E
Erich A. Nigg
Researcher at University of Basel
Publications - 302
Citations - 54857
Erich A. Nigg is an academic researcher from University of Basel. The author has contributed to research in topics: Mitosis & Centrosome. The author has an hindex of 90, co-authored 302 publications receiving 52056 citations. Previous affiliations of Erich A. Nigg include European Bioinformatics Institute & University of Leicester.
Papers
More filters
Journal ArticleDOI
STIL binding to Polo-box 3 of PLK4 regulates centriole duplication
Christian Arquint,Anna-Maria Gabryjonczyk,Stefan Imseng,Raphael Böhm,Evelyn Sauer,Sebastian Hiller,Erich A. Nigg,Timm Maier +7 more
TL;DR: It is suggested that the STIL-CC/PLK4 interaction mediates PLK4 activation as well as stabilization of centriolar PLK 4 and plays a key role in centriole duplication.
Journal ArticleDOI
Uncoupling of the spindle-checkpoint and chromosome-congression functions of BubR1.
TL;DR: A functional analysis of conserved motifs of human BubR1 shows that spindle assembly checkpoint (SAC) and chromosome attachment functions can be uncoupled from each other and that the GLEBS motif is strictly required for both major functions of humanbubR1.
Journal ArticleDOI
Quantitative Analysis of the Human Spindle Phosphoproteome at Distinct Mitotic Stages
TL;DR: A quantitative comparison of spindle phosphoproteomes prepared from different mitotic stages and finds that late mitosis (anaphase, telophase) is correlated with a drastic alteration in protein phosphorylation, and a substrate preference of phosphatases for phospho-threonine at this stage is observed.
Journal ArticleDOI
The mechanism regulating the dissociation of the centrosomal protein C-Nap1 from mitotic spindle poles.
TL;DR: The data indicate that the mitotic C-Nap1 signal is reduced as a consequence of M-phase-specific phosphorylation, and this activity is a prime candidate for the centrosomal protein kinase Nek2, as the formation of large C- Nap1 structures was substantially reduced upon co-expression of active Nek2.
Journal ArticleDOI
Immunofluorescent localization of the transforming protein of Rous sarcoma virus with antibodies against a synthetic src peptide
TL;DR: The excellent agreement of the results obtained with two completely independent antibody preparations indicates strongly that the observed immunolabeling patterns correctly define the intracellular distribution of p60src.