Microscopic Temperature Control Reveals Cooperative Regulation of Actin–Myosin Interaction by Drebrin E by Hiroaki Kubota (5798264)

“…Here, by applying the microscopic heat pulse method to actomyosin motility assay, the regulatory mechanism is examined from the room temperature up to 37 °C without a thermal denaturing of proteins. We show that the inhibition of actomyosin motility by drebrin E is eliminated immediately and reversibly during heating and depends on drebrin E concentration. …”

Microscopic Temperature Control Reveals Cooperative Regulation of Actin–Myosin Interaction by Drebrin E by Hiroaki Kubota (5798264)

“…Here, by applying the microscopic heat pulse method to actomyosin motility assay, the regulatory mechanism is examined from the room temperature up to 37 °C without a thermal denaturing of proteins. We show that the inhibition of actomyosin motility by drebrin E is eliminated immediately and reversibly during heating and depends on drebrin E concentration. …”

Microscopic Temperature Control Reveals Cooperative Regulation of Actin–Myosin Interaction by Drebrin E by Hiroaki Kubota (5798264)

“…Here, by applying the microscopic heat pulse method to actomyosin motility assay, the regulatory mechanism is examined from the room temperature up to 37 °C without a thermal denaturing of proteins. We show that the inhibition of actomyosin motility by drebrin E is eliminated immediately and reversibly during heating and depends on drebrin E concentration. …”

Microscopic Temperature Control Reveals Cooperative Regulation of Actin–Myosin Interaction by Drebrin E by Hiroaki Kubota (5798264)

“…Here, by applying the microscopic heat pulse method to actomyosin motility assay, the regulatory mechanism is examined from the room temperature up to 37 °C without a thermal denaturing of proteins. We show that the inhibition of actomyosin motility by drebrin E is eliminated immediately and reversibly during heating and depends on drebrin E concentration. …”

Microscopic Temperature Control Reveals Cooperative Regulation of Actin–Myosin Interaction by Drebrin E by Hiroaki Kubota (5798264)

“…Here, by applying the microscopic heat pulse method to actomyosin motility assay, the regulatory mechanism is examined from the room temperature up to 37 °C without a thermal denaturing of proteins. We show that the inhibition of actomyosin motility by drebrin E is eliminated immediately and reversibly during heating and depends on drebrin E concentration. …”

Microscopic Temperature Control Reveals Cooperative Regulation of Actin–Myosin Interaction by Drebrin E by Hiroaki Kubota (5798264)

“…Here, by applying the microscopic heat pulse method to actomyosin motility assay, the regulatory mechanism is examined from the room temperature up to 37 °C without a thermal denaturing of proteins. We show that the inhibition of actomyosin motility by drebrin E is eliminated immediately and reversibly during heating and depends on drebrin E concentration. …”

Microscopic Temperature Control Reveals Cooperative Regulation of Actin–Myosin Interaction by Drebrin E by Hiroaki Kubota (5798264)

“…Here, by applying the microscopic heat pulse method to actomyosin motility assay, the regulatory mechanism is examined from the room temperature up to 37 °C without a thermal denaturing of proteins. We show that the inhibition of actomyosin motility by drebrin E is eliminated immediately and reversibly during heating and depends on drebrin E concentration. …”

Microscopic Temperature Control Reveals Cooperative Regulation of Actin–Myosin Interaction by Drebrin E by Hiroaki Kubota (5798264)

“…Here, by applying the microscopic heat pulse method to actomyosin motility assay, the regulatory mechanism is examined from the room temperature up to 37 °C without a thermal denaturing of proteins. We show that the inhibition of actomyosin motility by drebrin E is eliminated immediately and reversibly during heating and depends on drebrin E concentration. …”

Supplementary Material for: Nutrition Status Plays a partial Mediation Role in the relationship between number of Teeth and Frailty: A Cross-sectional Multi-center Study by Xia X. (5813546)

“…Results Among the 6664 participants aged over 50 years old, the prevalence of frailty was 6.2%. …”

Primer sequences used in experiments. by Han Jiang (195350)

“…Repression of <i>tspan12</i> and <i>tspan13</i> gene expression led to decreased secretion of cysteine proteases, while repression of <i>tspan4</i> led to a four-fold increase in the activity of cysteine proteases in crude extracellular vesicles (EVs) fraction. …”

Evolutionary changes during adaptation to a nutrient-rich environment. by Kazufumi Hosoda (229927)

“…The transfers of the culture by dilution are depicted as the vertical decrease in the cell concentration. (B) Evolutionary changes in the specific growth rate (<i>μ</i>) in media with different toxic amino acid concentrations (the colors are same as in A). …”

Sediment Bacterial Communities Reflect the History of a Sea Basin by Christina Lyra (215633)

“…Palaeosalinity was one of the major parameters that separated the bacterial communities of the stratified sediments. A discontinuous spatial structure with a surprising increase in community heterogeneity was detected in Litorina Sea sediments from 388 to 422 cm deep, which suggests that a salinity maximum occurred in the central Gulf of Finland app. 6200–6600 years ago. …”

Coacervation of Elastin-Like Polypeptides: A Coarse-Grained Perspective by Piyali Mukherjee (372956)

“…Higher temperatures lead to stronger interchain interactions among polypeptides and weaker interactions with water, supported by a decrease in water number density during coacervate formation. …”

Trophic Shifts of a Generalist Consumer in Response to Resource Pulses by Pei-Jen L. Shaner (227093)

“…However, the pattern was reversed in the second grid, with a 13% decrease in the consumer contribution with the cicadas pulse. …”

Coacervation of Elastin-Like Polypeptides: A Coarse-Grained Perspective by Piyali Mukherjee (372956)

“…Higher temperatures lead to stronger interchain interactions among polypeptides and weaker interactions with water, supported by a decrease in water number density during coacervate formation. …”

Coacervation of Elastin-Like Polypeptides: A Coarse-Grained Perspective by Piyali Mukherjee (372956)

“…Higher temperatures lead to stronger interchain interactions among polypeptides and weaker interactions with water, supported by a decrease in water number density during coacervate formation. …”

Coacervation of Elastin-Like Polypeptides: A Coarse-Grained Perspective by Piyali Mukherjee (372956)

“…Higher temperatures lead to stronger interchain interactions among polypeptides and weaker interactions with water, supported by a decrease in water number density during coacervate formation. …”

Coacervation of Elastin-Like Polypeptides: A Coarse-Grained Perspective by Piyali Mukherjee (372956)

“…Higher temperatures lead to stronger interchain interactions among polypeptides and weaker interactions with water, supported by a decrease in water number density during coacervate formation. …”

Antibiotic therapy in ventilator-associated tracheobronchitis: a literature review by Abel Eduardo Alves (5187140)

“…This review provides a better understanding of the differentiation between tracheobronchitis associated with mechanical ventilation and pneumonia associated with mechanical ventilation, which can significantly decrease the use of antibiotics in critically ventilated patients.…”

FSL of MSO neurons in relation to click intensity, frequency, and within the same animal. by Martijn C. Sierksma (11608174)