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 Activity and Affinity of Pin1 Variants

2019 ◽  
Author(s):  
Alexandra Born ◽  
Morkos A. Henen ◽  
Beat Vögeli
Keyword(s):  
Catalytic Activity ◽  
Ligand Binding ◽  
Binding Site ◽  
Structure And Function ◽  
Ligand Binding Site ◽  
Prolyl Isomerase ◽  
Peptidyl Prolyl Isomerase ◽  
Isomerase Activity ◽  
Ppiase Domain ◽  
And Function

Pin1 is a peptidyl-prolyl isomerase responsible for isomerizing phosphorylated S/T-P motifs. Pin1 has two domains that each have a distinct ligand binding site, but only its PPIase domain has catalytic activity. Vast evidence supports interdomain allostery of Pin1, with binding of a ligand to its regulatory WW domain impacting activity in the PPIase domain. Many diverse studies have made mutations in Pin1 in order to elucidate interactions that are responsible for ligand binding, isomerase activity, and interdomain allostery. Here, we summarize these mutations and their impact on Pin1’s structure and function.

scholarly journals Peptidyl‐Prolyl Isomerase 1 Regulates Ca 2+ Handling by Modulating Sarco(Endo)Plasmic Reticulum Calcium ATPase and Na 2+ /Ca 2+ Exchanger 1 Protein Levels and Function

2017 ◽  
Vol 6 (10) ◽  
Author(s):  
Veronica Sacchi ◽  
Bingyan J. Wang ◽  
Dieter Kubli ◽  
Alexander S. Martinez ◽  
Jung‐Kang Jin ◽  
...  
Keyword(s):  
Calcium Atpase ◽  
Prolyl Isomerase ◽  
Peptidyl Prolyl Isomerase ◽  
Protein Levels ◽  
Plasmic Reticulum ◽  
And Function

scholarly journals Activity and Affinity of Pin1 Variants

Molecules ◽  
2019 ◽  
Vol 25 (1) ◽  
pp. 36
Author(s):  
Alexandra Born ◽  
Morkos A. Henen ◽  
Beat Vögeli
Keyword(s):  
Catalytic Activity ◽  
Ligand Binding ◽  
Binding Site ◽  
Structure And Function ◽  
Ligand Binding Site ◽  
Prolyl Isomerase ◽  
Peptidyl Prolyl Isomerase ◽  
Isomerase Activity ◽  
Ppiase Domain ◽  
And Function

Pin1 is a peptidyl-prolyl isomerase responsible for isomerizing phosphorylated S/T-P motifs. Pin1 has two domains that each have a distinct ligand binding site, but only its PPIase domain has catalytic activity. Vast evidence supports interdomain allostery of Pin1, with binding of a ligand to its regulatory WW domain impacting activity in the PPIase domain. Many diverse studies have made mutations in Pin1 in order to elucidate interactions that are responsible for ligand binding, isomerase activity, and interdomain allostery. Here, we summarize these mutations and their impact on Pin1′s structure and function.

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 Expression and Function of Estrogen Receptor Subtypes in Granulosa Cells: Regulation by Estradiol and Forskolin1

Endocrinology ◽  
1999 ◽  
Vol 140 (9) ◽  
pp. 4320-4334 ◽  
Author(s):  
S. Chidananda Sharma ◽  
Jeffrey W. Clemens ◽  
Margareta D. Pisarska ◽  
JoAnne S. Richards
Keyword(s):  
Estrogen Receptor ◽  
Granulosa Cells ◽  
Receptor Subtypes ◽  
And Function

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
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