scholarly journals Roles of peptidyl-prolyl isomerase Pin1 in disease pathogenesis

Theranostics ◽  
2021 ◽  
Vol 11 (7) ◽  
pp. 3348-3358
Author(s):  
Jingyi Li ◽  
Chunfen Mo ◽  
Yifan Guo ◽  
Bowen Zhang ◽  
Xiao Feng ◽  
...  
Keyword(s):  
Prolyl Isomerase ◽  
Disease Pathogenesis ◽  
Peptidyl Prolyl Isomerase

The peptidyl-prolyl isomerase SlrA contributes to virulence and adherence of Streptococcus pneumoniae

Pneumologie ◽  
2006 ◽  
Vol 60 (02) ◽  
Author(s):  
S Hammerschmidt ◽  
PV Adrian ◽  
C Albert ◽  
S Estevão ◽  
T Hoogenboezem ◽  
...  
Keyword(s):  
Streptococcus Pneumoniae ◽  
Prolyl Isomerase ◽  
Peptidyl Prolyl Isomerase

scholarly journals Preliminary characterization of a cloned neutral isoelectric form of the human peptidyl prolyl isomerase cyclophilin

1991 ◽  
Vol 266 (4) ◽  
pp. 2474-2479
Author(s):  
T F Holzman ◽  
D A Egan ◽  
R Edalji ◽  
R L Simmer ◽  
R Helfrich ◽  
...  
Keyword(s):  
Prolyl Isomerase ◽  
Peptidyl Prolyl Isomerase ◽  
Preliminary Characterization

scholarly journals Nerve Growth Factor Stimulates Interaction of Cayman Ataxia Protein BNIP-H/Caytaxin with Peptidyl-Prolyl Isomerase Pin1 in Differentiating Neurons

PLoS ONE ◽  
2008 ◽  
Vol 3 (7) ◽  
pp. e2686 ◽  
Author(s):  
Jan Paul Buschdorf ◽  
Li Li Chew ◽  
Unice Jim Kim Soh ◽  
Yih-Cherng Liou ◽  
Boon Chuan Low
Keyword(s):  
Nerve Growth Factor ◽  
Growth Factor ◽  
Prolyl Isomerase ◽  
Peptidyl Prolyl Isomerase ◽  
Nerve Growth

Immunophilin AtFKBP13 Sustains All Peptidyl−Prolyl Isomerase Activity in the Thylakoid Lumen fromArabidopsis thalianaDeficient in AtCYP20-2†

Biochemistry ◽  
2007 ◽  
Vol 46 (33) ◽  
pp. 9432-9442 ◽  
Author(s):  
Anna Edvardsson ◽  
Alexey Shapiguzov ◽  
Ulrika A. Petersson ◽  
Wolfgang P. Schröder ◽  
Alexander V. Vener
Keyword(s):  
Prolyl Isomerase ◽  
Peptidyl Prolyl Isomerase ◽  
Thylakoid Lumen ◽  
Isomerase Activity

scholarly journals Regulation of Estrogen Receptor   N-Terminus Conformation and Function by Peptidyl Prolyl Isomerase Pin1

2011 ◽  
Vol 32 (2) ◽  
pp. 445-457 ◽  
Author(s):  
P. Rajbhandari ◽  
G. Finn ◽  
N. M. Solodin ◽  
K. K. Singarapu ◽  
S. C. Sahu ◽  
...  
Keyword(s):  
Estrogen Receptor ◽  
Prolyl Isomerase ◽  
Peptidyl Prolyl Isomerase ◽  
N Terminus ◽  
And Function

scholarly journals Ablation of a peptidyl prolyl isomerase Pin1 from p53-null mice accelerated thymic hyperplasia by increasing the level of the intracellular form of Notch1

Oncogene ◽  
2006 ◽  
Vol 26 (26) ◽  
pp. 3835-3845 ◽  
Author(s):  
K Takahashi ◽  
H Akiyama ◽  
K Shimazaki ◽  
C Uchida ◽  
H Akiyama-Okunuki ◽  
...  
Keyword(s):  
Thymic Hyperplasia ◽  
Prolyl Isomerase ◽  
Peptidyl Prolyl Isomerase ◽  
Intracellular Form

scholarly journals FK506-binding protein FklB is involved in biofilm formation through its peptidyl-prolyl isomerase activity

2020 ◽  
Author(s):  
Chrysoula Zografou ◽  
Maria Dimou ◽  
Panagiotis Katinakis
Keyword(s):  
Biofilm Formation ◽  
Negative Regulator ◽  
Cell Length ◽  
Wild Type ◽  
Prolyl Isomerase ◽  
Ppiase Activity ◽  
Peptidyl Prolyl Isomerase ◽  
Knock Out ◽  
E Coli ◽  
The Mean

AbstractFklB is a member of the FK506-binding proteins (FKBPs), a family that consists of five genes in Escherichia coli. Little is known about the physiological and functional role of FklB in bacterial movement. In the present study, FklB knock-out mutant ΔfklB presented an increased swarming and swimming motility and biofilm formation phenotype, suggesting that FklB is a negative regulator of these cellular processes. Complementation with Peptidyl-prolyl isomerase (PPIase)-deficient fklB gene (Y181A) revealed that the defects in biofilm formation were not restored by Y181A, indicating that PPIase activity of FklB is modulating biofilm formation in E. coli. The mean cell length of ΔfklB swarming cells was significantly smaller as compared to the wild-type BW25113. Furthermore, the mean cell length of swarming and swimming wild-type and ΔfklB cells overexpressing fklB or Y181A was considerably larger, suggesting that PPIase activity of FklB plays a role in cell elongation and/or cell division. A multi-copy suppression assay demonstrated that defects in motility and biofilm phenotype were compensated by overexpressing sets of PPIase-encoding genes. Taken together, our data represent the first report demonstrating the involvement of FklB in cellular functions of E. coli.

scholarly journals The Role of Electrostatics in Enzymes: Do Biomolecular Force Fields Reflect Protein Electric Fields?

2020 ◽  
Author(s):  
Richard T Bradshaw ◽  
Jacek Dziedzic ◽  
Chris-Kriton Skylaris ◽  
Jonathan W. Essex
Keyword(s):  
Electric Fields ◽  
Active Sites ◽  
Catalytic Mechanism ◽  
Force Fields ◽  
Prolyl Isomerase ◽  
Peptidyl Prolyl Isomerase ◽  
Polarizable Force Field ◽  
Polarizable Force Fields ◽  
Protein Active Sites ◽  
Dynamics Simulations

<div><div><div><p>Preorganization of large, directionally oriented, electric fields inside protein active sites has been proposed as a crucial contributor to catalytic mechanism in many enzymes, and may be efficiently investigated at the atomistic level with molecular dynamics simulations. Here we evaluate the ability of the AMOEBA polarizable force field, as well as the additive Amber ff14SB and Charmm C36m models, to describe the electric fields present inside the active site of the peptidyl-prolyl isomerase cyclophilin A. We compare the molecular mechanical electric fields to those calculated with a fully first principles quantum mechanical (QM) representation of the protein, solvent, and ions, and find that AMOEBA consistently shows far greater correlation with the QM electric fields than either of the additive force fields tested. Catalytically-relevant fields calculated with AMOEBA were typically smaller than those observed with additive potentials, but were generally consistent with an electrostatically-driven mechanism for catalysis. Our results highlight the accuracy and the potential advantages of using polarizable force fields in systems where accurate electrostatics may be crucial for providing mechanistic insights.</p></div></div></div>

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