Results 191 to 200 of about 3,149,059 (351)

A minimal cellulosome‐like system in Cellulosilyticum lentocellum

open access: yesFEBS Open Bio, EarlyView.
Cellulose‐degrading bacteria typically use cellulosomes, large multi‐enzyme complexes on a scaffold protein. In Cellulosilyticum lentocellum, we characterise a far smaller arrangement, a single scaffold bound to one cellulase through a single cohesin‐dockerin interaction.
John Allan   +2 more
wiley   +1 more source

A disposable chemical heater and dry enzyme preparation for lysis and extraction of DNA and RNA from microorganisms. [PDF]

open access: yesAnal Methods, 2016
Buser JR   +10 more
europepmc   +1 more source

Physical Evaluation and Stability of HPMC-Based Bromelain Enzyme Gel Preparation

open access: hybrid
Fira Irianti Umar   +4 more
openalex   +2 more sources

The C‐terminal truncated splicing variant of NK1R negatively modulates substance P‐stimulated NK1R signaling

open access: yesFEBS Open Bio, EarlyView.
The neurokinin 1 receptor exists as full‐length (NK1L) and C‐terminally truncated (NK1S) splice variants. We show that NK1S heterodimerizes with NK1L, impairing Gαq coupling and Ca2+ mobilization while enhancing β‐arrestin1 recruitment. NK1S suppresses substance P‐driven gene expression and cell migration, revealing NK1S as an endogenous biased ...
Lan Phuong Nguyen   +8 more
wiley   +1 more source

The C‐terminal domain of yeast Arginyltransferase1 is essential for its catalytic activity

open access: yesFEBS Open Bio, EarlyView.
Arginyltransferase 1 (Ate1), a eukaryotic enzyme, catalyses arginylation, transferring arginine from tRNA‐Arg to the amino terminus of the target protein. Overexpression of Ate1 in yeast is lethal and is dependent on arginylation. This study elucidates how mutations in the cofactor‐binding and active site of Ate1 and truncation of its structural ...
Vikas Kumar Yadav   +4 more
wiley   +1 more source

Home - About - Disclaimer - Privacy