Results 51 to 60 of about 114,835 (256)

Karyopherin binding interactions and nuclear import mechanism of nuclear pore complex protein Tpr

BMC Cell Biology, 2009
Background Tpr is a large protein with an extended coiled-coil domain that is localized within the nuclear basket of the nuclear pore complex. Previous studies 1 involving antibody microinjection into mammalian cells suggested a role for Tpr in nuclear ...
Frosst Phyllis D, Ben-Efraim Iris, Gerace Larry   +2 more
doaj   +1 more source

Expression of DNAJB12 or DNAJB14 causes coordinate invasion of the nucleus by membranes associated with a novel nuclear pore structure. [PDF]

PLoS ONE, 2014
DNAJB12 and DNAJB14 are transmembrane proteins in the endoplasmic reticulum (ER) that serve as co-chaperones for Hsc70/Hsp70 heat shock proteins. We demonstrate that over-expression of DNAJB12 or DNAJB14 causes the formation of elaborate membranous ...
Edward C Goodwin, Nasim Motamedi, Alex Lipovsky, Rubén Fernández-Busnadiego, Daniel DiMaio   +4 more
doaj   +1 more source

Calpain small subunit homodimerization is robust and calcium‐independent

FEBS Letters, EarlyView.
Calpains dimerize via penta‐EF‐hand (PEF) domains. Using single‐molecule force spectroscopy, we measured the strength and kinetics of PEF–PEF homodimer binding. The interaction is robust, shows a transient conformational step before dissociation, and remains largely insensitive to Ca2+.
Nesha May O. Andoy, Trina Dykstra‐MacPherson, Mathias A. Bell, Peter L. Davies, Ruby May A. Sullan   +4 more
wiley   +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

The major polypeptides of the nuclear pore complex [PDF]

Experimental Cell Research, 1978
Abstract Nuclear envelopes of maturing oocytes of various amphibia contain an unusually high number of pore complexes in very close packing. Consequently, nuclear envelopes, which can be manually isolated in great purity, provide a remarkable enrichment of nuclear pore complex material, relative to membranous and other interporous structures.
Krohne, Georg, Franke, Werner W., Scheer, Ulrich   +2 more
openaire   +2 more sources

Structural insights into an engineered feruloyl esterase with improved MHET degrading properties

FEBS Letters, EarlyView.
A feruloyl esterase was engineered to mimic key features of MHETase, enhancing the degradation of PET oligomers. Structural and computational analysis reveal how a point mutation stabilizes the active site and reshapes the binding cleft, expading substrate scope.
Panagiota Karampa, Konstantinos Makryniotis, Theofani‐Iosifina Sousani, Evangelos Topakas, Vangelis Daskalakis, Maria Dimarogona   +5 more
wiley   +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

Higher nucleoporin-Importinβ affinity at the nuclear basket increases nucleocytoplasmic import.

PLoS ONE, 2013
Several in vitro studies have shown the presence of an affinity gradient in nuclear pore complex proteins for the import receptor Importinβ, at least partially contributing to nucleocytoplasmic transport, while others have historically argued against the
Mohammad Azimi, Mohammad R K Mofrad
doaj   +1 more source

Valosin‐containing protein counteracts ATP‐driven dissolution of FUS condensates through its ATPase activity in vitro

FEBS Letters, EarlyView.
Biomolecular condensates formed by fused in sarcoma (FUS) are dissolved by high ATP concentrations yet persist in cells. Using a reconstituted system, we demonstrate that valosin‐containing protein (VCP), an AAA+ ATPase, counteracts ATP‐driven dissolution of FUS condensates through its D2 ATPase activity.
Hitomi Kimura, Shin‐ichi Tate, Kyota Yasuda   +2 more
wiley   +1 more source