Results 61 to 70 of about 9,261 (202)

Characterization of Inhibition Reveals Distinctive Properties for Human and Saccharomyces cerevisiae CRM1

open access: yes, 2020
The receptor CRM1 is responsible for the nuclear export of many tumor-suppressor proteins and viral ribonucleoproteins. This renders CRM1 an interesting target for therapeutic intervention in diverse cancer types and viral diseases. Structural studies of
Ficner, Ralf   +3 more
core   +1 more source

NESdb: a database of NES-containing CRM1 cargoes

open access: yesMolecular Biology of the Cell, 2012
The leucine-rich nuclear export signal (NES) is the only known class of targeting signal that directs macromolecules out of the cell nucleus. NESs are short stretches of 8–15 amino acids with regularly spaced hydrophobic residues that bind the export karyopherin CRM1. NES-containing proteins are involved in numerous cellular and disease processes.
Xu, Darui   +2 more
openaire   +2 more sources

A Role for Ran-GTP and Crm1 in Blocking Re-Replication [PDF]

open access: yesCell, 2003
All eukaryotic cells have regulatory mechanisms that limit genomic replication to a single round each cell cycle. These systems function by blocking formation of prereplication complexes. The regulatory mechanisms in the yeast S. cerevisiae have been identified, but these do not appear to be conserved in metazoans.
Yamaguchi, Ryuji, Newport, John
openaire   +2 more sources

Nuclear export of BATF2 enhances colorectal cancer proliferation through binding to CRM1

open access: yesClinical and Translational Medicine, 2023
Background During the tumourigenesis and development of colorectal cancer (CRC), the inactivation of tumour suppressor genes is closely involved, although detailed molecular mechanisms remain elusive.
Jie Zhou   +12 more
doaj   +1 more source

The Interaction of CRM1 and the Nuclear Pore Protein Tpr

open access: yesPLoS ONE, 2014
While much has been devoted to the study of transport mechanisms through the nuclear pore complex (NPC), the specifics of interactions and binding between export transport receptors and the NPC periphery have remained elusive. Recent work has demonstrated a binding interaction between the exportin CRM1 and the unstructured carboxylic tail of Tpr, on ...
Zhao, Charles L   +3 more
openaire   +6 more sources

Insights into the function of the CRM1 cofactor RanBP3 from the structure of its Ran-binding domain.

open access: yesPLoS ONE, 2011
Proteins bearing a leucine-rich nuclear export signal (NES) are exported from the nucleus by the transport factor CRM1, which forms a cooperative ternary complex with the NES-bearing cargo and with the small GTPase Ran.
Karla Langer   +4 more
doaj   +1 more source

RNA‐centric world of retroviruses: unravelling the molecular strategies of genomic RNA packaging

open access: yesBiological Reviews, EarlyView.
ABSTRACT Retroviruses constitute a unique group of RNA viruses that have profoundly influenced both evolutionary trajectories and biomedical research. Their ability to reverse transcribe and integrate into host genomes has shaped genomic architecture across species and contributed to our understanding of oncogenes, gene regulation, and RNA biology ...
Mohammad Abdullah Jehad   +5 more
wiley   +1 more source

CRM1 mediates nuclear-cytoplasmic shuttling of mature microRNAs [PDF]

open access: yesProceedings of the National Academy of Sciences, 2009
Drosha-processed microRNAs (miRNAs) have been shown to be exported from the nucleus to the cytoplasm by Exportin 5, where they are processed a second time to generate mature miRNAs. In this work we show that miRNAs also use CRM1 for nuclear-cytoplasmic shuttling.
Daniela, Castanotto   +3 more
openaire   +2 more sources

Role of SoxE transcription factors in development and disease

open access: yesDevelopmental Dynamics, EarlyView.
Abstract Sox8, Sox9, and Sox10 arose by multiple rounds of genome duplications from a single SoxE gene in ancestral vertebrates. In this review, we will briefly discuss the molecular structure and function of SoxE transcription factors and their evolutionary origin. We will then discuss their expression, function, and developmental disorders.
Merin Lawrence, Gerhard Schlosser
wiley   +1 more source

Binding of CRM1 to TFP-NES constructs.

open access: yes, 2015
(A) Scheme of the engineered TFP constructs, showing the sequence of the NES motifs. Φ residues are highlighted in red. (B) Titration of CRM1 onto the different TFP constructs (50 nM), at 25°C, in buffer 20 mM Tris/HCl, pH 7.4, 50 mM NaCl, 5 mM DTT, 2 mM
Igor Arregi (757643)   +7 more
core   +1 more source

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