scholarly journals NF‐κB Rel Subunit Exchange on a Physiological Timescale

2021 ◽  
Author(s):  
Matthew Biancalana ◽  
Eviatar Natan ◽  
Michael J. Lenardo ◽  
Alan R. Fersht
Keyword(s):  
Subunit Exchange

Ribosomal subunit exchange in cell-free polyphenylalanine synthesis

1971 ◽  
Vol 232 (3) ◽  
pp. 575-579 ◽  
Author(s):  
Yoshifumi Takeda ◽  
Kyoko Miyazaki ◽  
Kazuei Igarashi
Keyword(s):  
Ribosomal Subunit ◽  
Subunit Exchange

scholarly journals Association of hemoglobin Saint Etienne (alpha2beta295F8 His replaced by G1n) with hemoglobins A and F. Synthesis and subunit exchange in vitro.

1976 ◽  
Vol 251 (14) ◽  
pp. 4346-4354
Author(s):  
J F Godeau ◽  
Y G Beuzard ◽  
J Cacheleux ◽  
C P Brizard ◽  
A Gibaud ◽  
...  
Keyword(s):  
Subunit Exchange

scholarly journals Mutations in Human αA-Crystallin/sHSP Affect Subunit Exchange Interaction with αB-Crystallin

PLoS ONE ◽  
2012 ◽  
Vol 7 (2) ◽  
pp. e31421 ◽  
Author(s):  
Ilangovan Raju ◽  
Lalita Oonthonpan ◽  
Edathara C. Abraham
Keyword(s):  
Exchange Interaction ◽  
Subunit Exchange ◽  
Αb Crystallin

scholarly journals Ciliary protein conservation during development in the ciliated protozoan, Oxytricha.

1987 ◽  
Vol 105 (6) ◽  
pp. 2855-2859 ◽  
Author(s):  
G W Grimes ◽  
R H Gavin
Keyword(s):  
Cell Division ◽  
Daughter Cell ◽  
Basal Bodies ◽  
Ciliated Protozoan ◽  
Subunit Exchange ◽  
Electrophoretic Data ◽  
Autoradiographic Analysis ◽  
Protein Conservation ◽  
The One ◽  
Molecular Conservation

The ciliated protozoan Oxytricha fallax possesses multiple highly localized clusters of basal bodies and cilia, all of which are broken down and rebuilt during prefission morphogenesis-with one major exception. The adoral zone of membranelles (AZM) of the ciliate oral apparatus contains approximately 1,500-2,000 basal bodies and cilia, and it is the only compound ciliary structure that is passed morphologically intact to one daughter cell at each cell division. By labeling all proteins in cells, and then picking the one daughter cell possessing the original labeled AZM, we could then evaluate whether or not the ciliary proteins of the AZM were diluted (i.e., either by degradation to constituent amino acids or by subunit exchange) during cell division. Autoradiographic analysis demonstrated that the label was highly conserved in the AZM (i.e., we saw no evidence of turnover), and electrophoretic data illustrate that at least one of the proteins of the AZM is tubulin. We, therefore, conclude that for at least some of the ciliary and basal body proteins of Oxytricha fallax, AZM morphological conservation is essentially equivalent to molecular conservation.

scholarly journals Kinetic Asymmetry of Subunit Exchange of Homooligomeric Protein as Revealed by Deuteration-Assisted Small-Angle Neutron Scattering

2011 ◽  
Vol 101 (8) ◽  
pp. 2037-2042 ◽  
Author(s):  
Masaaki Sugiyama ◽  
Eiji Kurimoto ◽  
Hirokazu Yagi ◽  
Kazuhiro Mori ◽  
Toshiharu Fukunaga ◽  
...  
Keyword(s):  
Neutron Scattering ◽  
Small Angle ◽  
Small Angle Neutron Scattering ◽  
Subunit Exchange

scholarly journals The CaMKII holoenzyme structure in activation-competent conformations

2017 ◽  
Vol 8 (1) ◽  
Author(s):  
Janette B. Myers ◽  
Vincent Zaegel ◽  
Steven J. Coultrap ◽  
Adam P. Miller ◽  
K. Ulrich Bayer ◽  
...  
Keyword(s):  
Molecular Crowding ◽  
Extended State ◽  
Dependent Protein Kinase ◽  
Subunit Exchange ◽  
Regulatory Processes ◽  
Predominant Form ◽  
Dependent Protein ◽  
Bona Fide ◽  
Additional Level ◽  
Compact Conformation

Abstract The Ca2+/calmodulin-dependent protein kinase II (CaMKII) assembles into large 12-meric holoenzymes, which is thought to enable regulatory processes required for synaptic plasticity underlying learning, memory and cognition. Here we used single particle electron microscopy (EM) to determine a pseudoatomic model of the CaMKIIα holoenzyme in an extended and activation-competent conformation. The holoenzyme is organized by a rigid central hub complex, while positioning of the kinase domains is highly flexible, revealing dynamic holoenzymes ranging from 15–35 nm in diameter. While most kinase domains are ordered independently, ∼20% appear to form dimers and <3% are consistent with a compact conformation. An additional level of plasticity is revealed by a small fraction of bona-fide 14-mers (<4%) that may enable subunit exchange. Biochemical and cellular FRET studies confirm that the extended state of CaMKIIα resolved by EM is the predominant form of the holoenzyme, even under molecular crowding conditions.

scholarly journals L55P Transthyretin Accelerates Subunit Exchange and Leads to Rapid Formation of Hybrid Tetramers

2005 ◽  
Vol 280 (50) ◽  
pp. 41667-41674 ◽  
Author(s):  
Catherine A. Keetch ◽  
Elizabeth H. C. Bromley ◽  
Margaret G. McCammon ◽  
Nan Wang ◽  
John Christodoulou ◽  
...  
Keyword(s):  
Subunit Exchange ◽  
Rapid Formation
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