Results 71 to 80 of about 6,846,511 (358)

Gate-count estimates for performing quantum chemistry on small quantum computers [PDF]

open access: green, 2014
Dave Wecker   +4 more
openalex   +1 more source

Phosphatidylinositol 4‐kinase as a target of pathogens—friend or foe?

open access: yesFEBS Letters, EarlyView.
This graphical summary illustrates the roles of phosphatidylinositol 4‐kinases (PI4Ks). PI4Ks regulate key cellular processes and can be hijacked by pathogens, such as viruses, bacteria and parasites, to support their intracellular replication. Their dual role as essential host enzymes and pathogen cofactors makes them promising drug targets.
Ana C. Mendes   +3 more
wiley   +1 more source

Association Of G-Quadruplex Forming Sequences With Human MtDNA Deletion Breakpoints [PDF]

open access: yes, 2014
Background: Mitochondrial DNA (mtDNA) deletions cause disease and accumulate during aging, yet our understanding of the molecular mechanisms underlying their formation remains rudimentary.
Barrett, Steven Paul, , \u2713   +8 more
core   +1 more source

Chemistry on the inside: green chemistry in mesoporous materials [PDF]

open access: yes, 2000
An overview of the rapidly expanding area of tailored mesoporous solids is presented. The synthesis of a wide range of the materials is covered, both inorganically and organically modified.
Brunel D.   +3 more
core   +1 more source

Structural insights into lacto‐N‐biose I recognition by a family 32 carbohydrate‐binding module from Bifidobacterium bifidum

open access: yesFEBS Letters, EarlyView.
Bifidobacterium bifidum establishes symbiosis with infants by metabolizing lacto‐N‐biose I (LNB) from human milk oligosaccharides (HMOs). The extracellular multidomain enzyme LnbB drives this process, releasing LNB via its catalytic glycoside hydrolase family 20 (GH20) lacto‐N‐biosidase domain.
Xinzhe Zhang   +5 more
wiley   +1 more source

The Caenorhabditis elegans DPF‐3 and human DPP4 have tripeptidyl peptidase activity

open access: yesFEBS Letters, EarlyView.
The dipeptidyl peptidase IV (DPPIV) family comprises serine proteases classically defined by their ability to remove dipeptides from the N‐termini of substrates, a feature that gave the family its name. Here, we report the discovery of a previously unrecognized tripeptidyl peptidase activity in DPPIV family members from two different species.
Aditya Trivedi, Rajani Kanth Gudipati
wiley   +1 more source

Home - About - Disclaimer - Privacy