نتایج جستجو برای: import

تعداد نتایج: 23938  

Journal: :Proceedings of the National Academy of Sciences of the United States of America 2005
Takehiro Sato Masatoshi Esaki Julio M Fernandez Toshiya Endo

Many newly synthesized proteins have to become unfolded during translocation across biological membranes. We have analyzed the effects of various stabilization/destabilization mutations in the Ig-like module of the muscle protein titin upon its import from the N terminus or C terminus into mitochondria. The effects of mutations on the import of the titin module from the C terminus correlate wel...

Journal: :Nature communications 2014
Christian Schulz Peter Rehling

Proteins with N-terminal targeting signals are transported across the inner mitochondrial membrane by the presequence translocase. To drive precursor translocation, the Hsp70-import motor associates with the protein-conducting channel of the TIM23 complex. It is unknown how the ATPase cycle of Hsp70 is regulated in the context of a translocating polypeptide chain. Here we establish an assay to ...

Journal: Iranian Economic Review 2017

T his paper investigates the gain of bilateral trade between China and U.S. in manufacturing sectors when both countries play a role in asymmetric (biased) growth of  international trade. Our model includes a special case of Biased Growth Theory in international trade. We collected labor productivity, export and import data by using classification of manufacturing industries, for U.S...

2015
P.K. Kim E.H. Hettema

Peroxisomes are unique among the organelles of the endomembrane system. Unlike other organelles that derive most if not all of their proteins from the ER (endoplasmic reticulum), peroxisomes contain dedicated machineries for import of matrix proteins and insertion of membrane proteins. However, peroxisomes are also able to import a subset of their membrane proteins from the ER. One aspect of pe...

Journal: :Cell 1989
T Söllner G Griffiths R Pfaller N Pfanner W Neupert

We have identified a 19 kd protein of the mitochondrial outer membrane (MOM19). Monospecific IgG and Fab fragments directed against MOM19 inhibit import of precursor proteins destined for the various mitochondrial subcompartments, including porin, cytochrome c1, Fe/S protein, F0 ATPase subunit 9, and F1 ATPase subunit beta. Inhibition occurs at the level of high affinity binding of precursors t...

Journal: :The Journal of biological chemistry 2006
Anna C Y Fan Melanie K Bhangoo Jason C Young

The Tom70 import receptor on the mitochondrial outer membrane specifically recognizes Hsp90 and Hsc70, a critical step for the import of mitochondrial preproteins, the targeting of which depends on these cytosolic chaperones. To analyze the role of Hsp90 in mitochondrial import, the effects of the Hsp90 inhibitors geldanamycin and novobiocin were compared. Geldanamycin occludes the N-terminal A...

2013
Chelsi J. Snow Ashraf Dar Anindya Dutta Ralph H. Kehlenbach Bryce M. Paschal

The RanGTPase acts as a master regulator of nucleocytoplasmic transport by controlling assembly and disassembly of nuclear transport complexes. RanGTP is required in the nucleus to release nuclear localization signal (NLS)-containing cargo from import receptors, and, under steady-state conditions, Ran is highly concentrated in the nucleus. We previously showed the nuclear/cytoplasmic Ran distri...

Journal: :Journal of cell science 2005
Sigrid Schaper Jacqueline Franke Sebastiaan H Meijsing Ann E Ehrenhofer-Murray

The protein complex SAS-I links histone acetylation to the assembly of repressed chromatin in Saccharomyces cerevisiae. Sas2p, the histone acetyltransferase subunit of SAS-I, forms a complex with Sas4p and Sas5p, which are both required for maximal complex activity. In this study, we found that Sas4p was the central subunit of the SAS-I complex, bridging Sas2p and Sas5p. We demonstrated that th...

Journal: :The Journal of biological chemistry 2007
Inga Waldmann Sarah Wälde Ralph H Kehlenbach

c-Jun and c-Fos are major components of the transcriptional complex AP-1. Here, we investigate the nuclear import pathway(s) of the transcription factor c-Jun. c-Jun bound specifically to the nuclear import receptors importin beta, transportin, importin 5, importin 7, importin 9, and importin 13. In digitonin-permeabilized cells, importin beta, transportin, importin 7, and importin 9 promoted e...

Journal: :The Journal of Cell Biology 2006
Benjamin L. Timney Jaclyn Tetenbaum-Novatt Diana S. Agate Rosemary Williams Wenzhu Zhang Brian T. Chait Michael P. Rout

Many cargoes destined for nuclear import carry nuclear localization signals that are recognized by karyopherins (Kaps). We present methods to quantitate import rates and measure Kap and cargo concentrations in single yeast cells in vivo, providing new insights into import kinetics. By systematically manipulating the amounts, types, and affinities of Kaps and cargos, we show that import rates in...

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