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Article ; Online: Analysis of Meiotic Sister Chromatid Cohesion in Caenorhabditis elegans.

Severson, Aaron F

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

2016 Volume 1515, Page(s) 65–95

Abstract: In sexually reproducing organisms, the formation of healthy gametes (sperm and eggs) requires the proper establishment and release of meiotic sister chromatid cohesion (SCC). SCC tethers replicated sisters from their formation in premeiotic S phase until ...

Abstract	In sexually reproducing organisms, the formation of healthy gametes (sperm and eggs) requires the proper establishment and release of meiotic sister chromatid cohesion (SCC). SCC tethers replicated sisters from their formation in premeiotic S phase until the stepwise removal of cohesion in anaphase of meiosis I and II allows the separation of homologs and then sisters. Defects in the establishment or release of meiotic cohesion cause chromosome segregation errors that lead to the formation of aneuploid gametes and inviable embryos. The nematode Caenorhabditis elegans is an attractive model for studies of meiotic sister chromatid cohesion due to its genetic tractability and the excellent cytological properties of the hermaphrodite gonad. Moreover, mutants defective in the establishment or maintenance of meiotic SCC nevertheless produce abundant gametes, allowing analysis of the pattern of chromosome segregation. Here I describe two approaches for analysis of meiotic cohesion in C. elegans. The first approach relies on cytology to detect and quantify defects in SCC. The second approach relies on PCR and restriction digests to identify embryos that inherited an incorrect complement of chromosomes due to aberrant meiotic chromosome segregation. Both approaches are sensitive enough to identify rare errors and precise enough to reveal distinctive phenotypes resulting from mutations that perturb meiotic SCC in different ways. The robust, quantitative nature of these assays should strengthen phenotypic comparisons of different meiotic mutants and enhance the reproducibility of data generated by different investigators.
MeSH term(s)	Anaphase/genetics ; Animals ; Caenorhabditis elegans/genetics ; Cell Cycle Proteins/genetics ; Cell Cycle Proteins/isolation & purification ; Chromatids/genetics ; Chromosomal Proteins, Non-Histone/genetics ; Chromosomal Proteins, Non-Histone/isolation & purification ; Chromosome Segregation/genetics ; Meiosis/genetics ; Molecular Biology/methods ; Sister Chromatid Exchange/genetics ; Cohesins
Chemical Substances	Cell Cycle Proteins ; Chromosomal Proteins, Non-Histone
Language	English
Publishing date	2016-10-28
Publishing country	United States
Document type	Journal Article ; Research Support, N.I.H., Extramural ; Research Support, Non-U.S. Gov't
ISSN	1940-6029
ISSN (online)	1940-6029
DOI	10.1007/978-1-4939-6545-8_5
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Article: Securin Regulates the Spatiotemporal Dynamics of Separase.

Sorensen Turpin, Christopher G / Sloan, Dillon / LaForest, Marian / Klebanow, Lindsey Uehlein / Mitchell, Diana / Severson, Aaron F / Bembenek, Joshua N

bioRxiv : the preprint server for biology

2023

Abstract: Separase is a key regulator of the metaphase to anaphase transition with multiple functions. Separase cleaves cohesin to allow chromosome segregation and localizes to vesicles to promote exocytosis in mid-anaphase. The anaphase promoting complex/ ... ...

Abstract	Separase is a key regulator of the metaphase to anaphase transition with multiple functions. Separase cleaves cohesin to allow chromosome segregation and localizes to vesicles to promote exocytosis in mid-anaphase. The anaphase promoting complex/cyclosome (APC/C) activates separase by ubiquitinating its inhibitory chaperone, securin, triggering its degradation. How this pathway controls the exocytic function of separase has not been investigated. During meiosis I, securin is degraded over several minutes, while separase rapidly relocalizes from kinetochore structures at the spindle and cortex to sites of action on chromosomes and vesicles at anaphase onset. The loss of cohesin coincides with the relocalization of separase to the chromosome midbivalent at anaphase onset. APC/C depletion prevents separase relocalization, while securin depletion causes precocious separase relocalization. Expression of non-degradable securin inhibits chromosome segregation, exocytosis, and separase localization to vesicles but not to the anaphase spindle. We conclude that APC/C mediated securin degradation controls separase localization. This spatiotemporal regulation will impact the effective local concentration of separase for more precise targeting of substrates in anaphase.
Language	English
Publishing date	2023-12-19
Publishing country	United States
Document type	Preprint
DOI	10.1101/2023.12.12.571338
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Article ; Online: Strategies for Efficient Genome Editing Using CRISPR-Cas9.

Farboud, Behnom / Severson, Aaron F / Meyer, Barbara J

Genetics

2018 Volume 211, Issue 2, Page(s) 431–457

Abstract: The targetable DNA endonuclease CRISPR-Cas9 has transformed analysis of biological processes by enabling robust genome editing in model and nonmodel organisms. Although rules directing Cas9 to its target DNA via a guide RNA are straightforward, wide ... ...

Abstract	The targetable DNA endonuclease CRISPR-Cas9 has transformed analysis of biological processes by enabling robust genome editing in model and nonmodel organisms. Although rules directing Cas9 to its target DNA via a guide RNA are straightforward, wide variation occurs in editing efficiency and repair outcomes for both imprecise error-prone repair and precise templated repair. We found that imprecise and precise DNA repair from double-strand breaks (DSBs) is asymmetric, favoring repair in one direction. Using this knowledge, we designed RNA guides and repair templates that increased the frequency of imprecise insertions and deletions and greatly enhanced precise insertion of point mutations in
MeSH term(s)	Animals ; CRISPR-Cas Systems ; Caenorhabditis elegans/genetics ; Gene Editing/methods
Language	English
Publishing date	2018-11-30
Publishing country	United States
Document type	Journal Article ; Research Support, N.I.H., Extramural ; Research Support, Non-U.S. Gov't
ZDB-ID	2167-2
ISSN	1943-2631 ; 0016-6731
ISSN (online)	1943-2631
ISSN	0016-6731
DOI	10.1534/genetics.118.301775
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Article ; Online: Divergent kleisin subunits of cohesin specify mechanisms to tether and release meiotic chromosomes.

Severson, Aaron F / Meyer, Barbara J

eLife

2014 Volume 3, Page(s) e03467

Abstract: We show that multiple, functionally specialized cohesin complexes mediate the establishment and two-step release of sister chromatid cohesion that underlies the production of haploid gametes. In C. elegans, the kleisin subunits REC-8 and COH-3/4 differ ... ...

Abstract	We show that multiple, functionally specialized cohesin complexes mediate the establishment and two-step release of sister chromatid cohesion that underlies the production of haploid gametes. In C. elegans, the kleisin subunits REC-8 and COH-3/4 differ between meiotic cohesins and endow them with distinctive properties that specify how cohesins load onto chromosomes and then trigger and release cohesion. Unlike REC-8 cohesin, COH-3/4 cohesin becomes cohesive through a replication-independent mechanism initiated by the DNA double-stranded breaks that induce crossover recombination. Thus, break-induced cohesion also tethers replicated meiotic chromosomes. Later, recombination stimulates separase-independent removal of REC-8 and COH-3/4 cohesins from reciprocal chromosomal territories flanking the crossover site. This region-specific removal likely underlies the two-step separation of homologs and sisters. Unexpectedly, COH-3/4 performs cohesion-independent functions in synaptonemal complex assembly. This new model for cohesin function diverges from that established in yeast but likely applies directly to plants and mammals, which utilize similar meiotic kleisins.
MeSH term(s)	Animals ; Caenorhabditis elegans/cytology ; Caenorhabditis elegans/metabolism ; Caenorhabditis elegans Proteins/metabolism ; Cell Cycle Proteins/metabolism ; Chromosomal Proteins, Non-Histone/metabolism ; Chromosomes/metabolism ; Crossing Over, Genetic ; DNA Breaks, Double-Stranded ; DNA Replication ; Meiosis ; Protein Subunits/metabolism ; Saccharomyces cerevisiae/cytology ; Saccharomyces cerevisiae/metabolism ; Sister Chromatid Exchange ; Cohesins
Chemical Substances	Caenorhabditis elegans Proteins ; Cell Cycle Proteins ; Chromosomal Proteins, Non-Histone ; Protein Subunits
Language	English
Publishing date	2014-08-29
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.03467
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Article ; Online: Oocyte Meiotic Spindle Assembly and Function.

Severson, Aaron F / von Dassow, George / Bowerman, Bruce

Current topics in developmental biology

2016 Volume 116, Page(s) 65–98

Abstract: Gametogenesis in animal oocytes reduces the diploid genome content of germline precursors to a haploid state in gametes by discarding ¾ of the duplicated chromosomes through a sequence of two meiotic cell divisions called meiosis I and II. The assembly ... ...

Abstract	Gametogenesis in animal oocytes reduces the diploid genome content of germline precursors to a haploid state in gametes by discarding ¾ of the duplicated chromosomes through a sequence of two meiotic cell divisions called meiosis I and II. The assembly of the microtubule-based spindle structure that mediates this reduction in genome content remains poorly understood compared to our knowledge of mitotic spindle assembly and function. In this review, we consider the diversity of oocyte meiotic spindle assembly and structure across animal phylogeny, review recent advances in our understanding of how animal oocytes assemble spindles in the absence of the centriole-based microtubule-organizing centers that dominate mitotic spindle assembly, and discuss different models for how chromosomes are captured and moved to achieve chromosome segregation during oocyte meiotic cell division.
MeSH term(s)	Animals ; Caenorhabditis elegans ; Centrosome/metabolism ; Centrosome/ultrastructure ; Chromosomes/metabolism ; Female ; Kinetochores/physiology ; Meiosis ; Microtubules/metabolism ; Microtubules/ultrastructure ; Oocytes/cytology ; Oocytes/physiology ; Spindle Apparatus/physiology ; Spindle Apparatus/ultrastructure
Language	English
Publishing date	2016-01-23
Publishing country	United States
Document type	Journal Article ; Research Support, N.I.H., Extramural ; Research Support, U.S. Gov't, Non-P.H.S. ; Review
ISSN	1557-8933 ; 0070-2153
ISSN (online)	1557-8933
ISSN	0070-2153
DOI	10.1016/bs.ctdb.2015.11.031
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Article ; Online: Condensin I protects meiotic cohesin from WAPL-1 mediated removal.

Hernandez, Margarita R / Davis, Michael B / Jiang, Jianhao / Brouhard, Elizabeth A / Severson, Aaron F / Csankovszki, Györgyi

PLoS genetics

2018 Volume 14, Issue 5, Page(s) e1007382

Abstract: Condensin complexes are key determinants of higher-order chromatin structure and are required for mitotic and meiotic chromosome compaction and segregation. We identified a new role for condensin in the maintenance of sister chromatid cohesion during C. ... ...

Abstract	Condensin complexes are key determinants of higher-order chromatin structure and are required for mitotic and meiotic chromosome compaction and segregation. We identified a new role for condensin in the maintenance of sister chromatid cohesion during C. elegans meiosis. Using conventional and stimulated emission depletion (STED) microscopy we show that levels of chromosomally-bound cohesin were significantly reduced in dpy-28 mutants, which lack a subunit of condensin I. SYP-1, a component of the synaptonemal complex central region, was also diminished, but no decrease in the axial element protein HTP-3 was observed. Surprisingly, the two key meiotic cohesin complexes of C. elegans were both depleted from meiotic chromosomes following the loss of condensin I, and disrupting condensin I in cohesin mutants increased the frequency of detached sister chromatids. During mitosis and meiosis in many organisms, establishment of cohesion is antagonized by cohesin removal by Wapl, and we found that condensin I binds to C. elegans WAPL-1 and counteracts WAPL-1-dependent cohesin removal. Our data suggest that condensin I opposes WAPL-1 to promote stable binding of cohesin to meiotic chromosomes, thereby ensuring linkages between sister chromatids in early meiosis.
MeSH term(s)	Adenosine Triphosphatases/genetics ; Adenosine Triphosphatases/metabolism ; Animals ; Caenorhabditis elegans/genetics ; Caenorhabditis elegans/metabolism ; Caenorhabditis elegans Proteins/genetics ; Caenorhabditis elegans Proteins/metabolism ; Cell Cycle Proteins/genetics ; Cell Cycle Proteins/metabolism ; Chromatids/genetics ; Chromatids/metabolism ; Chromosomal Proteins, Non-Histone/genetics ; Chromosomal Proteins, Non-Histone/metabolism ; Chromosome Segregation/genetics ; DNA-Binding Proteins/genetics ; DNA-Binding Proteins/metabolism ; In Situ Hybridization, Fluorescence ; Intercellular Signaling Peptides and Proteins/genetics ; Intercellular Signaling Peptides and Proteins/metabolism ; Meiosis/genetics ; Multiprotein Complexes/genetics ; Multiprotein Complexes/metabolism ; Mutation ; Nuclear Proteins/genetics ; Nuclear Proteins/metabolism ; RNA Interference ; Synaptonemal Complex/genetics ; Synaptonemal Complex/metabolism ; Cohesins
Chemical Substances	Caenorhabditis elegans Proteins ; Cell Cycle Proteins ; Chromosomal Proteins, Non-Histone ; DNA-Binding Proteins ; Intercellular Signaling Peptides and Proteins ; Multiprotein Complexes ; Nuclear Proteins ; condensin complexes ; wapl-1 protein, C elegans ; Adenosine Triphosphatases (EC 3.6.1.-)
Language	English
Publishing date	2018-05-16
Publishing country	United States
Document type	Journal Article ; Research Support, N.I.H., Extramural ; 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.1007382
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Article ; Online: Blue light photodynamic therapy with 5-aminolevulinic acid in refractory mycosis fungoides: A prospective, open-label study.

Severson, Kevin J / Cumsky, Helen J L / Brumfiel, Caitlin M / Janeczek, Monica C / Ginos, Brenda F / Kosiorek, Heidi E / Besch-Stokes, Jake / Patel, Meera H / Rule, William G / DiCaudo, David J / Rosenthal, Allison C / Pittelkow, Mark R / Mangold, Aaron R

Journal of the American Academy of Dermatology

2021 Volume 85, Issue 4, Page(s) 969–971

MeSH term(s)	Aminolevulinic Acid/therapeutic use ; Humans ; Mycosis Fungoides/drug therapy ; Photochemotherapy ; Photosensitizing Agents/therapeutic use ; Prospective Studies ; Skin Neoplasms/drug therapy
Chemical Substances	Photosensitizing Agents ; Aminolevulinic Acid (88755TAZ87)
Language	English
Publishing date	2021-01-23
Publishing country	United States
Document type	Letter
ZDB-ID	603641-7
ISSN	1097-6787 ; 0190-9622
ISSN (online)	1097-6787
ISSN	0190-9622
DOI	10.1016/j.jaad.2021.01.053
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Article ; Online: Divergent kleisin subunits of cohesin specify mechanisms to tether and release meiotic chromosomes

Aaron F Severson / Barbara J Meyer

eLife, Vol

2014 Volume 3

Abstract	We show that multiple, functionally specialized cohesin complexes mediate the establishment and two-step release of sister chromatid cohesion that underlies the production of haploid gametes. In C. elegans, the kleisin subunits REC-8 and COH-3/4 differ between meiotic cohesins and endow them with distinctive properties that specify how cohesins load onto chromosomes and then trigger and release cohesion. Unlike REC-8 cohesin, COH-3/4 cohesin becomes cohesive through a replication-independent mechanism initiated by the DNA double-stranded breaks that induce crossover recombination. Thus, break-induced cohesion also tethers replicated meiotic chromosomes. Later, recombination stimulates separase-independent removal of REC-8 and COH-3/4 cohesins from reciprocal chromosomal territories flanking the crossover site. This region-specific removal likely underlies the two-step separation of homologs and sisters. Unexpectedly, COH-3/4 performs cohesion-independent functions in synaptonemal complex assembly. This new model for cohesin function diverges from that established in yeast but likely applies directly to plants and mammals, which utilize similar meiotic kleisins.
Keywords	cohesin ; sister chromatid cohesion ; meiosis ; gametogenesis ; kleisin ; aneuploidy ; Medicine ; R ; Science ; Q ; Biology (General) ; QH301-705.5
Subject code	570
Language	English
Publishing date	2014-08-01T00:00:00Z
Publisher	eLife Sciences Publications Ltd
Document type	Article ; Online
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Article ; Online: Condensin and cohesin complexity: the expanding repertoire of functions.

Wood, Andrew J / Severson, Aaron F / Meyer, Barbara J

Nature reviews. Genetics

2010 Volume 11, Issue 6, Page(s) 391–404

Abstract: Condensin and cohesin complexes act in diverse nuclear processes in addition to their widely known roles in chromosome compaction and sister chromatid cohesion. Recent work has elucidated the contribution of condensin and cohesin to interphase genome ... ...

Abstract	Condensin and cohesin complexes act in diverse nuclear processes in addition to their widely known roles in chromosome compaction and sister chromatid cohesion. Recent work has elucidated the contribution of condensin and cohesin to interphase genome organization, control of gene expression, metazoan development and meiosis. Despite these wide-ranging functions, several themes have come to light: both complexes establish higher-order chromosome structure by inhibiting or promoting interactions between distant genomic regions, both complexes influence the chromosomal association of other proteins, and both complexes achieve functional specialization by swapping homologous subunits. Emerging data are expanding the range of processes in which condensin and cohesin are known to participate and are enhancing our knowledge of how chromosome architecture is regulated to influence numerous cellular functions.
MeSH term(s)	Adenosine Triphosphatases/metabolism ; Adenosine Triphosphatases/physiology ; Animals ; Cell Cycle Proteins/metabolism ; Cell Cycle Proteins/physiology ; Chromatin Assembly and Disassembly/physiology ; Chromosomal Proteins, Non-Histone/metabolism ; Chromosomal Proteins, Non-Histone/physiology ; DNA-Binding Proteins/metabolism ; DNA-Binding Proteins/physiology ; Gene Expression Regulation/physiology ; Genome/physiology ; Humans ; Meiosis/genetics ; Meiosis/physiology ; Models, Biological ; Multiprotein Complexes/metabolism ; Multiprotein Complexes/physiology ; Cohesins
Chemical Substances	Cell Cycle Proteins ; Chromosomal Proteins, Non-Histone ; DNA-Binding Proteins ; Multiprotein Complexes ; condensin complexes ; Adenosine Triphosphatases (EC 3.6.1.-)
Language	English
Publishing date	2010-05-05
Publishing country	England
Document type	Journal Article ; Research Support, N.I.H., Extramural ; Research Support, Non-U.S. Gov't ; Review
ZDB-ID	2035157-4
ISSN	1471-0064 ; 1471-0056
ISSN (online)	1471-0064
ISSN	1471-0056
DOI	10.1038/nrg2794
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Zs.A 5474: 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: Myosin and the PAR proteins polarize microfilament-dependent forces that shape and position mitotic spindles in Caenorhabditis elegans.

Severson, Aaron F / Bowerman, Bruce

The Journal of cell biology

2003 Volume 161, Issue 1, Page(s) 21–26

Abstract: In Caenorhabditis elegans, the partitioning proteins (PARs), microfilaments (MFs), dynein, dynactin, and a nonmuscle myosin II all localize to the cortex of early embryonic cells. Both the PARs and the actomyosin cytoskeleton are required to polarize the ...

Abstract	In Caenorhabditis elegans, the partitioning proteins (PARs), microfilaments (MFs), dynein, dynactin, and a nonmuscle myosin II all localize to the cortex of early embryonic cells. Both the PARs and the actomyosin cytoskeleton are required to polarize the anterior-posterior (a-p) body axis in one-cell zygotes, but it remains unknown how MFs influence embryonic polarity. Here we show that MFs are required for the cortical localization of PAR-2 and PAR-3. Furthermore, we show that PAR polarity regulates MF-dependent cortical forces applied to astral microtubules (MTs). These forces, which appear to be mediated by dynein and dynactin, produce changes in the shape and orientation of mitotic spindles. Unlike MFs, dynein, and dynactin, myosin II is not required for the production of these forces. Instead, myosin influences embryonic polarity by limiting PAR-3 to the anterior cortex. This in turn produces asymmetry in the forces applied to MTs at each pole and allows PAR-2 to accumulate in the posterior cortex of a one-cell zygote and maintain asymmetry.
MeSH term(s)	Actin Cytoskeleton/drug effects ; Actin Cytoskeleton/metabolism ; Actin Cytoskeleton/ultrastructure ; Animals ; Bridged Bicyclo Compounds, Heterocyclic/pharmacology ; Caenorhabditis elegans/embryology ; Caenorhabditis elegans/metabolism ; Caenorhabditis elegans/ultrastructure ; Caenorhabditis elegans Proteins/genetics ; Caenorhabditis elegans Proteins/metabolism ; Cell Compartmentation/drug effects ; Cell Compartmentation/genetics ; Cell Polarity/drug effects ; Cell Polarity/genetics ; Centrosome/metabolism ; Centrosome/ultrastructure ; Contractile Proteins ; Dynactin Complex ; Dyneins/genetics ; Dyneins/metabolism ; Gene Expression Regulation, Developmental/drug effects ; Gene Expression Regulation, Developmental/genetics ; Microfilament Proteins/deficiency ; Microfilament Proteins/genetics ; Microtubule-Associated Proteins/genetics ; Microtubule-Associated Proteins/metabolism ; Mitosis/drug effects ; Mitosis/physiology ; Mutation/genetics ; Myosin Type II/deficiency ; Myosin Type II/genetics ; Nocodazole/pharmacology ; Profilins ; Protein-Serine-Threonine Kinases ; Spindle Apparatus/drug effects ; Spindle Apparatus/metabolism ; Spindle Apparatus/ultrastructure ; Thiazoles/pharmacology ; Thiazolidines ; Zygote/drug effects ; Zygote/metabolism ; Zygote/ultrastructure
Chemical Substances	Bridged Bicyclo Compounds, Heterocyclic ; Caenorhabditis elegans Proteins ; Contractile Proteins ; Dynactin Complex ; Microfilament Proteins ; Microtubule-Associated Proteins ; Profilins ; Thiazoles ; Thiazolidines ; par-2 protein, C elegans ; PAR-3 protein, C elegans (EC 2.7.11.1) ; Protein-Serine-Threonine Kinases (EC 2.7.11.1) ; Myosin Type II (EC 3.6.1.-) ; Dyneins (EC 3.6.4.2) ; Nocodazole (SH1WY3R615) ; latrunculin A (SRQ9WWM084)
Language	English
Publishing date	2003-04-14
Publishing country	United States
Document type	Journal Article ; Research Support, U.S. Gov't, P.H.S.
ZDB-ID	218154-x
ISSN	1540-8140 ; 0021-9525
ISSN (online)	1540-8140
ISSN	0021-9525
DOI	10.1083/jcb.200210171
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