F-Box Proteins Are Receptors that Recruit Phosphorylated Substrates to the SCF Ubiquitin-Ligase Complex

Dorota Skowyra, Karen Craig, Mike Tyers, +2

Cell

Scf Ubiquitin-ligase ComplexProtein FunctionSignal TransductionSignaling PathwayNatural Sciences +8

Rbx1, a Component of the VHL Tumor Suppressor Complex and SCF Ubiquitin Ligase

Takumi Kamura, Deanna M. Koepp, Michael N. Conrad, +9

Science

Molecular RegulationMolecular BiologyCell CycleCancer BiologyTumor Biology +14

Certain Pairs of Ubiquitin-conjugating Enzymes (E2s) and Ubiquitin-Protein Ligases (E3s) Synthesize Nondegradable Forked Ubiquitin Chains Containing All Possible Isopeptide Linkages

Hyoung Tae Kim, Kwang Pyo Kim, Fernando Lledı́as, +5

Journal of Biological Chemistry

The E. coli dnaK gene product, the hsp70 homolog, can reactivate heat-inactivated RNA polymerase in an ATP hydrolysis-dependent manner

Dorota Skowyra, Costa Georgopoulos, Maclej Zylicz

Cell

Molecular ResearchBiochemistryNatural SciencesHsp70 HomologMolecular Biology +6

SGT1 Encodes an Essential Component of the Yeast Kinetochore Assembly Pathway and a Novel Subunit of the SCF Ubiquitin Ligase Complex

Katsumi Kitagawa, Dorota Skowyra, Stephen J. Elledge, +2

Molecular Cell

Protein FunctionNovel SubunitSgt1 EncodesGeneticsMolecular Biology +7

Reconstitution of G ₁ Cyclin Ubiquitination with Complexes Containing SCF ^Grr1 and Rbx1

Dorota Skowyra, Deanna M. Koepp, Takumi Kamura, +5

Science

Scf ComplexesTranscriptional RegulationCell RegulationBiochemistryMolecular Regulation +10

A molecular chaperone, ClpA, functions like DnaK and DnaJ.

Sue Wickner, Susan Gottesman, Dorota Skowyra, +3

Proceedings of the National Academy of Sciences

Protein AssemblyMolecular BiologyMolecular GeneticsProtein RefoldingNucleic Acid Chemistry +14

Biological role and regulation of the universally conserved heat shock proteins.

D. D. Ang, Krzysztof Liberek, Dorota Skowyra, +2

Journal of Biological Chemistry

Biological RoleProtein FunctionSignal TransductionMolecular RegulationProtein Folding +10

The Escherichia coli DnaK chaperone, the 70-kDa heat shock protein eukaryotic equivalent, changes conformation upon ATP hydrolysis, thus triggering its dissociation from a bound target protein

Krzysztof Liberek, Dorota Skowyra, Maciej Żylicz, +2

Journal of Biological Chemistry

Both the Escherichia coli chaperone systems, GroEL/GroES and DnaK/DnaJ/GrpE, can reactivate heat-treated RNA polymerase. Different mechanisms for the same activity.

Alicja Ziemienowicz, Dorota Skowyra, Jill H. Zeilstra-Ryalls, +3

Journal of Biological Chemistry

Different MechanismsMolecular ResearchHeat InactivationBiochemistryNucleic Acid Chemistry +13