Dorota Wloga

Details der Publikationsliste

Zeitraum

2006 - 2009

Anzahl

22

Co-Autoren

O-GlcNAc modifications regulate cell survival and epiboly during zebrafish development (2009)

Webster, Danielle M, Teo, Chin, Sun, Yuhua, Wloga, Dorota, Gay, Steven, Klonowski, Kimberly D, ...

Abstract Background The post-translational addition of the monosaccharide O-linked β- N -acetylglucosamine (O-GlcNAc) regulates the activity of a wide variety of nuclear and cytoplasmic proteins....

Evolutionary divergence of enzymatic mechanisms for posttranslational polyglycylation. (2009)

Rogowski, Krzysztof, Juge, François, Van Dijk, Juliette, Wloga, Dorota, Strub, Jean-Marc, Levilliers, Nicolette, ...

Polyglycylation is a posttranslational modification that generates glycine side chains on proteins. Here we identify a family of evolutionarily conserved glycine ligases that modify tubulin using...

Evolutionary divergence of enzymatic mechanisms for posttranslational polyglycylation. (2009)

Rogowski, Krzysztof, Juge, François, Van Dijk, Juliette, Wloga, Dorota, Strub, Jean-Marc, Levilliers, Nicolette, ...

Polyglycylation is a posttranslational modification that generates glycine side chains on proteins. Here we identify a family of evolutionarily conserved glycine ligases that modify tubulin using...

Evolutionary divergence of enzymatic mechanisms for posttranslational polyglycylation. (2009)

Rogowski, Krzysztof, Juge, François, Van Dijk, Juliette, Wloga, Dorota, Strub, Jean-Marc, Levilliers, Nicolette, ...

Polyglycylation is a posttranslational modification that generates glycine side chains on proteins. Here we identify a family of evolutionarily conserved glycine ligases that modify tubulin using...

Evolutionary divergence of enzymatic mechanisms for posttranslational polyglycylation. (2009)

Rogowski, Krzysztof, Juge, François, Van Dijk, Juliette, Wloga, Dorota, Strub, Jean-Marc, Levilliers, Nicolette, ...

Polyglycylation is a posttranslational modification that generates glycine side chains on proteins. Here we identify a family of evolutionarily conserved glycine ligases that modify tubulin using...

Macronuclear genome sequence of the ciliate Tetrahymena thermophila, a model eukaryote. (2006)

Eisen, Jonathan A, Coyne, Robert S, Wu, Martin, Wu, Dongying, Thiagarajan, Mathangi, Wortman, Jennifer R, ...

The ciliate Tetrahymena thermophila is a model organism for molecular and cellular biology. Like other ciliates, this species has separate germline and soma functions that are embodied by distinct...

Macronuclear Genome Sequence of the Ciliate Tetrahymena thermophila, a Model Eukaryote (2006)

Eisen, Jonathan A, Coyne, Robert S, Wu, Martin, Wu, Dongying, Thiagarajan, Mathangi, Wortman, Jennifer R, ...

The ciliate Tetrahymena thermophila is a model organism for molecular and cellular biology. Like other ciliates, this species has separate germline and soma functions that are embodied by distinct...

Macronuclear Genome Sequence of the Ciliate Tetrahymena thermophila, a Model Eukaryote (2006)

Jonathan A. Eisen, Robert S. Coyne, Martin Wu, Dongying Wu, Mathangi Thiagarajan, Jennifer R. Wortman, ...

The ciliate Tetrahymena thermophila is a model organism for molecular and cellular biology. Like other ciliates, this species has separate germline and soma functions that are embodied by distinct...

Macronuclear Genome Sequence of the Ciliate Tetrahymena thermophila, a Model Eukaryote (2006)

Eisen, Jonathan A., Coyne, Robert S., Wu, Martin, Wu, Dongying, Thiagarajan, Mathangi, Wortman, Jennifer R., ...

The ciliate Tetrahymena thermophila is a model organism for molecular and cellular biology. Like other ciliates, this species has separate germline and soma functions that are embodied by distinct...

Macronuclear Genome Sequence of the Ciliate Tetrahymena thermophila, a Model Eukaryote (2006)

Eisen, Jonathan A., Coyne, Robert S., Wu, Martin, Wu, Dongying, Thiagarajan, Mathangi, Wortman, Jennifer R., ...

The ciliate Tetrahymena thermophila is a model organism for molecular and cellular biology. Like other ciliates, this species has separate germline and soma functions that are embodied by distinct...

Cell Context-specific Effects of the β-Tubulin Glycylation Domain on Assembly and Size of Microtubular Organelles

Thazhath, Rupal, Jerka-Dziadosz, Maria, Duan, Jianming, Wloga, Dorota, Gorovsky, Martin A., Frankel, Joseph, ...

Tubulin glycylation is a posttranslational modification found in cells with cilia or flagella. The ciliate Tetrahymena has glycylation on ciliary and cortical microtubules. We showed previously that...

Metallothionein Gene from Tetrahymena thermophila with a Copper-Inducible-Repressible Promoter

Boldrin, Francesco, Santovito, Gianfranco, Gaertig, Jacek, Wloga, Dorota, Cassidy-Hanley, Donna, Clark, Theodore G., ...

We describe a novel metallothionein gene from Tetrahymena thermophila that has a strong copper-inducible promoter. This promoter can be turned on and off rapidly, making it a useful system for...

Members of the NIMA-related Kinase Family Promote Disassembly of Cilia by Multiple Mechanisms

Wloga, Dorota, Camba, Amy, Rogowski, Krzysztof, Manning, Gerard, Jerka-Dziadosz, Maria, Gaertig, Jacek

The genome of Tetrahymena thermophila contains 39 loci encoding NIMA-related kinases (NRKs), an extraordinarily large number for a unicellular organism. Evolutionary analyses grouped these sequences...

Macronuclear Genome Sequence of the Ciliate Tetrahymena thermophila, a Model Eukaryote

Eisen, Jonathan A, Coyne, Robert S, Wu, Martin, Wu, Dongying, Thiagarajan, Mathangi, Wortman, Jennifer R, ...

The ciliate Tetrahymena thermophila is a model organism for molecular and cellular biology. Like other ciliates, this species has separate germline and soma functions that are embodied by distinct...

Cell Context-specific Effects of the β-Tubulin Glycylation Domain on Assembly and Size of Microtubular Organelles

Thazhath, Rupal, Jerka-Dziadosz, Maria, Duan, Jianming, Wloga, Dorota, Gorovsky, Martin A., Frankel, Joseph, ...

Tubulin glycylation is a posttranslational modification found in cells with cilia or flagella. The ciliate Tetrahymena has glycylation on ciliary and cortical microtubules. We showed previously that...

Metallothionein Gene from Tetrahymena thermophila with a Copper-Inducible-Repressible Promoter

Boldrin, Francesco, Santovito, Gianfranco, Gaertig, Jacek, Wloga, Dorota, Cassidy-Hanley, Donna, Clark, Theodore G., ...

We describe a novel metallothionein gene from Tetrahymena thermophila that has a strong copper-inducible promoter. This promoter can be turned on and off rapidly, making it a useful system for...

Members of the NIMA-related Kinase Family Promote Disassembly of Cilia by Multiple Mechanisms

Wloga, Dorota, Camba, Amy, Rogowski, Krzysztof, Manning, Gerard, Jerka-Dziadosz, Maria, Gaertig, Jacek

The genome of Tetrahymena thermophila contains 39 loci encoding NIMA-related kinases (NRKs), an extraordinarily large number for a unicellular organism. Evolutionary analyses grouped these sequences...

Macronuclear Genome Sequence of the Ciliate Tetrahymena thermophila, a Model Eukaryote

Eisen, Jonathan A, Coyne, Robert S, Wu, Martin, Wu, Dongying, Thiagarajan, Mathangi, Wortman, Jennifer R, ...

The ciliate Tetrahymena thermophila is a model organism for molecular and cellular biology. Like other ciliates, this species has separate germline and soma functions that are embodied by distinct...

Katanin regulates dynamics of microtubules and biogenesis of motile cilia

Sharma, Neeraj, Bryant, Jessica, Wloga, Dorota, Donaldson, Rachel, Davis, Richard C., Jerka-Dziadosz, Maria, ...

The in vivo significance of microtubule severing and the mechanisms governing its spatial regulation are not well understood. In Tetrahymena, a cell type with elaborate microtubule arrays, we...

Glutamylation on α-Tubulin Is Not Essential but Affects the Assembly and Functions of a Subset of Microtubules in Tetrahymena thermophila▿ †

Wloga, Dorota, Rogowski, Krzysztof, Sharma, Neeraj, Van Dijk, Juliette, Janke, Carsten, Eddé, Bernard, ...

Tubulin undergoes glutamylation, a conserved posttranslational modification of poorly understood function. We show here that in the ciliate Tetrahymena, most of the microtubule arrays contain...

DYF-1 Is Required for Assembly of the Axoneme in Tetrahymena thermophila▿ †

Dave, Drashti, Wloga, Dorota, Sharma, Neeraj, Gaertig, Jacek

In most cilia, the axoneme can be subdivided into three segments: proximal (the transition zone), middle (with outer doublet microtubules), and distal (with singlet extensions of outer doublet...