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.
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Journal ArticleDOI
Cloning and sequencing of cDNA clones encoding chicken lamins A and B1 and comparison of the primary structures of vertebrate A- and B-type lamins
Matthias Peter,Gregory T. Kitten,Christian F. Lehner,K. Vorburger,S.M. Bailer,G. Maridor,Erich A. Nigg +6 more
TL;DR: The complete primary structures of chicken lamins A and B1, as they are deduced from cloned cDNAs are reported, and in the accompanying paper, the complete sequence of lamin B2, a second avian B-type lamin is presented.
Journal ArticleDOI
Centromere DNA decatenation depends on cohesin removal and is required for mammalian cell division
TL;DR: It is shown that persistent DNA catenation induced by inhibition of Topoisomerase-IIα can contribute to sister chromatid cohesion in the absence of cohesin complexes and that resolution ofCatenation is essential for abscission.
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Mitogen-activated protein kinases phosphorylate nuclear lamins and display sequence specificity overlapping that of mitotic protein kinase p34cdc2
TL;DR: Two distinct members of the mitogen-activated protein (MAP) kinase family are shown to phosphorylate chicken lamin B2 at a single site identified as Ser16, raising the possibility that some of the purported substrates of p34cdc2 may actually be physiological substrate of MAP kinases.
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The fates of chicken nuclear lamin proteins during mitosis: evidence for a reversible redistribution of lamin B2 between inner nuclear membrane and elements of the endoplasmic reticulum.
TL;DR: Both chicken lamins B1 and B2 may functionally resemble mammalian lamin B during mitosis, and it appears likely that during mitotic disassembly and reassembly of the nuclear envelope lamin L2 may reversibly distribute between the inner nuclear membrane and the endoplasmic reticulum.
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Activity of the Human Centrosomal Kinase, Nek2, Depends on an Unusual Leucine Zipper Dimerization Motif
TL;DR: This study reveals not only an important mechanism for the regulation of the Nek2 kinase but, furthermore, highlights an unusual organization of a leucine zipper dimerization motif.