نتایج جستجو برای: oligomerization

تعداد نتایج: 7072  

Journal: :Biochimica et biophysica acta 2009
Chunhua Shi Matthew F Paige Jason Maley Michèle C Loewen

BACKGROUND The S. cerevisiae alpha-factor receptor, Ste2p, is a G-protein coupled receptor that plays key roles in yeast signaling and mating. Oligomerization of Ste2p has previously been shown to be important for intracellular trafficking, receptor processing and endocytosis. However the role of ligand in receptor oligomerization remains enigmatic. METHODS Using functional recombinant forms ...

Journal: :The Journal of biological chemistry 2003
Axel Mogk Christian Schlieker Christine Strub Wolfgang Rist Jimena Weibezahn Bernd Bukau

ClpB of Escherichia coli is an ATP-dependent ring-forming chaperone that mediates the resolubilization of aggregated proteins in cooperation with the DnaK chaperone system. ClpB belongs to the Hsp100/Clp subfamily of AAA+ proteins and is composed of an N-terminal domain and two AAA-domains that are separated by a "linker" region. Here we present a detailed structure-function analysis of ClpB, d...

2011
Wei-Wei Shen Maud Frieden Nicolas Demaurex

The Ca(2+) depletion of the endoplasmic reticulum (ER) activates the ubiquitous store-operated Ca(2+) entry (SOCE) pathway that sustains long-term Ca(2+) signals critical for cellular functions. ER Ca(2+) depletion initiates the oligomerization of stromal interaction molecules (STIM) that control SOCE activation, but whether ER Ca(2+) refilling controls STIM de-oligomerization and SOCE terminat...

Journal: :Molecular pharmacology 2011
Peng Duan Shanshan Li Guofeng You

Human organic anion transporter 1 (hOAT1) plays a critical role in the body disposition of environmental toxins and clinically important drugs, including anti-HIV therapeutics, antitumor drugs, antibiotics, antihypertensives, and anti-inflammatories. We have demonstrated previously that hOAT1 forms homo-oligomers in cultured cells and in rat kidney. However, the functional consequence of such o...

Journal: :Biochemical and Biophysical Research Communications 2016

Journal: :Journal of bacteriology 2009
C M Santosh Kumar Garima Khare C V Srikanth Anil K Tyagi Abhijit A Sardesai Shekhar C Mande

The distinctive feature of the GroES-GroEL chaperonin system in mediating protein folding lies in its ability to exist in a tetradecameric state, form a central cavity, and encapsulate the substrate via the GroES lid. However, recombinant GroELs of Mycobacterium tuberculosis are unable to act as effective molecular chaperones when expressed in Escherichia coli. We demonstrate here that the inab...

Journal: Polyolefins Journal 2015

EEthylene polymerization catalysts became available in an enormous variety. The challenge in this research is to find catalysts that are able to connect ethylene molecules in such a way that not only linear chains are produced but variations like branched materials that possess very interesting mechanical properties like linear low density polyethylene (LLDPE). In this contribution, three diffe...

Journal: :Chemical communications 2015
Chikako Fujimoto Ayako Shinozaki Koichi Mimura Tamihito Nishida Hirotada Gotou Kazuki Komatsu Hiroyuki Kagi

Pressure-induced oligomerization was found from high-pressure experiments at 25 °C on alanine powder soaked in its saturated aqueous solution. The oligomerization to alanylalanine occurred at 5 GPa. The maximum yields of alanylalanine and trialanine were, respectively, 1.1 × 10(-3) and 1.3 × 10(-4) at 11 GPa.

Journal: :Acta biochimica et biophysica Sinica 2015
Kejiang Lin Ziyao Yu Yuanhui Yu Xinli Liao Pei Huang Chenyun Guo Donghai Lin

The cellular prion protein (PrP(C)) is a kind of cell-surface Cu(2+)-binding glycoprotein. The oligomerization of PrP(C) is highly related to transmissible spongiform encephalopathies (TSEs). Cu(2+) plays a vital role in the oligomerization of PrP(C), and participates in the pathogenic process of TSE diseases. It is expected that Cu(2+)-binding has different effects on the oligomerization of TS...

Journal: :The Journal of Membrane Biology 2019

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