal development and tissue homeostasis. Its small dimensions and complexity necessitate advanced imaging approaches to uncover the molecular mechanisms behind its function. Here, we ... ...

Abstract	The primary cilium is an important signaling organelle critical for normal development and tissue homeostasis. Its small dimensions and complexity necessitate advanced imaging approaches to uncover the molecular mechanisms behind its function. Here, we outline how single-molecule fluorescence microscopy can be used for tracking molecular dynamics and interactions and for super-resolution imaging of nanoscale structures in the primary cilium. Specifically, we describe in detail how to capture and quantify the 2D dynamics of individual transmembrane proteins PTCH1 and SMO and how to map the 3D nanoscale distributions of the inversin compartment proteins INVS, ANKS6, and NPHP3. This protocol can, with minor modifications, be adapted for studies of other proteins and cell lines to further elucidate the structure and function of the primary cilium at the molecular level.
MeSH term(s)	Humans ; Cilia/metabolism ; Single Molecule Imaging ; Kidney Diseases, Cystic/metabolism ; Signal Transduction ; Cell Line
Language	English
Publishing date	2023-02-24
Publishing country	United States
Document type	Journal Article ; Research Support, N.I.H., Extramural ; Research Support, Non-U.S. Gov't
ISSN	0091-679X
ISSN	0091-679X
DOI	10.1016/bs.mcb.2023.01.003
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Article ; Online: The IFT81-IFT74 complex acts as an unconventional RabL2 GTPase-activating protein during intraflagellar transport.

Boegholm, Niels / Petriman, Narcis A / Loureiro-López, Marta / Wang, Jiaolong / Vela, Miren Itxaso Santiago / Liu, Beibei / Kanie, Tomoharu / Ng, Roy / Jackson, Peter K / Andersen, Jens S / Lorentzen, Esben

The EMBO journal

2023 Volume 42, Issue 18, Page(s) e111807

Abstract: Cilia are important cellular organelles for signaling and motility and are constructed via intraflagellar transport (IFT). RabL2 is a small GTPase that localizes to the basal body of cilia via an interaction with the centriolar protein CEP19 before ... ...

Abstract	Cilia are important cellular organelles for signaling and motility and are constructed via intraflagellar transport (IFT). RabL2 is a small GTPase that localizes to the basal body of cilia via an interaction with the centriolar protein CEP19 before downstream association with the IFT machinery, which is followed by initiation of IFT. We reconstituted and purified RabL2 with CEP19 or IFT proteins to show that a reconstituted pentameric IFT complex containing IFT81/74 enhances the GTP hydrolysis rate of RabL2. The binding site on IFT81/74 that promotes GTP hydrolysis in RabL2 was mapped to a 70-amino-acid-long coiled-coil region of IFT81/74. We present structural models for RabL2-containing IFT complexes that we validate in vitro and in cellulo and demonstrate that Chlamydomonas IFT81/74 enhances GTP hydrolysis of human RabL2, suggesting an ancient evolutionarily conserved activity. Our results provide an architectural understanding of how RabL2 is incorporated into the IFT complex and a molecular rationale for why RabL2 dissociates from anterograde IFT trains soon after departure from the ciliary base.
MeSH term(s)	Humans ; GTPase-Activating Proteins/genetics ; Signal Transduction ; Biological Transport ; Amino Acids ; Guanosine Triphosphate ; Muscle Proteins ; Cytoskeletal Proteins
Chemical Substances	GTPase-Activating Proteins ; Amino Acids ; Guanosine Triphosphate (86-01-1) ; IFT81 protein, human ; Muscle Proteins ; IFT74 protein, human ; Cytoskeletal Proteins
Language	English
Publishing date	2023-08-22
Publishing country	England
Document type	Journal Article ; Research Support, N.I.H., Extramural ; Research Support, Non-U.S. Gov't
ZDB-ID	586044-1
ISSN	1460-2075 ; 0261-4189
ISSN (online)	1460-2075
ISSN	0261-4189
DOI	10.15252/embj.2022111807
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Article ; Online: Tetraspanin Tspan8 restrains interferon signaling to stabilize intestinal epithelium by directing endocytosis of interferon receptor.

Min, Jiang / Yang, Shenglan / Cai, Yang / Vanderwall, David R / Wu, Zhiping / Li, Shuping / Liu, Songlan / Liu, Beibei / Wang, Jie / Ding, Yingjun / Chen, Junxiong / Jiang, Chao / Wren, Jonathan D / Csiszar, Anna / Ungvari, Zoltan / Greco, Céline / Kanie, Tomoharu / Peng, Junmin / Zhang, Xin A

Cellular and molecular life sciences : CMLS

2023 Volume 80, Issue 6, Page(s) 154

Abstract: Inflammation can impair intestinal barrier, while increased epithelial permeability can lead to inflammation. In this study, we found that the expression of Tspan8, a tetraspanin expressed specifically in epithelial cells, is downregulated in mouse model ...

Abstract	Inflammation can impair intestinal barrier, while increased epithelial permeability can lead to inflammation. In this study, we found that the expression of Tspan8, a tetraspanin expressed specifically in epithelial cells, is downregulated in mouse model of ulcerative disease (UC) but correlated with those of cell-cell junction components, such as claudins and E-cadherin, suggesting that Tspan8 supports intestinal epithelial barrier. Tspan8 removal increases intestinal epithelial permeability and upregulates IFN-γ-Stat1 signaling. We also demonstrated that Tspan8 coalesces with lipid rafts and facilitates IFNγ-R1 localization at or near lipid rafts. As IFN-γ induces its receptor undergoing clathrin- or lipid raft-dependent endocytosis and IFN-γR endocytosis plays an important role in Jak-Stat1 signaling, our analysis on IFN-γR endocytosis revealed that Tspan8 silencing impairs lipid raft-mediated but promotes clathrin-mediated endocytosis of IFN-γR1, leading to increased Stat1 signaling. These changes in IFN-γR1 endocytosis upon Tspan8 silencing correlates with fewer lipid raft component GM1 at the cell surface and more clathrin heavy chain in the cells. Our findings indicate that Tspan8 determines the IFN-γR1 endocytosis route, to restrain Stat1 signaling, stabilize intestine epithelium, and subsequently prevent intestine from inflammation. Our finding also implies that Tspan8 is needed for proper endocytosis through lipid rafts.
MeSH term(s)	Animals ; Mice ; Clathrin/metabolism ; Endocytosis/physiology ; Inflammation/metabolism ; Interferons/metabolism ; Intestinal Mucosa/metabolism ; Receptors, Interferon/metabolism ; Tetraspanins/genetics ; Tetraspanins/metabolism
Chemical Substances	Clathrin ; Interferons (9008-11-1) ; Receptors, Interferon ; Tetraspanins
Language	English
Publishing date	2023-05-19
Publishing country	Switzerland
Document type	Journal Article
ZDB-ID	1358415-7
ISSN	1420-9071 ; 1420-682X
ISSN (online)	1420-9071
ISSN	1420-682X
DOI	10.1007/s00018-023-04803-x
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Article ; Online: CD151 Maintains Endolysosomal Protein Quality to Inhibit Vascular Inflammation.

Chen, Junxiong / Ding, Yingjun / Jiang, Chao / Qu, Rongmei / Wren, Jonathan D / Georgescu, Constantin / Wang, Xuejun / Reuter, Darlene N / Liu, Beibei / Giles, Cory B / Mayr, Christoph H / Schiller, Herbert B / Dai, Jingxing / Stipp, Christopher S / Subramaniyan, Bharathiraja / Wang, Jie / Zuo, Houjuan / Huang, Chao / Fung, Kar-Ming /

Rice, Heather C / Sonnenberg, Arnoud / Wu, David / Walters, Matthew S / Zhao, You-Yang / Kanie, Tomoharu / Hays, Franklin A / Papin, James F / Wang, Dao Wen / Zhang, Xin A

Circulation research

2024 Volume 134, Issue 10, Page(s) 1330–1347

Abstract: Background: Tetraspanin CD151 is highly expressed in endothelia and reinforces cell adhesion, but its role in vascular inflammation remains largely unknown.: Methods: In vitro molecular and cellular biological analyses on genetically modified ... ...

Abstract	Background: Tetraspanin CD151 is highly expressed in endothelia and reinforces cell adhesion, but its role in vascular inflammation remains largely unknown. Methods: In vitro molecular and cellular biological analyses on genetically modified endothelial cells, in vivo vascular biological analyses on genetically engineered mouse models, and in silico systems biology and bioinformatics analyses on CD151-related events. Results: Endothelial ablation of Conclusions: Distinct from its canonical function in strengthening cell adhesion at cell surface, CD151 maintains endolysosome function by sustaining VCP/p97-mediated protein unfolding and turnover. By supporting protein quality control and protein degradation, CD151 prevents proteins from (1) buildup in endolysosomes and (2) discharge through exosomes, to limit vascular inflammation. Also, our study conceptualizes that balance between degradation and discharge of proteins in endothelial cells determines vascular information. Thus, the IFITM3/V-ATPase-tetraspanin-VCP/p97 complexes on endolysosome, as a protein quality control and inflammation-inhibitory machinery, could be beneficial for therapeutic intervention against vascular inflammation.
MeSH term(s)	Animals ; Lysosomes/metabolism ; Tetraspanin 24/metabolism ; Tetraspanin 24/genetics ; Humans ; Mice ; COVID-19/metabolism ; COVID-19/immunology ; COVID-19/pathology ; Endosomes/metabolism ; Mice, Knockout ; Vasculitis/metabolism ; Mice, Inbred C57BL ; SARS-CoV-2 ; Inflammation/metabolism ; Inflammation/pathology ; Sepsis/metabolism
Chemical Substances	Tetraspanin 24 ; CD151 protein, human
Language	English
Publishing date	2024-04-01
Publishing country	United States
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	80100-8
ISSN	1524-4571 ; 0009-7330 ; 0931-6876
ISSN (online)	1524-4571
ISSN	0009-7330 ; 0931-6876
DOI	10.1161/CIRCRESAHA.123.323190
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Article ; Online: The CEP19-RABL2 GTPase Complex Binds IFT-B to Initiate Intraflagellar Transport at the Ciliary Base.

Kanie, Tomoharu / Abbott, Keene Louis / Mooney, Nancie Ann / Plowey, Edward Douglas / Demeter, Janos / Jackson, Peter Kent

Developmental cell

2017 Volume 42, Issue 1, Page(s) 22–36.e12

Abstract: Highly conserved intraflagellar transport (IFT) protein complexes direct both the assembly of primary cilia and the trafficking of signaling molecules. IFT complexes initially accumulate at the base of the cilium and periodically enter the cilium, ... ...

Abstract	Highly conserved intraflagellar transport (IFT) protein complexes direct both the assembly of primary cilia and the trafficking of signaling molecules. IFT complexes initially accumulate at the base of the cilium and periodically enter the cilium, suggesting an as-yet-unidentified mechanism that triggers ciliary entry of IFT complexes. Using affinity-purification and mass spectrometry of interactors of the centrosomal and ciliopathy protein, CEP19, we identify CEP350, FOP, and the RABL2B GTPase as proteins organizing the first known mechanism directing ciliary entry of IFT complexes. We discover that CEP19 is recruited to the ciliary base by the centriolar CEP350/FOP complex and then specifically captures GTP-bound RABL2B, which is activated via its intrinsic nucleotide exchange. Activated RABL2B then captures and releases its single effector, the intraflagellar transport B holocomplex, from the large pool of pre-docked IFT-B complexes, and thus initiates ciliary entry of IFT.
MeSH term(s)	Animals ; Cell Cycle Proteins/metabolism ; Centrioles/metabolism ; Cilia/metabolism ; Ciliopathies ; Flagella/metabolism ; Gene Knockout Techniques ; Guanosine Triphosphate/metabolism ; Mice, Inbred C57BL ; Mice, Knockout ; Multiprotein Complexes/metabolism ; Nucleotides/metabolism ; Phenotype ; Protein Binding ; Protein Stability ; Protein Transport ; Reproducibility of Results ; rab GTP-Binding Proteins/deficiency ; rab GTP-Binding Proteins/metabolism
Chemical Substances	CEP19 protein, human ; Cell Cycle Proteins ; Multiprotein Complexes ; Nucleotides ; Guanosine Triphosphate (86-01-1) ; RABL2 protein, mouse (EC 3.6.1.-) ; RABL2A protein, human (EC 3.6.1.-) ; rab GTP-Binding Proteins (EC 3.6.5.2)
Language	English
Publishing date	2017--10
Publishing country	United States
Document type	Journal Article ; Research Support, Non-U.S. Gov't ; Research Support, N.I.H., Extramural
ZDB-ID	2054967-2
ISSN	1878-1551 ; 1534-5807
ISSN (online)	1878-1551
ISSN	1534-5807
DOI	10.1016/j.devcel.2017.05.016
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Article: Development of mice without Cip/Kip CDK inhibitors

Tateishi, Yuki / Matsumoto, Akinobu / Kanie, Tomoharu / Hara, Eiji / Nakayama, Keiko / Nakayama, Keiichi I

Biochemical and biophysical research communications. 2012 Oct. 19, v. 427, no. 2

2012

Abstract: Timely exit of cells from the cell cycle is essential for proper cell differentiation during embryogenesis. Cyclin-dependent kinase (CDK) inhibitors (CKIs) of the Cip/Kip family (p21, p27, and p57) are negative regulators of cell cycle progression and ... ...

Abstract	Timely exit of cells from the cell cycle is essential for proper cell differentiation during embryogenesis. Cyclin-dependent kinase (CDK) inhibitors (CKIs) of the Cip/Kip family (p21, p27, and p57) are negative regulators of cell cycle progression and are thought to be essential for development. However, the extent of functional redundancy among Cip/Kip family members has remained largely unknown. We have now generated mice that lack all three Cip/Kip CKIs (TKO mice) and compared them with those lacking each possible pair of these proteins (DKO mice). We found that the TKO embryos develop normally until midgestation but die around embryonic day (E) 13.5, slightly earlier than p27/p57 DKO embryos. The TKO embryos manifested morphological abnormalities as well as increased rates of cell proliferation and apoptosis in the placenta and lens that were essentially indistinguishable from those of p27/p57 DKO mice. Unexpectedly, the proliferation rate and cell cycle profile of mouse embryonic fibroblasts (MEFs) lacking all three Cip/Kip CKIs did not differ substantially from those of control MEFs. The abundance and kinase activity of CDK2 were markedly increased, whereas CDK4 activity and cyclin D1 abundance were decreased, in both p27/p57 DKO and TKO MEFs during progression from G₀ to S phase compared with those in control MEFs. The extents of the increase in CDK2 activity and the decrease in CDK4 activity and cyclin D1 abundance were greater in TKO MEFs than in p27/p57 DKO MEFs. These results suggest that p27 and p57 play an essential role in mouse development after midgestation, and that p21 plays only an auxiliary role in normal development (although it is thought to be a key player in the response to DNA damage).
Keywords	DNA damage ; apoptosis ; cell differentiation ; cell proliferation ; cyclin-dependent kinase ; embryogenesis ; fibroblasts ; interphase ; mice ; placenta ; proteins
Language	English
Dates of publication	2012-1019
Size	p. 285-292.
Publishing place	Elsevier Inc.
Document type	Article
ZDB-ID	205723-2
ISSN	0006-291X ; 0006-291X
ISSN (online)	0006-291X
ISSN	0006-291X
DOI	10.1016/j.bbrc.2012.09.041
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