Results 21 to 30 of about 2,484 (223)
Internal Motility in Stiffening Actin-Myosin Networks
, 2003 We present a study on filamentous actin solutions containing heavy meromyosin subfragments of myosin II motor molecules. We focus on the viscoelastic phase behavior and internal dynamics of such networks during ATP depletion.
A. G. Weeds +10 more
core +1 more source
Protease-sensitive regions in myosin subfragment 1. [PDF]
Proceedings of the National Academy of Sciences, 1983 Proteolytic digestions of myosin subfragment 1 (S-1) with elastase, subtilisin, papain, thermolysin, and Staphylococcus aureus protease reveal that the two trypsin-sensitive regions in S-1 have broad protease susceptibility. The cleavage of S-1 by these enzymes yields products that correspond within 1-2 kilodaltons (kDa) to the 25-, 50-, and 20-kDa ...
D, Applegate, E, Reisler
openaire +2 more sources
FEBS Letters, Volume 593, Issue 2, Page 219-229, January 2019., 2019 Deinococcus radiodurans R1 is extremely resistant to ionizing radiation and oxidative stress. In this study, we characterized DR0846, a candidate peroxiredoxin in D. radiodurans. DR0846 is a peroxiredoxin Q containing two conserved cysteine residues. DR0846 exists mainly in monomeric form with an intramolecular disulfide bond between the two cysteine ...
Chuloh Cho +8 more
wiley +1 more source
The central domain of UNC‐45 chaperone inhibits the myosin power stroke
FEBS Open Bio, Volume 8, Issue 1, Page 41-48, January 2018., 2018 The multidomain UNC‐45B chaperone is crucial for the proper folding and function of sarcomeric myosin. Here, we show—using in vitro myosin motility and ATPase assays—that the central domain of UNC‐45B inhibits myosin power stroke through a mechanism that allows ATP turnover. Based on these data, we propose a novel model for the action of this chaperone
Paul J. Bujalowski +3 more
wiley +1 more source
Axon Initial Segment Cytoskeleton: Architecture, Development, and Role in Neuron Polarity
Neural Plasticity, Volume 2016, Issue 1, 2016., 2016 The axon initial segment (AIS) is a specialized structure in neurons that resides in between axonal and somatodendritic domains. The localization of the AIS in neurons is ideal for its two major functions: it serves as the site of action potential firing and helps to maintain neuron polarity.
Steven L. Jones +2 more
wiley +1 more source
Competitive titration in living sea urchin embryos of regulatory factors required for expression of the CyIIIa actin gene [PDF]
, 1990 Previous studies have located some twenty distinct sites within the 2.3 kb 5' regulatory domain of the sea urchin CyIIIa cytoskeletal actin gene, where there occur in vitro high-specificity interactions with nuclear DNA-binding proteins of the embryo ...
Anderson, Roger +5 more
core
Gelation properties of porcine muscle proteins [PDF]
, 1989 The effects of linearly increasing heating rates (17, 38 and 85°C/hr) and protein concentration (10, 20, 30, 40 and 50 mg/mL) on thermally induced gels made of extracted salt-soluble proteins were evaluated. Gel strength analyses indicated that the force
Camou Arriola, Juan Pedro
core +2 more sources
Plant, Cell &Environment, Volume 48, Issue 12, Page 8561-8572, December 2025.ABSTRACT Entomopathogenic nematodes (EPNs) are key biological control agents in agriculture, but their direct effects on plant metabolism and resistance to herbivory remain underexplored. By combining transcriptomic, metabolomic, and herbivore assays, this study aimed at providing a holistic description of maize root responses to EPNs and to assess ...
Arletys M. Verdecia‐Mogena +7 more
wiley +1 more source
Poorly Understood Aspects of Striated Muscle Contraction
BioMed Research International, Volume 2015, Issue 1, 2015., 2015 Muscle contraction results from cyclic interactions between the contractile proteins myosin and actin, driven by the turnover of adenosine triphosphate (ATP). Despite intense studies, several molecular events in the contraction process are poorly understood, including the relationship between force‐generation and phosphate‐release in the ATP‐turnover ...
Alf Månsson +3 more
wiley +1 more source
Structural and Energetic Characterization of the Ankyrin Repeat Protein Family [PDF]
, 2015 Ankyrin repeat containing proteins are one of the most abundant solenoid folds. Usually implicated in specific protein-protein interactions, these proteins are readily amenable for design, with promising biotechnological and biomedical applications ...
Espada, Rocío +3 more
core +1 more source