Results 301 to 310 of about 127,473 (347)
A signal transduction blind spot: the function of adenylyl cyclase transmembrane domains
The FEBS Journal, EarlyView.Transmembrane adenylyl cyclases (tmACs) are essential for synthesising the universal second messenger cyclic AMP. All tmACs share a common topology that includes a large 12‐helix transmembrane (TM) domain. This domain accounts for ~ 35% of the coding sequence but its function is still an open question.
Ryan S. Dowsell, Matthew G. Gold
wiley +1 more source
Uncertainty‐Aware Visualization of Biomolecular Structures
Computer Graphics Forum, EarlyView.
A. Sterzik +3 more
wiley +1 more source
Aptamers for allosteric regulation [PDF]
Nature Chemical Biology, 2011 Aptamers are useful for allosteric regulation because they are nucleic acid-based structures in which ligand binding induces conformational changes that may alter the function of a connected oligonucleotide at a distant site. Through this approach, a specific input is efficiently converted into an altered output.
Vinkenborg, J. +2 more
openaire +3 more sources
Some of the next articles are maybe not open access.
Related searches:
Related searches:
Allosteric Regulation of Proteases
ChemBioChem, 2008AbstractAllostery is a basic principle of control of enzymatic activities based on the interaction of a protein or small molecule at a site distinct from an enzyme's active center. Allosteric modulators represent an alternative approach to the design and synthesis of small‐molecule activators or inhibitors of proteases and are therefore of wide ...
Hauske, Patrick +4 more
openaire +4 more sources
Allosteric regulation of chaperonins
Current Opinion in Structural Biology, 2005Chaperonins are molecular machines that facilitate protein folding by undergoing energy (ATP)-dependent movements that are coordinated in time and space by complex allosteric regulation. Recently, progress has been made in describing the various functional (allosteric) states of these machines, the pathways by which they interconvert, and the coupling ...
Horovitz, A, Willison, KR
openaire +4 more sources
Diversity of Allosteric Regulation in Proteases
ACS Chemical Biology, 2012Allostery is a fundamental regulatory mechanism that is based on a functional modulation of a site by a distant site. Allosteric regulation can be triggered by binding of diverse allosteric effectors, ranging from small molecules to macromolecules, and is therefore offering promising opportunities for functional modulation in a wide range of ...
Merdanovic, Melisa +3 more
openaire +4 more sources
NADPH Is an Allosteric Regulator of HSCARG
Journal of Molecular Biology, 2009NADP(H) is an important cofactor that controls many fundamental cellular processes. We have determined the crystal structure of HSCARG, a novel NADPH sensor, and found that it forms an asymmetrical dimer with only one subunit occupied by an NADPH molecule, and the two subunits have dramatically different conformations.
Geng Meng +8 more
openaire +2 more sources
Allosteric regulation of phosphoribulokinase activity
Biochemical and Biophysical Research Communications, 1968Inhibition of ATP-dependent CO2 fixation by AMP has been reported in several autotrophic organisms (Johnson and Peck, 1965; Mayeux and Johnson, 1966;Johnson, 1966; Gale and Beck, 1966). Johnson (1966) suggested that the site of AMP inhibition is phosphoribulokinase and that inhibition may occur through allosteric modification of the enzyme. In contrast,
Emmett J. Johnson +2 more
openaire +3 more sources
The role of dynamics in allosteric regulation
Current Opinion in Structural Biology, 2003The biomolecular conformational changes often associated with allostery are, by definition, dynamic processes. Recent publications have disclosed the role of pre-existing equilibria of conformational substates in this process. In addition, the role of dynamics as an entropic carrier of free energy of allostery has been investigated.
Erik R. P. Zuiderweg, Dorothee Kern
openaire +3 more sources