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Biochemical and Biophysical Research Communications, ISSN 0006-291X, 05/2018, Volume 499, Issue 3, pp. 681 - 687
We searched for inhibitors against prolyl isomerase Pin1 in order to develop functional foods to prevent and cure various Pin1 related diseases such as cancer,... 
Tannic acid | Pin1 | Food polyphenols | Prolyl isomerase | EGCG | Caffeic acid | BIOCHEMISTRY & MOLECULAR BIOLOGY | RISK | CANCER | TEA | BIOPHYSICS | DISEASE | CELL-CYCLE | MICE | INHIBITORS | Index Medicus
Journal Article
EMBO Molecular Medicine, ISSN 1757-4676, 01/2014, Volume 6, Issue 1, pp. 99 - 119
Mammary epithelial stem cells are fundamental to maintain tissue integrity. Cancer stem cells (CSCs) are implicated in both treatment resistance and disease... 
stem cells | breast cancer | Fbxw7 E3 ubiquitin‐ligase | prolyl‐isomerase Pin1 | Notch | Breast cancer | Prolyl-isomerase Pin1 | Fbxw7 E3 ubiquitin-ligase | Stem cells | MEDICINE, RESEARCH & EXPERIMENTAL | APOPTOSIS | ACTIVATION | prolyl-isomerase Pin1 | PHOSPHORYLATION | MOLECULAR HETEROGENEITY | P53 | EPITHELIAL-MESENCHYMAL TRANSITION | THERAPEUTIC TARGET | TUMOR-SUPPRESSOR | GROWTH-FACTOR | F-Box-WD Repeat-Containing Protein 7 | Neoplastic Stem Cells - cytology | Receptors, Notch - metabolism | Humans | Peptidylprolyl Isomerase - antagonists & inhibitors | Receptors, Notch - genetics | Transplantation, Heterologous | Antineoplastic Agents - therapeutic use | Stem Cells - cytology | Stem Cells - metabolism | Breast Neoplasms - metabolism | Neoplastic Stem Cells - metabolism | Triple Negative Breast Neoplasms - pathology | Cell Cycle Proteins - genetics | Female | Peptidylprolyl Isomerase - metabolism | Peptidylprolyl Isomerase - genetics | Proto-Oncogene Proteins - metabolism | Mammary Glands, Human - cytology | Signal Transduction | F-Box Proteins - metabolism | Cell Cycle Proteins - metabolism | Ubiquitin-Protein Ligases - metabolism | Proto-Oncogene Proteins - genetics | NIMA-Interacting Peptidylprolyl Isomerase | Receptor, Notch1 - metabolism | Mice, SCID | Breast Neoplasms - drug therapy | Mice, Knockout | Animals | Breast Neoplasms - pathology | Triple Negative Breast Neoplasms - metabolism | Cell Line, Tumor | Mice | Receptor, Notch1 - genetics | Ubiquitin-Protein Ligases - genetics | F-Box Proteins - genetics | Receptor, Notch4 | Ubiquitin | Ligases | Index Medicus
Journal Article
Journal of Biological Chemistry, ISSN 0021-9258, 07/2017, Volume 292, Issue 28, pp. 11886 - 11895
The prolyl isomerase Pin1 binds to the phosphorylated Ser/Thr-Pro motif of target proteins and enhances their cis-trans conversion. This report is the first to... 
PATHOGENESIS | TRANSCRIPTIONAL ACTIVITY | OBESITY | PROTEIN | ISLET HYPERPLASIA | CYCLIN D1 | COMPENSATION | BIOCHEMISTRY & MOLECULAR BIOLOGY | GROWTH | RESISTANCE | NONALCOHOLIC STEATOHEPATITIS | NIMA-Interacting Peptidylprolyl Isomerase - metabolism | Cell Proliferation | Humans | Diet, High-Fat - adverse effects | NIMA-Interacting Peptidylprolyl Isomerase - antagonists & inhibitors | Recombinant Fusion Proteins - metabolism | Insulin-Secreting Cells - metabolism | NIMA-Interacting Peptidylprolyl Isomerase - chemistry | RNA Interference | Mice, Mutant Strains | Obesity - etiology | Insulin-Secreting Cells - cytology | Binding Sites | Insulin Secretion | Calcium Signaling | Protein-Serine-Threonine Kinases - metabolism | Cell Line | Protein-Serine-Threonine Kinases - genetics | Enzyme Induction | Mice, Transgenic | NIMA-Interacting Peptidylprolyl Isomerase - genetics | Recombinant Fusion Proteins - chemistry | Mice, Knockout | Obesity - metabolism | Obesity - pathology | Insulin - metabolism | Animals | Recombinant Fusion Proteins - genetics | Diet, Carbohydrate Loading - adverse effects | Protein-Serine-Threonine Kinases - chemistry | Mutation | Amino Acid Substitution | Insulin-Secreting Cells - enzymology | Index Medicus | pancreatic islet | salt inducible kinase | cell proliferation | prolyl isomerase | insulin secretion | Metabolism | diabetes
Journal Article
Bioorganic & Medicinal Chemistry Letters, ISSN 0960-894X, 02/2019, Volume 29, Issue 3, pp. 353 - 356
Pin1 (protein interacting with never in mitosis A-1) is a member of the peptidyl prolyl isomerase (PPIase) family, and catalyzes - isomerization of... 
Covalent bond | Cysteine | Michael acceptor | Irreversible inhibition | Peptidyl prolyl isomerase | TARGET | CHEMISTRY, MEDICINAL | ACID | STRUCTURAL BASIS | ISOMERIZATION | CHEMISTRY, ORGANIC | CANCER | Enzyme inhibitors | Proteases | Prostate cancer | Bonds | Isomerization
Journal Article
Biochemical and Biophysical Research Communications, ISSN 0006-291X, 02/2018, Volume 497, Issue 1, pp. 388 - 393
A prolyl isomerase Pin1 deficient (Pin1 ) male mice had severe testicular atrophy. We investigated the function of Pin1 in spermatogenesis by analyzing the... 
Testis | Spermatogonial stem cell | GFRα1 | Prolyl isomerase | Cell cycle | BIOCHEMISTRY & MOLECULAR BIOLOGY | SELF-RENEWAL | PROLIFERATION | PLZF | P53 | BIOPHYSICS | GFR alpha 1 | GDNF | MICE | Index Medicus
Journal Article
Scientific Reports, ISSN 2045-2322, 04/2017, Volume 7, Issue 1, pp. 45915 - 45915
Journal Article
Journal of Molecular Biology, ISSN 0022-2836, 12/2018, Volume 430, Issue 24, pp. 5169 - 5181
Human Pin1 is a peptidyl prolyl / isomerase with a unique preference for phosphorylated Ser/Thr-Pro substrate motifs. Here we report that MCM3 (minichromosome... 
MCM3 | Pin1 | prolyl isomerase | cell cycle | phosphorylation | Proline | DNA replication | Chromatin | Peptides | Isomerization | Protein binding
Journal Article
Journal Article
Oncogene, ISSN 0950-9232, 06/2012, Volume 31, Issue 23, pp. 2876 - 2887
Pin1 regulates a subset of phosphoproteins by isomerizing phospho-Ser/Thr-Pro motifs via a 'post-phosphorylation' mechanism. Here, we characterize TR3 as a... 
prolyl isomerase pin1 | cell proliferation | phosphorylation | orphan receptor TR3 | APOPTOSIS | COACTIVATOR RECRUITMENT | CANCER CELL | BIOCHEMISTRY & MOLECULAR BIOLOGY | N-TERMINAL KINASE | CELL BIOLOGY | NGFI-B | ONCOLOGY | NEGATIVE REGULATION | SUBSTRATE | GROWTH-FACTORS | GENETICS & HEREDITY | NUR77 | RNA, Small Interfering - genetics | Cyclin D2 - metabolism | Phosphorylation | Cell Proliferation | Immunoprecipitation | Luciferases - metabolism | Stereoisomerism | Humans | Chromatin Immunoprecipitation | Peptidylprolyl Isomerase - metabolism | Electrophoretic Mobility Shift Assay | Peptidylprolyl Isomerase - genetics | Nuclear Receptor Subfamily 4, Group A, Member 1 - genetics | Nuclear Receptor Subfamily 4, Group A, Member 1 - chemistry | Signal Transduction | NIMA-Interacting Peptidylprolyl Isomerase | E2F1 Transcription Factor - metabolism | Dipeptides - chemistry | Blotting, Western | p300-CBP Transcription Factors - metabolism | Animals | Mitosis - physiology | Mice, Nude | Nuclear Receptor Subfamily 4, Group A, Member 1 - metabolism | Mice | Mice, Inbred BALB C | HeLa Cells | Mitogen-Activated Protein Kinase 1 - metabolism | Physiological aspects | Isomerases | Research | Mitosis | Health aspects | Proteins | Cell division | Enzymes | Oncology | Tumors | Index Medicus | Cell proliferation | Peptidylprolyl isomerase | Phosphoproteins | Isomerization | Extracellular signal-regulated kinase | cyclin D2 | Pin1 protein | Promoters | orphan nuclear receptors
Journal Article