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PH domain and leucine rich repeat protein phosphatase 1

This gene encodes a member of the serine/threonine phosphatase family. The encoded protein promotes apoptosis by dephosphorylating and inactivating the serine/threonine kinase Akt, and functions as a tumor suppressor in multiple types of cancer. Increased expression of this gene may also play a role in obesity and type 2 diabetes by interfering with Akt-mediated insulin signaling. [provided by RefSeq, Dec 2011] (from NCBI)
Top mentioned proteins: CAN, SET, ACID, OUT, Presenilin-1
Papers using SCOP antibodies
Support vector machine classification on the web
Sætrom Pål et al., In BMC Bioinformatics, 2003
... The first column gives SCOP sequence IDs; the first row identifies ...
The pymol molecular graphics system
Nussinov Ruth, In PLoS Computational Biology, 2001
... , we do not consider intra-chain interactions, (ii) SCOP domains spanning several protein chains involved in the binding site are excluded from the ...
Papers on SCOP
Molecular modeling, mutational analysis and conformational switching in IL27: An in silico structural insight towards AIDS research.
Ray et al., Durgāpur, India. In Gene, Feb 2016
Though huge RMSD variations were observed on superimposing the MT structures on WT individually, the MTs were examined to share similar SCOP/CATH fold with TM-score=0.8, indicating that they retained their functionality even after mutation.
PASS2 database for the structure-based sequence alignment of distantly related SCOP domain superfamilies: update to version 5 and added features.
Sowdhamini et al., Bengaluru, India. In Nucleic Acids Res, Feb 2016
Structure-based sequence alignment is an essential step in assessing and analysing the relationship of distantly related proteins.
Visualizing global properties of a molecular dynamics trajectory.
Makowski et al., Boston, United States. In Proteins, Jan 2016
Comparison of sigma-r plots calculated from 10 ns trajectories of proteins representing the four major SCOP fold classes indicates diversity of dynamic behaviors which are recognizably different among the four classes.
The history of the CATH structural classification of protein domains.
Orengo et al., London, United Kingdom. In Biochimie, Dec 2015
Together with the SCOP database, CATH remains comprehensive and reasonably up-to-date with the now more than 100,000 protein structures in the PDB.
TAPO: A combined method for the identification of tandem repeats in protein structures.
Kajava et al., Montpellier, France. In Febs Lett, Oct 2015
Databases focused on structure classifications (PDB, SCOP, CATH) do not provide an easy solution for selection of these structures from PDB.
An Integrated Framework for Functional Annotation of Protein Structural Domains.
Chen et al., In Ieee/acm Trans Comput Biol Bioinform, Jul 2015
In this article, we present Structural Domain Annotation (SDA), a novel computational approach to predict functions for SCOP structural domains.
Internal symmetry in protein structures: prevalence, functional relevance and evolution.
Balaji, Cambridge, United Kingdom. In Curr Opin Struct Biol, Jun 2015
Based on the results from these methods, about 20% of SCOP folds, superfamilies and families are estimated to have structures with internal symmetry (Figure 1d).
Precise assembly of complex beta sheet topologies from de novo designed building blocks.
Baker et al., Seattle, United States. In Elife, 2014
Searches for similar structures in the SCOP protein domain database yield only weak matches with different beta sheet connectivities.
An assessment of catalytic residue 3D ensembles for the prediction of enzyme function.
Merkl et al., Hagen, Germany. In Bmc Bioinformatics, 2014
RESULTS: We have analyzed the SCOP database on the superfamily level in order to estimate the number of non-homologous enzymes possessing the same function according to their EC number.
Extending Protein Domain Boundary Predictors to Detect Discontinuous Domains.
Wang et al., Wuhan, China. In Plos One, 2014
Discontinuous domains are predicted by matching the sequence profile of concatenated continuous domain segments with the profiles from a single-domain library derived from SCOP and CATH, and Pfam.
Improving Protein Fold Recognition by Deep Learning Networks.
Cheng et al., Columbia, United States. In Sci Rep, 2014
We evaluated the performance of DN-Fold along with 18 different methods on Lindahl's benchmark dataset and on a large benchmark set extracted from SCOP 1.75 consisting of about one million protein pairs, at three different levels of fold recognition (i.e., protein family, superfamily, and fold) depending on the evolutionary distance between protein sequences.
Mechanisms and consequences of the loss of PHLPP1 phosphatase in chronic lymphocytic leukemia (CLL).
Handel et al., In Leukemia, 2012
Loss of PHLPP1 is associated with chronic lymphocytic leukemia.
USP1 regulates AKT phosphorylation by modulating the stability of PHLPP1 in lung cancer cells.
Yuepeng et al., Xinxiang, China. In J Cancer Res Clin Oncol, 2012
a novel USP1-PHLPP1-Akt signaling axis, and decreased USP1 level in lung cancer cells may play an important role in lung cancer progress.
Pleckstrin homology domain leucine-rich repeat protein phosphatase (PHLPP): a new player in cell signaling.
Newton et al., San Diego, United States. In J Biol Chem, 2012
PHLPP as a novel tumor suppressor.
The phosphatase PHLPP1 regulates Akt2, promotes pancreatic cancer cell death, and inhibits tumor formation.
Gukovskaya et al., Los Angeles, United States. In Gastroenterology, 2012
PHLPP1 has tumor suppressive activity and might represent a therapeutic or diagnostic tool for pancreatic ductal adenocarcinoma.
Ras-associating domain proteins: a new class of cyclic nucleotide-gated channel modulators.
Rajala et al., Oklahoma City, United States. In Adv Exp Med Biol, 2011
PHLPP1 and PHLPP2 have an effect on retinal rod CNG channel sensitivity.
Structural classification of proteins and structural genomics: new insights into protein folding and evolution.
Murzin et al., Cambridge, United Kingdom. In Acta Crystallogr Sect F Struct Biol Cryst Commun, 2010
During the past decade, the Protein Structure Initiative (PSI) centres have become major contributors of new families, superfamilies and folds to the Structural Classification of Proteins (SCOP) database.
SCOP/PHLPP and its functional role in the brain.
Storm et al., Tokyo, Japan. In Mol Biosyst, 2010
SCOP (suprachiasmatic nucleus (SCN) circadian oscillatory protein) was originally identified in 1999 in a differential display screen of the rat SCN for genes whose expression were regulated in a circadian manner (K.
Proteolytic degradation of SCOP in the hippocampus contributes to activation of MAP kinase and memory.
Storm et al., Seattle, United States. In Cell, 2007
To determine if hippocampus-dependent memory is influenced by SCOP in vivo, a transgenic mouse strain was generated for the inducible overexpression of SCOP in the forebrain; overexpression SCOP completely blocked memory for novel objects.
SCOPing out proteases in long-term memory.
Bolshakov, Belmont, United States. In Cell, 2007
In this issue, Shimizu et al. (2007) provide new insight into the regulation of this pathway by demonstrating that activation of MAP kinase occurs through the calcium-dependent degradation of SCOP (suprachiasmatic nucleus circadian oscillatory protein) by the protease calpain.
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