Results 161 to 170 of about 19,485,349 (343)
Performance Appraisal Research: A Critical Review of Work on “The Social Context and Politics of Appraisal” [PDF]
This paper reviews existing literatures on the analysis of performance appraisal (PA) paying special attention to those which try to take into account the “social context” of appraisal systems and processes.
Jenkins , Alan
core +1 more source
Phosphatidylinositol 4‐kinase as a target of pathogens—friend or foe?
FEBS 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
Mitochondrial genome structure and composition in 70 fishes: a key resource for fisheries management in the South Atlantic [PDF]
Marcela Alvarenga +6 more
openalex +1 more source
Cross-Server End-to-End Patient Key Agreement Protocol for DNA-Based U-Healthcare in the Internet of Living Things [PDF]
, 2023 Tuan‐Vinh Le
openalex +1 more source
Four Myths and a Financial Crisis [PDF]
The main driving force of the financial crisis of 2007-2009 was a rapid deterioration of the trust of private agents in the quality of financial institutions. In turn, this loss of confidence entailed the collapse of several key asset markets and a sharp
Vranceanu, Radu
core +1 more source
FEBS 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
FEBS 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