Discover Community Create You

Loading publication...

Noodle always counts identifier-free feature events for service operation. With your permission, Google Analytics can also estimate audience and engagement. Search text, publication identifiers, cookies, IP addresses and browser fingerprints are never included in Noodle's first-party event counters.

Privacy details

Article

Mutational analysis of human prothymosin alpha reveals a bipartite nuclear localization signal.

FEBS letters - 11 Aug 1997

Rubtsov Y P, Zolotukhin A S, Vorobjev I A, Chichkova N V, Pavlov N A, Karger E M, Evstafieva A G, Felber B K, Vartapetian A B

Abstract excerpt

Mutants of human prothymosin alpha with impaired ability to inhibit yeast Saccharomyces cerevisiae. cerevisiae cell growth were characterized. Two types of prothymosin alpha-inactivating mutations were observed. Mutations that belong to the first type compromised the nuclear entry of prothymosin alpha by affecting its nuclear localization signal. Analysis of subcellular distribution of GFP-prothymosin alpha...

Read the complete abstract on PubMed

Topics

Share this publication in a Topic to start or enrich a Post.

Share to Amino Acid Sequence
Share to Cell Division

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Cells, Cultured

Share to Molecular Sequence Data

Share to Mutagenesis

Share to Mutation

Share to Nuclear Proteins

Share to Saccharomyces cerevisiae

Source

Identifiers

PMID: 9287131
DOI: 10.1016/s0014-5793(97)00824-7

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-07.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Mutational analysis of human prothymosin alpha reveals a bipartite nuclear localization signal.PMID 9287131Read ↗

A bipartite, mutation-tolerant NLS regulates interaction of ΔNp63α with importin alpha, nuclear transport and transcriptional activitySemantic proximity Read ↗

Dissection of the karyopherin alpha nuclear localization signal (NLS)-binding groove: functional requirements for NLS binding.Semantic proximity Read ↗

Characterization of the nuclear import of human MutLαSemantic proximity Read ↗

[Influence of prothymosin alpha and its mutants on activity of the p53 tumor suppressor].Semantic proximity Read ↗

Parafibromin is a nuclear protein with a functional monopartite nuclear localization signal.Semantic proximity Read ↗

Apoptosis-related fragmentation, translocation, and properties of human prothymosin alpha.Semantic proximity Read ↗

[Novel functions of the well-known protein--prothymosin alpha is involved in protection of cells against apoptosis and oxidative stress].Semantic proximity Read ↗

Characterization of the auto-inhibitory sequence within the N-terminal domain of importin alpha.Semantic proximity Read ↗

Analysis of epitope-tagged forms of the dyskeratosis congenital protein (dyskerin): identification of a nuclear localization signal.Semantic proximity Read ↗

Recovery of mitogenic activity of a growth factor mutant with a nuclear translocation sequence.Semantic proximity Read ↗

The Drosophila importin-α3 is required for nuclear import of notch in vivo and it displays synergistic effects with notch receptor on cell proliferation.Semantic proximity Read ↗

Kinetic Characterization of the Human Retinoblastoma Protein Bipartite Nuclear Localization Sequence (NLS) in Vivo andin VitroSemantic proximity Read ↗

⌁Select a neighboring publication to make it the new centre.