Significantly decreased necrosis observed on wheat leaves inoculated with <i>ΔZtknr4</i>. by Erika Kroll (20537020)

Data Sheet 2_Ruxolitinib synergizes with regulatory T cells to improve inflammation but has no added benefits in decreasing albuminuria in SLE.pdf by Mi-Ae Lyu (20413646)

“…UCB-Treg and ruxolitinib combination also downregulates the soluble form of inflammatory cytokines including IFN-γ, IP-10, TNF-α, IL-6, sCD40L, IL-17A, IL-17F, IL-1α, and LIF in cocultures. The addition of ruxolitinib increases UCB-Treg cell persistence in peripheral blood in vivo and decreases the soluble form of human inflammatory cytokines including IFN-γ, TNF-α, and sCD40L in plasma along with improvement of skin lesions in SLE xenografts. …”

Data Sheet 3_Ruxolitinib synergizes with regulatory T cells to improve inflammation but has no added benefits in decreasing albuminuria in SLE.pdf by Mi-Ae Lyu (20413646)

“…UCB-Treg and ruxolitinib combination also downregulates the soluble form of inflammatory cytokines including IFN-γ, IP-10, TNF-α, IL-6, sCD40L, IL-17A, IL-17F, IL-1α, and LIF in cocultures. The addition of ruxolitinib increases UCB-Treg cell persistence in peripheral blood in vivo and decreases the soluble form of human inflammatory cytokines including IFN-γ, TNF-α, and sCD40L in plasma along with improvement of skin lesions in SLE xenografts. …”

Data Sheet 1_Ruxolitinib synergizes with regulatory T cells to improve inflammation but has no added benefits in decreasing albuminuria in SLE.pdf by Mi-Ae Lyu (20413646)

“…UCB-Treg and ruxolitinib combination also downregulates the soluble form of inflammatory cytokines including IFN-γ, IP-10, TNF-α, IL-6, sCD40L, IL-17A, IL-17F, IL-1α, and LIF in cocultures. The addition of ruxolitinib increases UCB-Treg cell persistence in peripheral blood in vivo and decreases the soluble form of human inflammatory cytokines including IFN-γ, TNF-α, and sCD40L in plasma along with improvement of skin lesions in SLE xenografts. …”

Table 1_Fertilization decreases the effect of ammonium nitrogen on microorganisms in Chinese Carex tibetikobresia meadows during rest-grazing.docx by Xuanbo Zhou (19374205)

Data from: <b>Selection and genetic variation in plasticity drive age-related decreases in among-individual behavioural correlations</b> by Chang Seok Han (21814121)

“…In addition, genetic variation in age-related plasticity in exploration contributed to a decrease in the magnitude of genetic correlations during the adult stage. …”

Data Sheet 1_Dihydroartemisinin decreases pre-existing neutralizing antibodies against adeno-associated virus in challenged mice.pdf by Jingjing Fang (124938)

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. …”

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. …”