Results 91 to 100 of about 659,160 (268)

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

Protocol to process follow-up electronic medical records of peritoneal dialysis patients to train AI models

open access: yesSTAR Protocols
Summary: The absence of standardized protocols for integrating end-stage renal disease patient data into AI models has constrained the potential of AI in enhancing patient care. Here, we present a protocol for processing electronic medical records from 1,
Tianlong Wang   +9 more
doaj   +1 more source

The inhibitory SAPS3–AMPK interaction detected in HEK293 cells is not detectable in muscle or liver from humans or mice

open access: yesFEBS Letters, EarlyView.
This study challenges the idea that Sit4‐associated protein subunit 3 (SAPS3) inhibits the energy‐sensing enzyme AMP‐activated protein kinase (AMPK) in muscle and liver tissue. Although SAPS3 interacts with AMPK in cultured cells, we found no such interaction in human or mouse tissues subjected to fasting, exercise, or a high‐fat diet.
Jesper B. Birk   +3 more
wiley   +1 more source

The zinc finger domains of PARP‐1 are selectively and potently inhibited by the Au(I)‐based drugs sodium aurothiomalate and aurothioglucose

open access: yesFEBS Letters, EarlyView.
PARP‐1 is a key enzyme in the DNA damage response, and its inhibition induces cancer cell death via synthetic lethality. Au(I)‐based drugs, such as aurothioglucose and sodium aurothiomalate, block PARP‐1's DNA‐dependent activity by targeting its zinc finger domains.
Uliana Bashtanova, Melinda Jane Duer
wiley   +1 more source

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