Results 1 to 10 of about 3,145 (114)

Distribution of Peptidyl-Prolyl Isomerase (PPIase) in the Archaea

open access: yesFrontiers 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 ...
Manisha Goel, Goel Manisha
exaly   +3 more sources

Structural analysis of extracellular ATP-independent chaperones of streptococcal species and protein substrate interactions [PDF]

open access: yesmSphere
During 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
doaj   +2 more sources

Data sets on the interaction of FKBP35 from Plasmodium knowlesi and Hsp90 C-terminal pentapeptideMendeley Data [PDF]

open access: yesData in Brief
FK506-binding protein 35 from Plasmodium knowlesi (Pk-FKBP35) is a multidomain peptidyl–prolyl cis–trans isomerase (PPIase) considered a potential target for antimalarial drug development. The protein consists of an N-terminal FK506-binding domain (FKBD)
Cahyo Budiman   +9 more
doaj   +2 more sources

Cyclophilin J PPIase Inhibitors Derived from 2,3-Quinoxaline-6 Amine Exhibit Antitumor Activity

open access: yesFrontiers in Pharmacology, 2018
Cyclophilin J (CyPJ), also called peptidylprolyl isomerase like 3, has been identified as a novel member of the cyclophilin family. Our previous research has resolved the three-dimensional structure of CyPJ and demonstrated the peptidylprolyl cis–trans ...
Yulong Liang, Chengcai Xia
exaly   +3 more sources

Thermococcus sp. KS-1 PPIase as a fusion partner improving soluble production of aromatic amino acid decarboxylase

open access: yesAMB 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.

open access: yesPLoS 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

The Virulence Factor Macrophage Infectivity Potentiator (Mip) Influences Branched-Chain Amino Acid Metabolism and Pathogenicity of Legionella pneumophila

open access: yesMetabolites, 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]

open access: yesPLoS 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

Cyclophilin E (CypE) Functions as a Positive Regulator in Osteoblast Differentiation by Regulating the Transcriptional Activity of Runx2

open access: yesCells, 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

Home - About - Disclaimer - Privacy