Results 131 to 140 of about 1,825,564 (240)

Eosinophilic pediatric ABPM lacking fungal sensitization responsive to anti-IL-5. [PDF]

J Allergy Clin Immunol Glob
Mizutani M, Nomura T, Nakaoka A, Tanida H, Kanemitsu Y, Hizuka K, Ueki S, Saitoh S.   +7 more
europepmc   +1 more source

ABL kinase‐dependent phosphorylation of SH proteins promotes their direct interaction with CRK family SH2 domains

FEBS Letters, EarlyView.
CT10 regulator of kinase (CRK) and CRK‐Like (CRKL) are signaling adaptors driving cell adhesion, motility, differentiation, and proliferation. SH2‐domain containing (SH) proteins are enriched in YXXP motifs which when phosphorylated create preferred binding sites for CRK family SH2 domains.
Phoebe M. Cousens, Brendan W. Chandler, Anna M. Schmoker, Jaye L. Weinert, Charlotte A. Kearns, Warren T. Yacawych, Amila Šemić, Alicia M. Ebert, Bryan A. Ballif   +8 more
wiley   +1 more source

Proteomic Identification of Plasma Biomarkers of Response to IL-5 Inhibitor Biologics in Healthy Subjects. [PDF]

Clin Transl Sci
Chekka LMS, Samarth DP, Howard KE, Guo Y, Mohamed EG, Decker E, Wheeler W, Wommack J, Gogain J, Deering J, Schrieber SJ, Wang YM, Strauss DG, Florian J, Hyland PL.   +14 more
europepmc   +1 more source

Mixed‐class J‐domain protein scaffolds promote expanded aggregate handling and multivalent Hsp70 engagement during functional disaggregase assembly

FEBS Letters, EarlyView.
Protein aggregates threaten proteostasis and cell health. In human cells, Hsp70–J‐domain protein‐based disaggregases remove aggregates, but how they assemble remains unclear. Our biochemical findings show that DNAJA2‐ and DNAJB1‐containing disaggregase scaffolds enhance luciferase aggregate targeting, and that Hsp70 recruitment by both J‐domain ...
Anna Szlachcic, Nadinath B. Nillegoda
wiley   +1 more source

Anti-IL-5 and anti-IL-5 receptor therapy significantly improves quality of life and FEV1 values in patients with severe asthma. [PDF]

Allergy Asthma Clin Immunol
Alfaro AOV, Vargas HCG, Díaz JM, Pinto JA, Cambero DCG, Cuellar EH, Zapata JAP, Domínguez AEL, Zapata JP, Ponce-Campos SD.   +9 more
europepmc   +1 more source

Reconstructing enzyme evolution by protein engineering

FEBS Letters, EarlyView.
Natural enzyme evolution can be retraced by protein engineering methods such as directed evolution, rational design, and ancestral sequence reconstruction. These approaches reveal how enzymes emerged from ligand‐binding scaffolds, developed varying substrate preferences, formed oligomeric complexes, adapted to environmental changes, and evolved novel ...
Lukas Drexler, Markus R. Busch, Reinhard Sterner   +2 more
wiley   +1 more source

Anti-IL-5 Vaccination Dampens Allergen-Specific IgE Levels and Modulates IL-4 and IL-5 Th2 Cytokines in Skin Allergy of Mice and Horses. [PDF]

Allergy
Jebbawi F, Olomski F, Inversini V, Keller G, Rhiner T, Waldern N, Lam J, Pantelyushin S, Canonica F, Birkmann K, Johansen P, Kündig TM, Fettelschoss-Gabriel A.   +12 more
europepmc   +1 more source

Decoding the dynamic extracellular matrix in cancer—3D models and bioscaffolds rewire the rules of tumor progression

FEBS Letters, EarlyView.
Cancer progression is regulated by the dynamic matrix code of the tumor microenvironment, which influences cellular behavior and disease development. Importantly, matrix remodeling in three‐dimensional cancer models more accurately reflects in vivo conditions compared to conventional two‐dimensional systems.
Sylvia Mangani, Konstantinos Spanopoulos, Zoi Piperigkou, Nikos K. Karamanos   +3 more
wiley   +1 more source

Siglec-8 as a Biomarker for Predicting Anti-IL-5 Response in Severe Asthma. [PDF]

Allergy Asthma Immunol Res
Lee Y, Kim H, Lee CE, Lee BJ, Kim MH, Park SY, Kim BK, Kim SH, Kim SH, Park HK, Lee T, Shim JS, Park CS, Park HK, Kwon JW, Kim S, Nam YH, Yang MS, Jung JW, Kim TB.   +19 more
europepmc   +1 more source

Identification of a Shiga toxin A‐derived peptide internalized into Gb3 receptor‐bearing cells via interaction with the Shiga toxin B subunit

FEBS Letters, EarlyView.
The process of internalization of the Shiga toxin A subunit via formation of a complex with the Shiga toxin B subunit, which specifically binds to the Gb3 receptor. The peptide is designed to act as a carrier of drugs into cancer cells. Here, we explored the potential of peptides derived from the catalytic A subunit of Shiga toxin (STxA) to be drug ...
Giulia Opassi, João C. Encarnação, Valeria Napolitano, Grzegorz Dubin, Grzegorz Popowicz, Karl Andersson, U. Helena Danielson   +6 more
wiley   +1 more source