Aging impairs renal mitochondrial function and antioxidant capacity. by Lihua Qiu (178071)

The loss of NLRP3 and AIM2 results in reduced Th17 and enhanced Th2 cytokine responses. by Madhusoodhanan Suresh Kumar Meena Kumari (20896666)

Egg-induced IL-1β and IL-17 production is dependent on both Caspase-1 and Caspase-8. by Madhusoodhanan Suresh Kumar Meena Kumari (20896666)

<i>In vivo</i> treatment decreases bacterial burden and colonization of vital organs in a skin abscess biofilm infection model. by Robert L. Beckman I.V (22784303)

Aging enhances α-SMA expression and collagen accumulation in the kidney. by Lihua Qiu (178071)

Alterations in renal tubular morphology and renal interstitial collagen deposition were observed in aged mice. by Lihua Qiu (178071)

Aging regulates mRNA levels of renal fibrosis-related genes in mice across varying age cohort. by Lihua Qiu (178071)

<i>shk-1</i> mutants display decreased glycogen storage. by Longjun Pu (20685717)

Pan-cancer analyses of ANGPTL4 expression and its prognostic significance in the TCGA database. by Yu Zhang (12946)

Pan-cancer analyses of NFKB2 expression and its prognostic significance in the TCGA database. by Yu Zhang (12946)

RipE1 undergoes phosphorylation in <i>N. benthamiana</i>, which contributes to protein stability. by Wenjia Yu (9422059)

Heterogeneous Condensation on Simplified Viral Envelope Protein Structures by Kawkab Ahasan (18784843)

“…The rapid initial condensation fills up the gap between the pillars, reducing the active surface area and leading to a gradual decrease and a plateau in the condensation rate. …”

Heterogeneous Condensation on Simplified Viral Envelope Protein Structures by Kawkab Ahasan (18784843)

“…The rapid initial condensation fills up the gap between the pillars, reducing the active surface area and leading to a gradual decrease and a plateau in the condensation rate. …”

Heterogeneous Condensation on Simplified Viral Envelope Protein Structures by Kawkab Ahasan (18784843)

“…The rapid initial condensation fills up the gap between the pillars, reducing the active surface area and leading to a gradual decrease and a plateau in the condensation rate. …”

Heterogeneous Condensation on Simplified Viral Envelope Protein Structures by Kawkab Ahasan (18784843)

“…The rapid initial condensation fills up the gap between the pillars, reducing the active surface area and leading to a gradual decrease and a plateau in the condensation rate. …”

Heterogeneous Condensation on Simplified Viral Envelope Protein Structures by Kawkab Ahasan (18784843)

“…The rapid initial condensation fills up the gap between the pillars, reducing the active surface area and leading to a gradual decrease and a plateau in the condensation rate. …”

Heterogeneous Condensation on Simplified Viral Envelope Protein Structures by Kawkab Ahasan (18784843)

“…The rapid initial condensation fills up the gap between the pillars, reducing the active surface area and leading to a gradual decrease and a plateau in the condensation rate. …”

Heterogeneous Condensation on Simplified Viral Envelope Protein Structures by Kawkab Ahasan (18784843)

“…The rapid initial condensation fills up the gap between the pillars, reducing the active surface area and leading to a gradual decrease and a plateau in the condensation rate. …”

Heterogeneous Condensation on Simplified Viral Envelope Protein Structures by Kawkab Ahasan (18784843)

“…The rapid initial condensation fills up the gap between the pillars, reducing the active surface area and leading to a gradual decrease and a plateau in the condensation rate. …”

Heterogeneous Condensation on Simplified Viral Envelope Protein Structures by Kawkab Ahasan (18784843)

“…The rapid initial condensation fills up the gap between the pillars, reducing the active surface area and leading to a gradual decrease and a plateau in the condensation rate. …”