Experimental Analysis of E2BB (LTIIb) Signal Peptide in Secretory Production of Reteplase in Escherichia coli

[1]  Reteplase , 2020, Reactions Weekly.

[2]  Y. Ghasemi,et al.  Experimental Evaluation of In Silico Selected Signal Peptides for Secretory Expression of Erwinia Asparaginase in Escherichia coli , 2019, International Journal of Peptide Research and Therapeutics.

[3]  H. Mir Mohammad Sadeghi,et al.  Optimization of Fermentation Conditions for Reteplase Expression by Escherichia coli Using Response Surface Methodology , 2019, Avicenna journal of medical biotechnology.

[4]  H. Sadeghpour,et al.  Double domain polyethylenimine-based nanoparticles for integrin receptor mediated delivery of plasmid DNA , 2018, Scientific Reports.

[5]  Xiao-yang Pang,et al.  Development an effective system to expression recombinant protein in E. coli via comparison and optimization of signal peptides: Expression of Pseudomonas fluorescens BJ-10 thermostable lipase as case study , 2018, Microbial Cell Factories.

[6]  Y. Ghasemi,et al.  In silico Analysis of Several Signal Peptides for the Excretory Production of Reteplase in Escherichia coli , 2017 .

[7]  Jaya Prakash,et al.  Basic and Applied Aspects of Biotechnology , 2017 .

[8]  G. King,et al.  A Strategy for Production of Correctly Folded Disulfide-Rich Peptides in the Periplasm of E. coli. , 2017, Methods in molecular biology.

[9]  Pratyoosh Shukla,et al.  Advanced technologies for improved expression of recombinant proteins in bacteria: perspectives and applications , 2016, Critical reviews in biotechnology.

[10]  Y. Ghasemi,et al.  Evaluation of Recombinant Human Growth Hormone Secretion in E. coli using the L-asparaginase II Signal Peptide , 2016, Avicenna journal of medical biotechnology.

[11]  N. Maghsoudi,et al.  Comparison of Three Escherichia coli Strains in Recombinant Production of Reteplase , 2016, Avicenna journal of medical biotechnology.

[12]  Mohammad Hossein Morowvat,et al.  Optimization of Fermentation Conditions for Recombinant Human Interferon Beta Production by Escherichia coli Using the Response Surface Methodology , 2015, Jundishapur journal of microbiology.

[13]  Md. Ramjan Ali,et al.  Aspect of Thrombolytic Therapy: A Review , 2014, TheScientificWorldJournal.

[14]  Germán L. Rosano,et al.  Recombinant protein expression in Escherichia coli: advances and challenges , 2014, Front. Microbiol..

[15]  R. Freedman,et al.  High‐level secretion of a recombinant protein to the culture medium with a Bacillus subtilis twin‐arginine translocation system in Escherichia coli , 2013, The FEBS journal.

[16]  M. Rabbani,et al.  COMPARISON OF THE CYTOPLASMIC AND PERIPLASMIC PRODUCTION OF RETEPLASE IN Escherichia coli , 2013, Preparative biochemistry & biotechnology.

[17]  Bharat V. Adkar,et al.  Effect of Signal Peptide on Stability and Folding of Escherichia coli Thioredoxin , 2013, PloS one.

[18]  Kheng Oon Low,et al.  Optimisation of signal peptide for recombinant protein secretion in bacterial hosts , 2013, Applied Microbiology and Biotechnology.

[19]  A. Chowdhury,et al.  Critical Factors Affecting the Success of Cloning, Expression, and Mass Production of Enzymes by Recombinant E. coli , 2012, ISRN biotechnology.

[20]  M. Shokrgozar,et al.  Expression of the recombinant plasminogen activator (reteplase) by a non-lytic insect cell expression system , 2013, Research in pharmaceutical sciences.

[21]  Jianzhi Zhang,et al.  Balanced Codon Usage Optimizes Eukaryotic Translational Efficiency , 2012, PLoS genetics.

[22]  S. Brunak,et al.  SignalP 4.0: discriminating signal peptides from transmembrane regions , 2011, Nature Methods.

[23]  Thomas Rattei,et al.  Effective—a database of predicted secreted bacterial proteins , 2010, Nucleic Acids Res..

[24]  R. Rahim,et al.  Screening for the optimal induction parameters for periplasmic producing interferon-2b in Escherichia coli , 2010 .

[25]  B. Nam,et al.  N-terminal pI determines the solubility of a recombinant protein lacking an internal transmembrane-like domain in E. coli , 2010, Molecules and cells.

[26]  Suman Bandyopadhyay,et al.  Asn12 and Asn278: Critical Residues for In Vitro Biological Activity of Reteplase , 2010, Advances in hematology.

[27]  S. Yoon,et al.  Secretory production of recombinant proteins in Escherichia coli. , 2010, Recent patents on biotechnology.

[28]  Pierre Baldi,et al.  SOLpro: accurate sequence-based prediction of protein solubility , 2009, Bioinform..

[29]  F. Mergulhão,et al.  Analysis of factors affecting the periplasmic production of recombinant proteins in Escherichia coli. , 2007, Journal of microbiology and biotechnology.

[30]  S. Idicula-Thomas,et al.  Protein aggregation : A perspective from amyloid and inclusion-body formation , 2007 .

[31]  Changkai Zhang,et al.  Cloning, Expression, and Renaturation Studies of Reteplase , 2003 .

[32]  J. Fareed,et al.  The Role of Thrombolytic Drugs in the Management of Acute Myocardial Infarction and Stroke. , 2002, Turkish journal of haematology : official journal of Turkish Society of Haematology.

[33]  Shen Zi-long Cloning and Expression of Tissue-Type Plasminogen Activator Mutant Reteplase(r-PA) in E. coli. , 2002 .

[34]  J. Manosroi,et al.  Secretion of Active Recombinant Human Tissue Plasminogen Activator Derivatives in Escherichia coli , 2001, Applied and Environmental Microbiology.

[35]  A. Luzier,et al.  Reteplase: A New Thrombolytic for the Treatment of Acute Myocardial Infarction , 1999, The Annals of pharmacotherapy.

[36]  M. Jobling,et al.  Construction and characterization of versatile cloning vectors for efficient delivery of native foreign proteins to the periplasm of Escherichia coli. , 1997, Plasmid.

[37]  J. Pagés,et al.  Expression vector promoting the synthesis and export of the human growth-hormone-releasing factor in Escherichia coli. , 1987, Gene.

[38]  U. K. Laemmli,et al.  Cleavage of Structural Proteins during the Assembly of the Head of Bacteriophage T4 , 1970, Nature.

[39]  L. Heppel,et al.  The release of enzymes by osmotic shock from Escherichia coli in exponential phase. , 1966, The Journal of biological chemistry.