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Topology Engineering of Proteins .

ACS central science

Liu D, Wu WH, Liu YJ, Wu XL, Cao Y, Song B, Li X, Zhang WB.
PMID: 28573210
ACS Cent Sci. 2017 May 24;3(5):473-481. doi: 10.1021/acscentsci.7b00104. Epub 2017 May 10.

Recombinant proteins are traditionally limited to linear configuration. Herein, we report

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Liu D, Wu WH, Liu YJ, et al. Topology Engineering of Proteins . ACS Cent Sci. 2017;3(5):473-481doi: 10.1021/acscentsci.7b00104.
Liu, D., Wu, W. H., Liu, Y. J., Wu, X. L., Cao, Y., Song, B., Li, X., & Zhang, W. B. (2017). Topology Engineering of Proteins . ACS central science, 3(5), 473-481. https://doi.org/10.1021/acscentsci.7b00104
Liu, Dong, et al. "Topology Engineering of Proteins ." ACS central science vol. 3,5 (2017): 473-481. doi: https://doi.org/10.1021/acscentsci.7b00104
Liu D, Wu WH, Liu YJ, Wu XL, Cao Y, Song B, Li X, Zhang WB. Topology Engineering of Proteins . ACS Cent Sci. 2017 May 24;3(5):473-481. doi: 10.1021/acscentsci.7b00104. Epub 2017 May 10. PMID: 28573210; PMCID: PMC5445526.
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Process Analytical Technology for Advanced Process Control in Biologics Manufacturing with the Aid of Macroscopic Kinetic Modeling.

Bioengineering (Basel, Switzerland)

Kornecki M, Strube J.
PMID: 29547557
Bioengineering (Basel). 2018 Mar 16;5(1). doi: 10.3390/bioengineering5010025.

Productivity improvements of mammalian cell culture in the production of recombinant proteins have been made by optimizing cell lines, media, and process operation. This led to enhanced titers and process robustness without increasing the cost of the upstream processing...

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Kornecki M, Strube J. Process Analytical Technology for Advanced Process Control in Biologics Manufacturing with the Aid of Macroscopic Kinetic Modeling. Bioengineering (Basel). 2018;5(1)doi: 10.3390/bioengineering5010025.
Kornecki, M., & Strube, J. (2018). Process Analytical Technology for Advanced Process Control in Biologics Manufacturing with the Aid of Macroscopic Kinetic Modeling. Bioengineering (Basel, Switzerland), 5(1), . https://doi.org/10.3390/bioengineering5010025
Kornecki, Martin, and Strube, Jochen. "Process Analytical Technology for Advanced Process Control in Biologics Manufacturing with the Aid of Macroscopic Kinetic Modeling." Bioengineering (Basel, Switzerland) vol. 5,1 (2018). doi: https://doi.org/10.3390/bioengineering5010025
Kornecki M, Strube J. Process Analytical Technology for Advanced Process Control in Biologics Manufacturing with the Aid of Macroscopic Kinetic Modeling. Bioengineering (Basel). 2018 Mar 16;5(1). doi: 10.3390/bioengineering5010025. PMID: 29547557; PMCID: PMC5874891.
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Human Antibody Fusion Proteins/Antibody Drug Conjugates in Breast and Ovarian Cancer.

Transfusion medicine and hemotherapy : offizielles Organ der Deutschen Gesellschaft fur Transfusionsmedizin und Immunhamatologie

Padayachee ER, Biteghe FAN, Malindi Z, Bauerschlag D, Barth S.
PMID: 29070975
Transfus Med Hemother. 2017 Sep;44(5):303-310. doi: 10.1159/000479979. Epub 2017 Sep 11.

Considerable research efforts have been dedicated to understanding ovarian and breast cancer mechanisms, but there has been little progress translating the research into effective clinical applications. Hence, personalized/precision medicine has emerged because of its potential to improve the accuracy...

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Padayachee ER, Biteghe FAN, Malindi Z, et al. Human Antibody Fusion Proteins/Antibody Drug Conjugates in Breast and Ovarian Cancer. Transfus Med Hemother. 2017;44(5):303-310doi: 10.1159/000479979.
Padayachee, E. R., Biteghe, F. A. N., Malindi, Z., Bauerschlag, D., & Barth, S. (2017). Human Antibody Fusion Proteins/Antibody Drug Conjugates in Breast and Ovarian Cancer. Transfusion medicine and hemotherapy : offizielles Organ der Deutschen Gesellschaft fur Transfusionsmedizin und Immunhamatologie, 44(5), 303-310. https://doi.org/10.1159/000479979
Padayachee, Eden R, et al. "Human Antibody Fusion Proteins/Antibody Drug Conjugates in Breast and Ovarian Cancer." Transfusion medicine and hemotherapy : offizielles Organ der Deutschen Gesellschaft fur Transfusionsmedizin und Immunhamatologie vol. 44,5 (2017): 303-310. doi: https://doi.org/10.1159/000479979
Padayachee ER, Biteghe FAN, Malindi Z, Bauerschlag D, Barth S. Human Antibody Fusion Proteins/Antibody Drug Conjugates in Breast and Ovarian Cancer. Transfus Med Hemother. 2017 Sep;44(5):303-310. doi: 10.1159/000479979. Epub 2017 Sep 11. PMID: 29070975; PMCID: PMC5649269.
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Activity Regulation by Heteromerization of Arabidopsis Allene Oxide Cyclase Family Members.

Plants (Basel, Switzerland)

Otto M, Naumann C, Brandt W, Wasternack C, Hause B.
PMID: 27135223
Plants (Basel). 2016 Jan 06;5(1). doi: 10.3390/plants5010003.

Jasmonates (JAs) are lipid-derived signals in plant stress responses and development. A crucial step in JA biosynthesis is catalyzed by allene oxide cyclase (AOC). Four genes encoding functional AOCs (AOC1, AOC2, AOC3 and AOC4) have been characterized for Arabidopsis...

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Otto M, Naumann C, Brandt W, et al. Activity Regulation by Heteromerization of Arabidopsis Allene Oxide Cyclase Family Members. Plants (Basel). 2016;5(1)doi: 10.3390/plants5010003.
Otto, M., Naumann, C., Brandt, W., Wasternack, C., & Hause, B. (2016). Activity Regulation by Heteromerization of Arabidopsis Allene Oxide Cyclase Family Members. Plants (Basel, Switzerland), 5(1), . https://doi.org/10.3390/plants5010003
Otto, Markus, et al. "Activity Regulation by Heteromerization of Arabidopsis Allene Oxide Cyclase Family Members." Plants (Basel, Switzerland) vol. 5,1 (2016). doi: https://doi.org/10.3390/plants5010003
Otto M, Naumann C, Brandt W, Wasternack C, Hause B. Activity Regulation by Heteromerization of Arabidopsis Allene Oxide Cyclase Family Members. Plants (Basel). 2016 Jan 06;5(1). doi: 10.3390/plants5010003. PMID: 27135223; PMCID: PMC4844422.
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Upscale of recombinant α-L-rhamnosidase production by Pichia pastoris Mut(S) strain.

Frontiers in microbiology

Markošová K, Weignerová L, Rosenberg M, Křen V, Rebroš M.
PMID: 26539173
Front Microbiol. 2015 Oct 19;6:1140. doi: 10.3389/fmicb.2015.01140. eCollection 2015.

Pichia pastoris is currently one of the most preferred microorganisms for recombinant enzyme production due to its efficient expression system. The advantages include the production of high amounts of recombinant proteins containing the appropriate posttranslational modifications and easy cultivation...

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Markošová K, Weignerová L, Rosenberg M, et al. Upscale of recombinant α-L-rhamnosidase production by Pichia pastoris Mut(S) strain. Front Microbiol. 2015;6:1140doi: 10.3389/fmicb.2015.01140.
Markošová, K., Weignerová, L., Rosenberg, M., Křen, V., & Rebroš, M. (2015). Upscale of recombinant α-L-rhamnosidase production by Pichia pastoris Mut(S) strain. Frontiers in microbiology, 61140. https://doi.org/10.3389/fmicb.2015.01140
Markošová, Kristína, et al. "Upscale of recombinant α-L-rhamnosidase production by Pichia pastoris Mut(S) strain." Frontiers in microbiology vol. 6 (2015): 1140. doi: https://doi.org/10.3389/fmicb.2015.01140
Markošová K, Weignerová L, Rosenberg M, Křen V, Rebroš M. Upscale of recombinant α-L-rhamnosidase production by Pichia pastoris Mut(S) strain. Front Microbiol. 2015 Oct 19;6:1140. doi: 10.3389/fmicb.2015.01140. eCollection 2015. PMID: 26539173; PMCID: PMC4611059.
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Recombinant proteins: hopes for tissue engineering.

BioImpacts : BI

Farajollahi MM, Hamzehlou S, Mehdipour A, Samadikuchaksaraei A.
PMID: 23678450
Bioimpacts. 2012;2(3):123-5. doi: 10.5681/bi.2012.010. Epub 2012 Jun 07.

Proteins constitute a group of key molecules with many applications in tissue engineering. Use of proteins provided from natural sources has several limitations which are overcome by the use of recombinant proteins. So far, the recombinant forms of many...

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Farajollahi MM, Hamzehlou S, Mehdipour A, et al. Recombinant proteins: hopes for tissue engineering. Bioimpacts. 2012;2(3):123-5doi: 10.5681/bi.2012.010.
Farajollahi, M. M., Hamzehlou, S., Mehdipour, A., & Samadikuchaksaraei, A. (2012). Recombinant proteins: hopes for tissue engineering. BioImpacts : BI, 2(3), 123-5. https://doi.org/10.5681/bi.2012.010
Farajollahi, Mohammad Morad, et al. "Recombinant proteins: hopes for tissue engineering." BioImpacts : BI vol. 2,3 (2012): 123-5. doi: https://doi.org/10.5681/bi.2012.010
Farajollahi MM, Hamzehlou S, Mehdipour A, Samadikuchaksaraei A. Recombinant proteins: hopes for tissue engineering. Bioimpacts. 2012;2(3):123-5. doi: 10.5681/bi.2012.010. Epub 2012 Jun 07. PMID: 23678450; PMCID: PMC3648934.
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The Induction of Recombinant Protein Bodies in Different Subcellular Compartments Reveals a Cryptic Plastid-Targeting Signal in the 27-kDa γ-Zein Sequence.

Frontiers in bioengineering and biotechnology

Hofbauer A, Peters J, Arcalis E, Rademacher T, Lampel J, Eudes F, Vitale A, Stoger E.
PMID: 25566533
Front Bioeng Biotechnol. 2014 Dec 11;2:67. doi: 10.3389/fbioe.2014.00067. eCollection 2014.

Naturally occurring storage proteins such as zeins are used as fusion partners for recombinant proteins because they induce the formation of ectopic storage organelles known as protein bodies (PBs) where the proteins are stabilized by intermolecular interactions and the...

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Hofbauer A, Peters J, Arcalis E, et al. The Induction of Recombinant Protein Bodies in Different Subcellular Compartments Reveals a Cryptic Plastid-Targeting Signal in the 27-kDa γ-Zein Sequence. Front Bioeng Biotechnol. 2014;2:67doi: 10.3389/fbioe.2014.00067.
Hofbauer, A., Peters, J., Arcalis, E., Rademacher, T., Lampel, J., Eudes, F., Vitale, A., & Stoger, E. (2014). The Induction of Recombinant Protein Bodies in Different Subcellular Compartments Reveals a Cryptic Plastid-Targeting Signal in the 27-kDa γ-Zein Sequence. Frontiers in bioengineering and biotechnology, 267. https://doi.org/10.3389/fbioe.2014.00067
Hofbauer, Anna, et al. "The Induction of Recombinant Protein Bodies in Different Subcellular Compartments Reveals a Cryptic Plastid-Targeting Signal in the 27-kDa γ-Zein Sequence." Frontiers in bioengineering and biotechnology vol. 2 (2014): 67. doi: https://doi.org/10.3389/fbioe.2014.00067
Hofbauer A, Peters J, Arcalis E, Rademacher T, Lampel J, Eudes F, Vitale A, Stoger E. The Induction of Recombinant Protein Bodies in Different Subcellular Compartments Reveals a Cryptic Plastid-Targeting Signal in the 27-kDa γ-Zein Sequence. Front Bioeng Biotechnol. 2014 Dec 11;2:67. doi: 10.3389/fbioe.2014.00067. eCollection 2014. PMID: 25566533; PMCID: PMC4263181.
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Expression Enhancement in Trastuzumab Therapeutic Monoclonal Antibody Production using Genomic Amplification with Methotrexate.

Avicenna journal of medical biotechnology

Akbarzadeh-Sharbaf S, Yakhchali B, Minuchehr Z, Shokrgozar MA, Zeinali S.
PMID: 23799177
Avicenna J Med Biotechnol. 2013 Apr;5(2):87-95.

BACKGROUND: Trastuzumab (Herceptin) is a humanized monoclonal antibody (mAb) which is used for specific treatment of metastatic breast cancer in patients with overexpression of HER2/neu receptor. In this study, we have attempted to develop a biosimilar version of trastuzumab...

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Akbarzadeh-Sharbaf S, Yakhchali B, Minuchehr Z, et al. Expression Enhancement in Trastuzumab Therapeutic Monoclonal Antibody Production using Genomic Amplification with Methotrexate. Avicenna J Med Biotechnol. 2013;5(2):87-95
Akbarzadeh-Sharbaf, S., Yakhchali, B., Minuchehr, Z., Shokrgozar, M. A., & Zeinali, S. (2013). Expression Enhancement in Trastuzumab Therapeutic Monoclonal Antibody Production using Genomic Amplification with Methotrexate. Avicenna journal of medical biotechnology, 5(2), 87-95.
Akbarzadeh-Sharbaf, Soudabeh, et al. "Expression Enhancement in Trastuzumab Therapeutic Monoclonal Antibody Production using Genomic Amplification with Methotrexate." Avicenna journal of medical biotechnology vol. 5,2 (2013): 87-95.
Akbarzadeh-Sharbaf S, Yakhchali B, Minuchehr Z, Shokrgozar MA, Zeinali S. Expression Enhancement in Trastuzumab Therapeutic Monoclonal Antibody Production using Genomic Amplification with Methotrexate. Avicenna J Med Biotechnol. 2013 Apr;5(2):87-95. PMID: 23799177; PMCID: PMC3689561.
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Target-based vs. phenotypic screenings in Leishmania drug discovery: A marriage of convenience or a dialogue of the deaf?.

International journal for parasitology. Drugs and drug resistance

Reguera RM, Calvo-Álvarez E, Alvarez-Velilla R, Balaña-Fouce R.
PMID: 25516847
Int J Parasitol Drugs Drug Resist. 2014 May 22;4(3):355-7. doi: 10.1016/j.ijpddr.2014.05.001. eCollection 2014 Dec.

Drug discovery programs sponsored by public or private initiatives pursue the same ambitious goal: a crushing defeat of major Neglected Tropical Diseases (NTDs) during this decade. Both target-based and target-free screenings have pros and cons when it comes to...

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Reguera RM, Calvo-Álvarez E, Alvarez-Velilla R, et al. Target-based vs. phenotypic screenings in Leishmania drug discovery: A marriage of convenience or a dialogue of the deaf?. Int J Parasitol Drugs Drug Resist. 2014;4(3):355-7doi: 10.1016/j.ijpddr.2014.05.001.
Reguera, R. M., Calvo-Álvarez, E., Alvarez-Velilla, R., & Balaña-Fouce, R. (2014). Target-based vs. phenotypic screenings in Leishmania drug discovery: A marriage of convenience or a dialogue of the deaf?. International journal for parasitology. Drugs and drug resistance, 4(3), 355-7. https://doi.org/10.1016/j.ijpddr.2014.05.001
Reguera, Rosa M, et al. "Target-based vs. phenotypic screenings in Leishmania drug discovery: A marriage of convenience or a dialogue of the deaf?." International journal for parasitology. Drugs and drug resistance vol. 4,3 (2014): 355-7. doi: https://doi.org/10.1016/j.ijpddr.2014.05.001
Reguera RM, Calvo-Álvarez E, Alvarez-Velilla R, Balaña-Fouce R. Target-based vs. phenotypic screenings in Leishmania drug discovery: A marriage of convenience or a dialogue of the deaf?. Int J Parasitol Drugs Drug Resist. 2014 May 22;4(3):355-7. doi: 10.1016/j.ijpddr.2014.05.001. eCollection 2014 Dec. PMID: 25516847; PMCID: PMC4266804.
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Optimization of Ammonium Sulfate Concentration for Purification of Colorectal Cancer Vaccine Candidate Recombinant Protein GA733-FcK Isolated from Plants.

Frontiers in plant science

Park SR, Lim CY, Kim DS, Ko K.
PMID: 26640471
Front Plant Sci. 2015 Nov 27;6:1040. doi: 10.3389/fpls.2015.01040. eCollection 2015.

A protein purification procedure is required to obtain high-value recombinant injectable vaccine proteins produced in plants as a bioreactor. However, existing purification procedures for plant-derived recombinant proteins are often not optimized and are inefficient, with low recovery rates. In...

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Park SR, Lim CY, Kim DS, et al. Optimization of Ammonium Sulfate Concentration for Purification of Colorectal Cancer Vaccine Candidate Recombinant Protein GA733-FcK Isolated from Plants. Front Plant Sci. 2015;6:1040doi: 10.3389/fpls.2015.01040.
Park, S. R., Lim, C. Y., Kim, D. S., & Ko, K. (2015). Optimization of Ammonium Sulfate Concentration for Purification of Colorectal Cancer Vaccine Candidate Recombinant Protein GA733-FcK Isolated from Plants. Frontiers in plant science, 61040. https://doi.org/10.3389/fpls.2015.01040
Park, Se-Ra, et al. "Optimization of Ammonium Sulfate Concentration for Purification of Colorectal Cancer Vaccine Candidate Recombinant Protein GA733-FcK Isolated from Plants." Frontiers in plant science vol. 6 (2015): 1040. doi: https://doi.org/10.3389/fpls.2015.01040
Park SR, Lim CY, Kim DS, Ko K. Optimization of Ammonium Sulfate Concentration for Purification of Colorectal Cancer Vaccine Candidate Recombinant Protein GA733-FcK Isolated from Plants. Front Plant Sci. 2015 Nov 27;6:1040. doi: 10.3389/fpls.2015.01040. eCollection 2015. PMID: 26640471; PMCID: PMC4661270.
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Adjuvant role of Pseudomonas flagellin for Acinetobacter baumannii biofilm associated protein.

World journal of methodology

Sefidi MD, Rasooli I, Owlia P, Talei D, Astaneh SD, Nazarian S.
PMID: 27679782
World J Methodol. 2016 Sep 26;6(3):190-9. doi: 10.5662/wjm.v6.i3.190. eCollection 2016 Sep 26.

AIM: To study immunogenicity of Pseudomonas N terminal flagellin as an adjuvant for Acinetobacter baumannii (A. baumannii) biofilm associated protein (Bap).METHODS: The N terminal flagellin gene was amplified. The pET28a (+) and polymerase chain reaction products were digested with...

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Sefidi MD, Rasooli I, Owlia P, et al. Adjuvant role of Pseudomonas flagellin for Acinetobacter baumannii biofilm associated protein. World J Methodol. 2016;6(3):190-9doi: 10.5662/wjm.v6.i3.190.
Sefidi, M. D., Rasooli, I., Owlia, P., Talei, D., Astaneh, S. D., & Nazarian, S. (2016). Adjuvant role of Pseudomonas flagellin for Acinetobacter baumannii biofilm associated protein. World journal of methodology, 6(3), 190-9. https://doi.org/10.5662/wjm.v6.i3.190
Sefidi, Mozhgan Derakhshan, et al. "Adjuvant role of Pseudomonas flagellin for Acinetobacter baumannii biofilm associated protein." World journal of methodology vol. 6,3 (2016): 190-9. doi: https://doi.org/10.5662/wjm.v6.i3.190
Sefidi MD, Rasooli I, Owlia P, Talei D, Astaneh SD, Nazarian S. Adjuvant role of Pseudomonas flagellin for Acinetobacter baumannii biofilm associated protein. World J Methodol. 2016 Sep 26;6(3):190-9. doi: 10.5662/wjm.v6.i3.190. eCollection 2016 Sep 26. PMID: 27679782; PMCID: PMC5031927.
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Development of Genetically Modified Chinese Hamster Ovary Host Cells for the Enhancement of Recombinant Tissue Plasminogen Activator Expression.

The Malaysian journal of medical sciences : MJMS

Rahimpour A, Ahani R, Najaei A, Adeli A, Barkhordari F, Mahboudi F.
PMID: 27547109
Malays J Med Sci. 2016 Mar;23(2):6-13.

BACKGROUND: Chinese hamster ovary (CHO) cells are the most commonly used host system for the expression of high quality recombinant proteins. However, the development of stable, high-yielding CHO cell lines is a major bottleneck in the industrial manufacturing of...

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Rahimpour A, Ahani R, Najaei A, et al. Development of Genetically Modified Chinese Hamster Ovary Host Cells for the Enhancement of Recombinant Tissue Plasminogen Activator Expression. Malays J Med Sci. 2016;23(2):6-13
Rahimpour, A., Ahani, R., Najaei, A., Adeli, A., Barkhordari, F., & Mahboudi, F. (2016). Development of Genetically Modified Chinese Hamster Ovary Host Cells for the Enhancement of Recombinant Tissue Plasminogen Activator Expression. The Malaysian journal of medical sciences : MJMS, 23(2), 6-13.
Rahimpour, Azam, et al. "Development of Genetically Modified Chinese Hamster Ovary Host Cells for the Enhancement of Recombinant Tissue Plasminogen Activator Expression." The Malaysian journal of medical sciences : MJMS vol. 23,2 (2016): 6-13.
Rahimpour A, Ahani R, Najaei A, Adeli A, Barkhordari F, Mahboudi F. Development of Genetically Modified Chinese Hamster Ovary Host Cells for the Enhancement of Recombinant Tissue Plasminogen Activator Expression. Malays J Med Sci. 2016 Mar;23(2):6-13. PMID: 27547109; PMCID: PMC4976708.
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Showing 13 to 24 of 1326 entries