Results 1 to 10 of about 5,578 (161)
Structural analysis of extracellular ATP-independent chaperones of streptococcal species and protein substrate interactions [PDF]
mSphereDuring infection, bacterial pathogens rely on secreted virulence factors to manipulate the host cell. However, in gram-positive bacteria, the molecular mechanisms underlying the folding and activity of these virulence factors after membrane translocation
Charles Agbavor +13 more
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Gears-In-Motion: The Interplay of WW and PPIase Domains in Pin1
Frontiers in Oncology, 2018 Pin1 belongs to the family of the peptidyl-prolyl cis-trans isomerase (PPIase), which is a class of enzymes that catalyze the cis/trans isomerization of the Proline residue. Pin1 is unique and only catalyzes the phosphorylated Serine/Threonine-Proline (S/
Yew Mun Lee, Yih-Cherng Liou
exaly +3 more sources
Dual client binding sites in the ATP-independent chaperone SurA [PDF]
Nature CommunicationsThe ATP-independent chaperone SurA protects unfolded outer membrane proteins (OMPs) from aggregation in the periplasm of Gram-negative bacteria, and delivers them to the β-barrel assembly machinery (BAM) for folding into the outer membrane (OM ...
Bob Schiffrin +11 more
doaj +2 more sources
AMB Express, 2021 Peptidyl-prolyl cis-trans isomerase (PPIase, EC 5.2.1.8) catalyzes the racemization reaction of proline residues on a polypeptide chain. This enzyme is also known to function as a molecular chaperon to stabilize protein conformation during the folding ...
Takashi Koyanagi +7 more
doaj +1 more source
A novel mode of control of nickel uptake by a multifunctional metallochaperone.
PLoS Pathogens, 2021 Cellular metal homeostasis is a critical process for all organisms, requiring tight regulation. In the major pathogen Helicobacter pylori, the acquisition of nickel is an essential virulence determinant as this metal is a cofactor for the acid-resistance
Milica Denic +7 more
doaj +1 more source
Distribution of Peptidyl-Prolyl Isomerase (PPIase) in the Archaea
Frontiers in Microbiology, 2021 Cis-trans isomerization of the peptide bond prior to proline is an intrinsically slow process but plays an essential role in protein folding. In vivo cis-trans isomerization reaction is catalyzed by Peptidyl-prolyl isomerase (PPIases), a category of ...
Anchal, Vineeta Kaushik, Manisha Goel
doaj +1 more source
Metabolites, 2023 Legionella pneumophila (Lp) is a common etiological agent of bacterial pneumonia that causes Legionnaires’ disease (LD). The bacterial membrane-associated virulence factor macrophage infectivity potentiator (Mip) exhibits peptidyl-prolyl-cis/trans ...
Fabian Nikolka +5 more
doaj +1 more source
Structural and Functional Characterization of a Novel Family of Cyclophilins, the AquaCyps. [PDF]
PLoS ONE, 2016 Cyclophilins are ubiquitous cis-trans-prolyl isomerases (PPIases) found in all kingdoms of life. Here, we identify a novel family of cyclophilins, termed AquaCyps, which specifically occurs in marine Alphaproteobacteria, but not in related terrestric ...
Roman P Jakob +4 more
doaj +1 more source
InterAKTions with FKBPs - mutational and pharmacological exploration [PDF]
, 2013 The FK506-binding protein 51 (FKBP51) is an Hsp90-associated co-chaperone which regulates steroid receptors and kinases. In pancreatic cancer cell lines, FKBP51 was shown to recruit the phosphatase PHLPP to facilitate dephosphorylation of the kinase Akt,
Biondi, Ricardo M. +5 more
core +9 more sources
Cells, 2023 Cyclophilin E (CypE) belongs to the cyclophilin family and exhibits peptidyl-prolyl cis-trans isomerase (PPIase) activity. It participates in various biological processes through the regulation of peptidyl-prolyl isomerization. However, the specific role
Meiyu Piao +5 more
doaj +1 more source