Results 131 to 140 of about 47,034,738 (363)

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

P126 | ABSTRACT WITHDRAWN

open access: yesHaematologica
Not presented.
Data not available.
doaj  

Phylogenetic analysis of Magnoliales and Myristicaceae based on multiple data sets: implications for character evolution [PDF]

open access: bronze, 2003
Hervé Sauquet   +6 more
openalex   +1 more source

Data Management: The Data Life Cycle [PDF]

open access: yes, 2012
The scientific site of Kiel provides support for projects with data management requirements due to project size or interdisciplinarity. This infrastructure is the Kiel Data Management Infrastructure (KDMI) and was initially created by SFB574, SFB754 ...
Czerniak, Andreas   +4 more
core  

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

DP086 | ABSTRACT WITHDRAWN

open access: yesHaematologica
Not presented.
Data not available.
doaj  

'Data' [PDF]

open access: yesNature, 1949
A L, BACHARACH, A V, HILL
openaire   +2 more sources

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

P196 | ABSTRACT WITHDRAWN

open access: yesHaematologica
Not presented.
Data not available.
doaj  

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