Results 71 to 80 of about 294,484 (344)

The coordination of nuclear envelope assembly and chromosome segregation in metazoans

Nucleus, 2020
The nuclear envelope (NE) is composed of two lipid bilayer membranes that enclose the eukaryotic genome. In interphase, the NE is perforated by thousands of nuclear pore complexes (NPCs), which allow transport in and out of the nucleus. During mitosis in
Shiwei Liu, David Pellman
doaj   +1 more source

Uncovering Nuclear Pore Complexity with Innovation [PDF]

Cell, 2013
Advances in imaging and reductionist approaches have provided a high-resolution understanding of nuclear pore complex structure and transport, revealing unexpected mechanistic complexities based on nucleoporin functions and specialized import and export pathways.
Adams, Rebecca L., Wente, Susan R.
openaire   +2 more sources

The Caenorhabditis elegans DPF‐3 and human DPP4 have tripeptidyl peptidase activity

FEBS Letters, EarlyView.
The dipeptidyl peptidase IV (DPPIV) family comprises serine proteases classically defined by their ability to remove dipeptides from the N‐termini of substrates, a feature that gave the family its name. Here, we report the discovery of a previously unrecognized tripeptidyl peptidase activity in DPPIV family members from two different species.
Aditya Trivedi, Rajani Kanth Gudipati
wiley   +1 more source

Proteasomes tether to two distinct sites at the nuclear pore complex

Proceedings of the National Academy of Sciences of the United States of America, 2017
Significance This study compares the native structures of cytosolic and nuclear proteasomes, visualized directly within cells. The assembly states and functional states of proteasomes in each compartment were similar, indicating comparable levels of ...
S. Albert, M. Schaffer, F. Beck, Shyamal Mosalaganti, Shoh M. Asano, H. Thomas, J. Plitzko, Martin Beck, W. Baumeister, B. Engel   +9 more
semanticscholar   +1 more source

Detailed characterisation of the trypanosome nuclear pore architecture reveals conserved asymmetrical functional hubs that drive mRNA export.

PLoS Biology
Nuclear export of mRNAs requires loading the mRNP to the transporter Mex67/Mtr2 in the nucleoplasm, controlled access to the pore by the basket-localised TREX-2 complex and mRNA release at the cytoplasmic site by the DEAD-box RNA helicase Dbp5 ...
Bernardo Papini Gabiatti, Johanna Krenzer, Silke Braune, Timothy Krüger, Martin Zoltner, Susanne Kramer   +5 more
doaj   +1 more source

The Potential of Nuclear Pore Complexes in Cancer Therapy

Molecules
Nuclear pore complexes (NPCs) play a critical role in regulating transport-dependent gene expression, influencing various stages of cancer development and progression.
Hanna Zaitsava, Martyna Gachowska, Elżbieta Bartoszewska, Alicja Kmiecik, Julita Kulbacka   +4 more
doaj   +1 more source

Nuclear pore complex protein mediated nuclear localization of dicer protein in human cells.

PLoS ONE, 2011
Human DICER1 protein cleaves double-stranded RNA into small sizes, a crucial step in production of single-stranded RNAs which are mediating factors of cytoplasmic RNA interference. Here, we clearly demonstrate that human DICER1 protein localizes not only
Yoshinari Ando, Yoshinari Ando, Yasuhiro Tomaru, Ayako Morinaga, Alexander Maxwell Burroughs, Hideya Kawaji, Atsutaka Kubosaki, Ryuichiro Kimura, Maiko Tagata, Yoko Ino, Hisashi Hirano, Joe Chiba, Harukazu Suzuki, Piero Carninci, Yoshihide Hayashizaki   +14 more
doaj   +1 more source

Peptide‐based ligand antagonists block a Vibrio cholerae adhesin

FEBS Letters, EarlyView.
The structure of a peptide‐binding domain of the Vibrio cholerae adhesin FrhA was solved by X‐ray crystallography, revealing how the inhibitory peptide AGYTD binds tightly at its Ca2+‐coordinated pocket. Structure‐guided design incorporating D‐amino acids enhanced binding affinity, providing a foundation for developing anti‐adhesion therapeutics ...
Mingyu Wang, Grace Du, Charity Yongo‐Luwawa, Angelina Lu, Brett Kinrade, Kim Munro, Karl E. Klose, William D. Lubell, Peter Davies, Shuaiqi Guo   +9 more
wiley   +1 more source

Mechanisms of nuclear pore complex assembly – two different ways of building one molecular machine

FEBS Letters, 2017
The nuclear pore complex (NPC) mediates all macromolecular transport across the nuclear envelope. In higher eukaryotes that have an open mitosis, NPCs assemble at two points in the cell cycle: during nuclear assembly in late mitosis and during nuclear ...
S. Otsuka, J. Ellenberg
semanticscholar   +1 more source

Nuclear pore dysfunction and disease: a complex opportunity

Nucleus
The separation of genetic material from bulk cytoplasm has enabled the evolution of increasingly complex organisms, allowing for the development of sophisticated forms of life. However, this complexity has created new categories of dysfunction, including
Charlotte M. Fare, Jeffrey D. Rothstein
doaj   +1 more source