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Article ; Online: Correction to: Live Imaging and Analysis of Cilia and Cell Cycle Dynamics with the Arl13bCerulean-Fucci2a Biosensor and Fucci Tools.

Van Kerckvoorde, Melinda / Ford, Matthew J / Yeyati, Patricia L / Mill, Pleasantine / Mort, Richard L

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

2022 Volume 2329, Page(s) C3

Language	English
Publishing date	2022-01-11
Publishing country	United States
Document type	Journal Article ; Published Erratum
ISSN	1940-6029
ISSN (online)	1940-6029
DOI	10.1007/978-1-0716-1538-6_25
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Article ; Online: Live Imaging and Analysis of Cilia and Cell Cycle Dynamics with the Arl13bCerulean-Fucci2a Biosensor and Fucci Tools.

Van Kerckvoorde, Melinda / Ford, Matthew J / Yeyati, Patricia L / Mill, Pleasantine / Mort, Richard L

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

2021 Volume 2329, Page(s) 291–309

Abstract: The cell and cilia cycles are inextricably linked through the dual functions of the centrioles at both the basal body of cilia and at mitotic centrosomes. How cilia assembly and disassembly, either through slow resorption or rapid deciliation, are ... ...

Abstract	The cell and cilia cycles are inextricably linked through the dual functions of the centrioles at both the basal body of cilia and at mitotic centrosomes. How cilia assembly and disassembly, either through slow resorption or rapid deciliation, are coordinated with cell cycle progression remains unclear in many cell types and developmental paradigms. Moreover, little is known about how additional cilia parameters including changes in ciliary length or frequency of distal tip shedding change with cell cycle stage. In order to explore these questions, we have developed the Arl13bCerulean-Fucci2a tricistronic cilia and cell cycle biosensor (Ford et al., Dev Cell 47:509-523.e7, 2018). This reporter allowed us to document the heterogeneity in ciliary behaviors during the cell cycle at a population level. Without the need for external stimuli, it revealed that in several cell types and in the developing embryo cilia persist beyond the G1/S checkpoint. Here, we describe the generation of stable cell lines expressing Arl13bCerulean-Fucci2a and open-source software to aid morphometric profiling of the primary cilium with cell cycle phases, including changes in cilium length. This resource will allow the investigation of multiple morphometric questions relating to cilia and cell cycle biology.
MeSH term(s)	3T3 Cells ; Animals ; Biosensing Techniques/methods ; Cell Cycle ; Cell Cycle Proteins/chemistry ; Cell Cycle Proteins/metabolism ; Cilia/metabolism ; Geminin/chemistry ; Geminin/metabolism ; Humans ; Luminescent Proteins/metabolism ; Mice ; Microscopy, Confocal ; Protein Domains ; Recombinant Fusion Proteins/chemistry ; Recombinant Fusion Proteins/metabolism ; Red Fluorescent Protein
Chemical Substances	CDT1 protein, human ; Cell Cycle Proteins ; GMNN protein, human ; Geminin ; Luminescent Proteins ; Recombinant Fusion Proteins
Language	English
Publishing date	2021-06-02
Publishing country	United States
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ISSN	1940-6029
ISSN (online)	1940-6029
DOI	10.1007/978-1-0716-1538-6_21
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Article ; Online: Nucleo-cytoplasmic shuttling of splicing factor SRSF1 is required for development and cilia function.

Haward, Fiona / Maslon, Magdalena M / Yeyati, Patricia L / Bellora, Nicolas / Hansen, Jan N / Aitken, Stuart / Lawson, Jennifer / von Kriegsheim, Alex / Wachten, Dagmar / Mill, Pleasantine / Adams, Ian R / Caceres, Javier F

eLife

2021 Volume 10

Abstract: Shuttling RNA-binding proteins coordinate nuclear and cytoplasmic steps of gene expression. The SR family proteins regulate RNA splicing in the nucleus and a subset of them, including SRSF1, shuttles between the nucleus and cytoplasm affecting post- ... ...

Abstract	Shuttling RNA-binding proteins coordinate nuclear and cytoplasmic steps of gene expression. The SR family proteins regulate RNA splicing in the nucleus and a subset of them, including SRSF1, shuttles between the nucleus and cytoplasm affecting post-splicing processes. However, the physiological significance of this remains unclear. Here, we used genome editing to knock-in a nuclear retention signal (NRS) in
MeSH term(s)	Animals ; Cell Nucleus/metabolism ; Cilia/metabolism ; Cytoplasm/metabolism ; Male ; Mice ; Serine-Arginine Splicing Factors/genetics ; Serine-Arginine Splicing Factors/metabolism
Chemical Substances	Srsf1 protein, mouse ; Serine-Arginine Splicing Factors (170974-22-8)
Language	English
Publishing date	2021-08-02
Publishing country	England
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	2687154-3
ISSN	2050-084X ; 2050-084X
ISSN (online)	2050-084X
ISSN	2050-084X
DOI	10.7554/eLife.65104
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Article ; Online: Centriolar satellites expedite mother centriole remodeling to promote ciliogenesis.

Hall, Emma A / Kumar, Dhivya / Prosser, Suzanna L / Yeyati, Patricia L / Herranz-Pérez, Vicente / García-Verdugo, Jose Manuel / Rose, Lorraine / McKie, Lisa / Dodd, Daniel O / Tennant, Peter A / Megaw, Roly / Murphy, Laura C / Ferreira, Marisa F / Grimes, Graeme / Williams, Lucy / Quidwai, Tooba / Pelletier, Laurence / Reiter, Jeremy F / Mill, Pleasantine

eLife

2023 Volume 12

Abstract: Centrosomes are orbited by centriolar satellites, dynamic multiprotein assemblies nucleated by Pericentriolar material 1 (PCM1). To study the requirement for centriolar satellites, we generated mice lacking PCM1, a crucial component of satellites. ...

Abstract	Centrosomes are orbited by centriolar satellites, dynamic multiprotein assemblies nucleated by Pericentriolar material 1 (PCM1). To study the requirement for centriolar satellites, we generated mice lacking PCM1, a crucial component of satellites.
MeSH term(s)	Animals ; Female ; Humans ; Mice ; Cell Cycle Proteins/genetics ; Cell Cycle Proteins/metabolism ; Centrioles/metabolism ; Centrosome/metabolism ; Cilia/metabolism ; Cytoskeletal Proteins/metabolism
Chemical Substances	Cell Cycle Proteins ; Cytoskeletal Proteins ; Pcm1 protein, mouse
Language	English
Publishing date	2023-02-15
Publishing country	England
Document type	Journal Article ; Research Support, N.I.H., Extramural ; Research Support, Non-U.S. Gov't
ZDB-ID	2687154-3
ISSN	2050-084X ; 2050-084X
ISSN (online)	2050-084X
ISSN	2050-084X
DOI	10.7554/eLife.79299
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Article: Incapacitating the evolutionary capacitor: Hsp90 modulation of disease.

Yeyati, Patricia L / van Heyningen, Veronica

Current opinion in genetics & development

2008 Volume 18, Issue 3, Page(s) 264–272

Abstract: The nature-nurture argument surrounding the mechanisms of disease causation cannot be resolved, as the roles of genes and environment are inextricably entwined. Environmental fluctuation is clearly a major modifier of phenotype, as well as a promoter of ... ...

Abstract	The nature-nurture argument surrounding the mechanisms of disease causation cannot be resolved, as the roles of genes and environment are inextricably entwined. Environmental fluctuation is clearly a major modifier of phenotype, as well as a promoter of evolutionary change. Both types of variability can be mediated by the stress response pathway, with the Hsp90 chaperone family as key components. Hsp90 has been hailed as a capacitor for evolutionary change, because partial inhibition of its functions can uncover cryptic mutations, leading to unexpected phenotypes that, although generally deleterious, will under rare new environmental conditions provide improved survival to the carrier of that variant. There is, therefore, a strong environmentally elicited link between the capacity to reveal hidden variation as human disease phenotype and as novel morphological forms for evolutionary selection.
MeSH term(s)	Animals ; Disease/genetics ; Evolution, Molecular ; Gene Dosage/physiology ; Gene Expression Regulation, Developmental ; HSP90 Heat-Shock Proteins/genetics ; HSP90 Heat-Shock Proteins/physiology ; Humans ; Inheritance Patterns/physiology ; Models, Biological ; Phenotype ; Plants/genetics ; Selection, Genetic ; Vertebrates/genetics
Chemical Substances	HSP90 Heat-Shock Proteins
Language	English
Publishing date	2008-08-28
Publishing country	England
Document type	Journal Article ; Review
ZDB-ID	1077312-5
ISSN	1879-0380 ; 0959-437X
ISSN (online)	1879-0380
ISSN	0959-437X
DOI	10.1016/j.gde.2008.07.004
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Article: Mechanisms of non-Mendelian inheritance in genetic disease.

Van Heyningen, Veronica / Yeyati, Patricia L

Human molecular genetics

2004 Volume 13 Spec No 2, Page(s) R225–33

Abstract: Single gene disorders with Mendelian inheritance patterns have contributed greatly to the identification of genes and pathways implicated in genetic disease. In these cases, molecular analysis predicts disease status relatively directly. However, there ... ...

Abstract	Single gene disorders with Mendelian inheritance patterns have contributed greatly to the identification of genes and pathways implicated in genetic disease. In these cases, molecular analysis predicts disease status relatively directly. However, there are many abnormalities which show familial recurrence and have a clear genetic component, but do not show regular Mendelian segregation patterns. Defining the causative gene for non-Mendelian diseases is more difficult, and even when the underlying gene is known, there is uncertainty for prenatal prediction. However, detailed examination of the different mechanisms that underlie non-Mendelian segregation provides insight into the types of interaction that regulate more complex disease genetics.
MeSH term(s)	Genetic Diseases, Inborn/genetics ; Genetic Linkage ; Genomic Imprinting ; Humans ; Inheritance Patterns/genetics
Language	English
Publishing date	2004-09-09
Publishing country	England
Document type	Journal Article ; Review
ZDB-ID	1108742-0
ISSN	1460-2083 ; 0964-6906
ISSN (online)	1460-2083
ISSN	0964-6906
DOI	10.1093/hmg/ddh254
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Article ; Online: Hsp90 selectively modulates phenotype in vertebrate development.

Yeyati, Patricia L / Bancewicz, Ruth M / Maule, John / van Heyningen, Veronica

PLoS genetics

2007 Volume 3, Issue 3, Page(s) e43

Abstract: Compromised heat shock protein 90 (Hsp90) function reveals cryptic phenotypes in flies and plants. These observations were interpreted to suggest that this molecular stress-response chaperone has a capacity to buffer underlying genetic variation. ... ...

Abstract	Compromised heat shock protein 90 (Hsp90) function reveals cryptic phenotypes in flies and plants. These observations were interpreted to suggest that this molecular stress-response chaperone has a capacity to buffer underlying genetic variation. Conversely, the protective role of Hsp90 could account for the variable penetrance or severity of some heritable developmental malformations in vertebrates. Using zebrafish as a model, we defined Hsp90 inhibitor levels that did not induce a heat shock response or perturb phenotype in wild-type strains. Under these conditions the severity of the recessive eye phenotype in sunrise, caused by a pax6b mutation, was increased, while in dreumes, caused by a sufu mutation, it was decreased. In another strain, a previously unobserved spectrum of severe structural eye malformations, reminiscent of anophthalmia, microphthalmia, and nanophthalmia complex in humans, was uncovered by this limited inhibition of Hsp90 function. Inbreeding of offspring from selected unaffected carrier parents led to significantly elevated malformation frequencies and revealed the oligogenic nature of this phenotype. Unlike in Drosophila, Hsp90 inhibition can decrease developmental stability in zebrafish, as indicated by increased asymmetric presentation of anophthalmia, microphthalmia, and nanophthalmia and sunrise phenotypes. Analysis of the sunrise pax6b mutation suggests a molecular mechanism for the buffering of mutations by Hsp90. The zebrafish studies imply that mild perturbation of Hsp90 function at critical developmental stages may underpin the variable penetrance and expressivity of many developmental anomalies where the interaction between genotype and environment plays a major role.
MeSH term(s)	Animals ; Animals, Genetically Modified ; Benzoquinones/pharmacology ; Dose-Response Relationship, Drug ; Embryo, Nonmammalian ; Eye Abnormalities/genetics ; Female ; HSP90 Heat-Shock Proteins/antagonists & inhibitors ; HSP90 Heat-Shock Proteins/physiology ; Humans ; Inheritance Patterns ; Lactams, Macrocyclic/pharmacology ; Male ; Models, Biological ; Pedigree ; Phenotype ; Time Factors ; Vertebrates/embryology ; Vertebrates/growth & development ; Zebrafish/embryology
Chemical Substances	Benzoquinones ; HSP90 Heat-Shock Proteins ; Lactams, Macrocyclic ; geldanamycin (Z3K3VJ16KU)
Language	English
Publishing date	2007-02-08
Publishing country	United States
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	2186725-2
ISSN	1553-7404 ; 1553-7390
ISSN (online)	1553-7404
ISSN	1553-7390
DOI	10.1371/journal.pgen.0030043
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Article ; Online: ZMYND10 functions in a chaperone relay during axonemal dynein assembly.

Mali, Girish R / Yeyati, Patricia L / Mizuno, Seiya / Dodd, Daniel O / Tennant, Peter A / Keighren, Margaret A / Zur Lage, Petra / Shoemark, Amelia / Garcia-Munoz, Amaya / Shimada, Atsuko / Takeda, Hiroyuki / Edlich, Frank / Takahashi, Satoru / von Kreigsheim, Alex / Jarman, Andrew P / Mill, Pleasantine

eLife

2018 Volume 7

Abstract: Molecular chaperones promote the folding and macromolecular assembly of a diverse set of 'client' proteins. How ubiquitous chaperone machineries direct their activities towards specific sets of substrates is unclear. Through the use of mouse genetics, ... ...

Abstract	Molecular chaperones promote the folding and macromolecular assembly of a diverse set of 'client' proteins. How ubiquitous chaperone machineries direct their activities towards specific sets of substrates is unclear. Through the use of mouse genetics, imaging and quantitative proteomics we uncover that ZMYND10 is a novel co-chaperone that confers specificity for the FKBP8-HSP90 chaperone complex towards axonemal dynein clients required for cilia motility. Loss of ZMYND10 perturbs the chaperoning of axonemal dynein heavy chains, triggering broader degradation of dynein motor subunits. We show that pharmacological inhibition of FKBP8 phenocopies dynein motor instability associated with the loss of ZMYND10 in airway cells and that human disease-causing variants of ZMYND10 disrupt its ability to act as an FKBP8-HSP90 co-chaperone. Our study indicates that primary ciliary dyskinesia (PCD), caused by mutations in dynein assembly factors disrupting cytoplasmic pre-assembly of axonemal dynein motors, should be considered a cell-type specific protein-misfolding disease.
MeSH term(s)	Animals ; Animals, Newborn ; Axoneme/metabolism ; Axoneme/ultrastructure ; Base Sequence ; Brain/cytology ; Brain/metabolism ; Cell Line ; Cilia/metabolism ; Cilia/ultrastructure ; Cytoskeletal Proteins ; DNA-Binding Proteins/genetics ; DNA-Binding Proteins/metabolism ; Dyneins/chemistry ; Dyneins/genetics ; Dyneins/metabolism ; Epithelial Cells/cytology ; Epithelial Cells/metabolism ; Gene Expression Regulation ; HEK293 Cells ; HSP90 Heat-Shock Proteins/genetics ; HSP90 Heat-Shock Proteins/metabolism ; Humans ; Mice ; Mice, Inbred C57BL ; Mice, Transgenic ; Molecular Chaperones/genetics ; Molecular Chaperones/metabolism ; Primary Cell Culture ; Tacrolimus Binding Proteins/genetics ; Tacrolimus Binding Proteins/metabolism ; Trachea/cytology ; Trachea/metabolism
Chemical Substances	Cytoskeletal Proteins ; DNA-Binding Proteins ; Fkbp8 protein, mouse ; HSP90 Heat-Shock Proteins ; Molecular Chaperones ; ZMYND10 protein, mouse ; Dyneins (EC 3.6.4.2) ; Tacrolimus Binding Proteins (EC 5.2.1.-)
Language	English
Publishing date	2018-06-19
Publishing country	England
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	2687154-3
ISSN	2050-084X ; 2050-084X
ISSN (online)	2050-084X
ISSN	2050-084X
DOI	10.7554/eLife.34389
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Article ; Online: A Cell/Cilia Cycle Biosensor for Single-Cell Kinetics Reveals Persistence of Cilia after G1/S Transition Is a General Property in Cells and Mice.

Ford, Matthew J / Yeyati, Patricia L / Mali, Girish R / Keighren, Margaret A / Waddell, Scott H / Mjoseng, Heidi K / Douglas, Adam T / Hall, Emma A / Sakaue-Sawano, Asako / Miyawaki, Atsushi / Meehan, Richard R / Boulter, Luke / Jackson, Ian J / Mill, Pleasantine / Mort, Richard L

Developmental cell

2018 Volume 47, Issue 4, Page(s) 509–523.e5

Abstract: The cilia and cell cycles are inextricably linked. Centrioles in the basal body of cilia nucleate the ciliary axoneme and sequester pericentriolar matrix (PCM) at the centrosome to organize the mitotic spindle. Cilia themselves respond to growth signals, ...

Abstract	The cilia and cell cycles are inextricably linked. Centrioles in the basal body of cilia nucleate the ciliary axoneme and sequester pericentriolar matrix (PCM) at the centrosome to organize the mitotic spindle. Cilia themselves respond to growth signals, prompting cilia resorption and cell cycle re-entry. We describe a fluorescent cilia and cell cycle biosensor allowing live imaging of cell cycle progression and cilia assembly and disassembly kinetics in cells and inducible mice. We define assembly and disassembly in relation to cell cycle stage with single-cell resolution and explore the intercellular heterogeneity in cilia kinetics. In all cells and tissues analyzed, we observed cilia that persist through the G1/S transition and into S/G2/M-phase. We conclude that persistence of cilia after the G1/S transition is a general property. This resource will shed light at an individual cell level on the interplay between the cilia and cell cycles in development, regeneration, and disease.
MeSH term(s)	Animals ; Basal Bodies/metabolism ; Biosensing Techniques/methods ; Cell Cycle/physiology ; Cell Cycle Proteins/metabolism ; Centrioles/metabolism ; Centrosome/metabolism ; Cilia/metabolism ; Kinetics ; Mice ; Microtubules/metabolism
Chemical Substances	Cell Cycle Proteins
Language	English
Publishing date	2018-08-15
Publishing country	United States
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	2054967-2
ISSN	1878-1551 ; 1534-5807
ISSN (online)	1878-1551
ISSN	1534-5807
DOI	10.1016/j.devcel.2018.10.027
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Zs.A 5742: 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 ; Online: Ciliopathy patient variants reveal organelle-specific functions for TUBB4B in axonemal microtubules.

Dodd, Daniel O / Mechaussier, Sabrina / Yeyati, Patricia L / McPhie, Fraser / Anderson, Jacob R / Khoo, Chen Jing / Shoemark, Amelia / Gupta, Deepesh K / Attard, Thomas / Zariwala, Maimoona A / Legendre, Marie / Bracht, Diana / Wallmeier, Julia / Gui, Miao / Fassad, Mahmoud R / Parry, David A / Tennant, Peter A / Meynert, Alison / Wheway, Gabrielle /

Fares-Taie, Lucas / Black, Holly A / Mitri-Frangieh, Rana / Faucon, Catherine / Kaplan, Josseline / Patel, Mitali / McKie, Lisa / Megaw, Roly / Gatsogiannis, Christos / Mohamed, Mai A / Aitken, Stuart / Gautier, Philippe / Reinholt, Finn R / Hirst, Robert A / O'Callaghan, Chris / Heimdal, Ketil / Bottier, Mathieu / Escudier, Estelle / Crowley, Suzanne / Descartes, Maria / Jabs, Ethylin W / Kenia, Priti / Amiel, Jeanne / Bacci, Giacomo Maria / Calogero, Claudia / Palazzo, Viviana / Tiberi, Lucia / Blümlein, Ulrike / Rogers, Andrew / Wambach, Jennifer A / Wegner, Daniel J / Fulton, Anne B / Kenna, Margaret / Rosenfeld, Margaret / Holm, Ingrid A / Quigley, Alan / Hall, Emma A / Murphy, Laura C / Cassidy, Diane M / von Kriegsheim, Alex / Papon, Jean-François / Pasquier, Laurent / Murris, Marlène S / Chalmers, James D / Hogg, Claire / Macleod, Kenneth A / Urquhart, Don S / Unger, Stefan / Aitman, Timothy J / Amselem, Serge / Leigh, Margaret W / Knowles, Michael R / Omran, Heymut / Mitchison, Hannah M / Brown, Alan / Marsh, Joseph A / Welburn, Julie P I / Ti, Shih-Chieh / Horani, Amjad / Rozet, Jean-Michel / Perrault, Isabelle / Mill, Pleasantine

Science (New York, N.Y.)

2024 Volume 384, Issue 6694, Page(s) eadf5489

Abstract: Tubulin, one of the most abundant cytoskeletal building blocks, has numerous isotypes in metazoans encoded by different conserved genes. Whether these distinct isotypes form cell type- and context-specific microtubule structures is poorly understood. ... ...

Abstract	Tubulin, one of the most abundant cytoskeletal building blocks, has numerous isotypes in metazoans encoded by different conserved genes. Whether these distinct isotypes form cell type- and context-specific microtubule structures is poorly understood. Based on a cohort of 12 patients with primary ciliary dyskinesia as well as mouse mutants, we identified and characterized variants in the
MeSH term(s)	Animals ; Humans ; Mice ; Axoneme/metabolism ; Centrioles/metabolism ; Cilia/metabolism ; Ciliary Motility Disorders/genetics ; Ciliary Motility Disorders/metabolism ; Mutation ; Protein Isoforms/genetics ; Protein Isoforms/metabolism ; Tubulin/genetics ; Tubulin/metabolism ; Male ; Female ; Mice, Knockout
Chemical Substances	Protein Isoforms ; Tubulin ; TUBB4B protein, human
Language	English
Publishing date	2024-04-26
Publishing country	United States
Document type	Journal Article ; Research Support, Non-U.S. Gov't ; Research Support, N.I.H., Extramural
ZDB-ID	128410-1
ISSN	1095-9203 ; 0036-8075
ISSN (online)	1095-9203
ISSN	0036-8075
DOI	10.1126/science.adf5489
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