Results 161 to 170 of about 9,693,328 (298)

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

open access: yesFEBS 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   +8 more
wiley   +1 more source

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

open access: yesFEBS 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

Will Urban Planning Change with the Climate?

open access: yes, 2010
How urban planning and land use may accommodate the impacts of climate change.not peer reviewedSubmitted by Anthony Larson (alarson6@illinois.edu) on 2010-06-15T20:29:59Z No.
Boyer, Robert, Deal, Brian Michael
core  

Reconstructing enzyme evolution by protein engineering

open access: yesFEBS 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   +2 more
wiley   +1 more source

A Journey of Growth: Advancing the Future of [PDF]

open access: yes운동과학
Ji-Seok Kim, Jinkyung Cho, Hyuntae Park
doaj   +1 more source

Change! Change! Change!

open access: yesCollege & Research Libraries, 1974
openaire   +2 more sources

Home - About - Disclaimer - Privacy