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Showing 13 to 22 of 22 entries
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A Recombinant Trivalent Fusion Protein F1-LcrV-HSP70(II) Augments Humoral and Cellular Immune Responses and Imparts Full Protection against Yersinia pestis.

Frontiers in microbiology

Verma SK, Batra L, Tuteja U.
PMID: 27458447
Front Microbiol. 2016 Jul 05;7:1053. doi: 10.3389/fmicb.2016.01053. eCollection 2016.

Plague is one of the most dangerous infections in humans caused by Yersinia pestis, a Gram-negative bacterium. Despite of an overwhelming research success, no ideal vaccine against plague is available yet. It is well established that F1/LcrV based vaccine...

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Verma SK, Batra L, Tuteja U. A Recombinant Trivalent Fusion Protein F1-LcrV-HSP70(II) Augments Humoral and Cellular Immune Responses and Imparts Full Protection against Yersinia pestis. Front Microbiol. 2016;7:1053doi: 10.3389/fmicb.2016.01053.
Verma, S. K., Batra, L., & Tuteja, U. (2016). A Recombinant Trivalent Fusion Protein F1-LcrV-HSP70(II) Augments Humoral and Cellular Immune Responses and Imparts Full Protection against Yersinia pestis. Frontiers in microbiology, 71053. https://doi.org/10.3389/fmicb.2016.01053
Verma, Shailendra K, et al. "A Recombinant Trivalent Fusion Protein F1-LcrV-HSP70(II) Augments Humoral and Cellular Immune Responses and Imparts Full Protection against Yersinia pestis." Frontiers in microbiology vol. 7 (2016): 1053. doi: https://doi.org/10.3389/fmicb.2016.01053
Verma SK, Batra L, Tuteja U. A Recombinant Trivalent Fusion Protein F1-LcrV-HSP70(II) Augments Humoral and Cellular Immune Responses and Imparts Full Protection against Yersinia pestis. Front Microbiol. 2016 Jul 05;7:1053. doi: 10.3389/fmicb.2016.01053. eCollection 2016. PMID: 27458447; PMCID: PMC4932849.
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Extending recombinant factor IX Fc fusion protein dosing interval to 14 or more days in patients with hemophilia B.

Research and practice in thrombosis and haemostasis

Shapiro AD, Pasi KJ, Ozelo MC, Kulkarni R, Barnowski C, Winding B, Szamosi J, Lethagen S.
PMID: 30656283
Res Pract Thromb Haemost. 2018 Nov 29;3(1):109-113. doi: 10.1002/rth2.12163. eCollection 2019 Jan.

BACKGROUND: In the phase 3 B-LONG study (NCT01027364), prophylaxis with recombinant factor IX Fc fusion protein (rFIXFc) every 7 to >14 days was associated with low annualized bleed rates (ABRs) in males aged ≥12 years with severe hemophilia B....

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Shapiro AD, Pasi KJ, Ozelo MC, et al. Extending recombinant factor IX Fc fusion protein dosing interval to 14 or more days in patients with hemophilia B. Res Pract Thromb Haemost. 2018;3(1):109-113doi: 10.1002/rth2.12163.
Shapiro, A. D., Pasi, K. J., Ozelo, M. C., Kulkarni, R., Barnowski, C., Winding, B., Szamosi, J., & Lethagen, S. (2019). Extending recombinant factor IX Fc fusion protein dosing interval to 14 or more days in patients with hemophilia B. Research and practice in thrombosis and haemostasis, 3(1), 109-113. https://doi.org/10.1002/rth2.12163
Shapiro, Amy D, et al. "Extending recombinant factor IX Fc fusion protein dosing interval to 14 or more days in patients with hemophilia B." Research and practice in thrombosis and haemostasis vol. 3,1 (2019): 109-113. doi: https://doi.org/10.1002/rth2.12163
Shapiro AD, Pasi KJ, Ozelo MC, Kulkarni R, Barnowski C, Winding B, Szamosi J, Lethagen S. Extending recombinant factor IX Fc fusion protein dosing interval to 14 or more days in patients with hemophilia B. Res Pract Thromb Haemost. 2018 Nov 29;3(1):109-113. doi: 10.1002/rth2.12163. eCollection 2019 Jan. PMID: 30656283; PMCID: PMC6332734.
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Bioluminescent fusion conjugates and bioluminescent immunoassays: 1988-1998.

Luminescence : the journal of biological and chemical luminescence

Kricka LJ, Stroebel J, Stanley PE.
PMID: 10398559
Luminescence. 1999 Jan;14(1):39-46. doi: 10.1002/(SICI)1522-7243(199901/02)14:1<39::AID-BIO515>3.0.CO;2-Y.

The first part of this survey focuses on immunoassays and related ligand:binder assays (receptor:ligand, DNA probe) that use either a luciferase or a photoprotein as a label. In addition, references to assays that use a conventional label detected using...

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Kricka LJ, Stroebel J, Stanley PE. Bioluminescent fusion conjugates and bioluminescent immunoassays: 1988-1998. Luminescence. 1999;14(1):39-46doi: 10.1002/(SICI)1522-7243(199901/02)14:1<39::AID-BIO515>3.0.CO;2-Y.
Kricka, L. J., Stroebel, J., & Stanley, P. E. (1999). Bioluminescent fusion conjugates and bioluminescent immunoassays: 1988-1998. Luminescence : the journal of biological and chemical luminescence, 14(1), 39-46. https://doi.org/10.1002/(SICI)1522-7243(199901/02)14:1<39::AID-BIO515>3.0.CO;2-Y
Kricka, et al. "Bioluminescent fusion conjugates and bioluminescent immunoassays: 1988-1998." Luminescence : the journal of biological and chemical luminescence vol. 14,1 (1999): 39-46. doi: https://doi.org/10.1002/(SICI)1522-7243(199901/02)14:1<39::AID-BIO515>3.0.CO;2-Y
Kricka LJ, Stroebel J, Stanley PE. Bioluminescent fusion conjugates and bioluminescent immunoassays: 1988-1998. Luminescence. 1999 Jan;14(1):39-46. doi: 10.1002/(SICI)1522-7243(199901/02)14:1<39::AID-BIO515>3.0.CO;2-Y. PMID: 10398559.
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The use of recombinant fusion proteases in the affinity purification of recombinant proteins.

Methods in molecular medicine

Leong LE.
PMID: 21390852
Methods Mol Med. 1998;13:323-9. doi: 10.1385/0-89603-485-2:323.

At present the protein expression systems used commonly by researchers incorporate an affinity tail fused to the protein of interest. These affinity tails provide a convenient and efficient method for the purification of the expressed fusion protein using affinity...

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Leong LE. The use of recombinant fusion proteases in the affinity purification of recombinant proteins. Methods Mol Med. 1998;13:323-9doi: 10.1385/0-89603-485-2:323.
Leong, L. E. (1998). The use of recombinant fusion proteases in the affinity purification of recombinant proteins. Methods in molecular medicine, 13323-9. https://doi.org/10.1385/0-89603-485-2:323
Leong, L E. "The use of recombinant fusion proteases in the affinity purification of recombinant proteins." Methods in molecular medicine vol. 13 (1998): 323-9. doi: https://doi.org/10.1385/0-89603-485-2:323
Leong LE. The use of recombinant fusion proteases in the affinity purification of recombinant proteins. Methods Mol Med. 1998;13:323-9. doi: 10.1385/0-89603-485-2:323. PMID: 21390852.
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Antigenicity and immunogenicity of recombinant proteins comprising African swine fever virus proteins p30 and p54 fused to a cell-penetrating peptide.

International immunopharmacology

Zhang G, Liu W, Gao Z, Yang S, Zhou G, Chang Y, Ma Y, Liang X, Shao J, Chang H.
PMID: 34715492
Int Immunopharmacol. 2021 Dec;101:108251. doi: 10.1016/j.intimp.2021.108251. Epub 2021 Oct 29.

African swine fever (ASF) is a highly fatal swine disease threatening the global pig industry. Currently, vaccine is not commercially available for ASF. Hence, it is desirable to develop effective subunit vaccines against ASF. Here, we expressed and purified...

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Zhang G, Liu W, Gao Z, et al. Antigenicity and immunogenicity of recombinant proteins comprising African swine fever virus proteins p30 and p54 fused to a cell-penetrating peptide. Int Immunopharmacol. 2021;101:108251doi: 10.1016/j.intimp.2021.108251.
Zhang, G., Liu, W., Gao, Z., Yang, S., Zhou, G., Chang, Y., Ma, Y., Liang, X., Shao, J., & Chang, H. (2021). Antigenicity and immunogenicity of recombinant proteins comprising African swine fever virus proteins p30 and p54 fused to a cell-penetrating peptide. International immunopharmacology, 101108251. https://doi.org/10.1016/j.intimp.2021.108251
Zhang, Guanglei, et al. "Antigenicity and immunogenicity of recombinant proteins comprising African swine fever virus proteins p30 and p54 fused to a cell-penetrating peptide." International immunopharmacology vol. 101 (2021): 108251. doi: https://doi.org/10.1016/j.intimp.2021.108251
Zhang G, Liu W, Gao Z, Yang S, Zhou G, Chang Y, Ma Y, Liang X, Shao J, Chang H. Antigenicity and immunogenicity of recombinant proteins comprising African swine fever virus proteins p30 and p54 fused to a cell-penetrating peptide. Int Immunopharmacol. 2021 Dec;101:108251. doi: 10.1016/j.intimp.2021.108251. Epub 2021 Oct 29. PMID: 34715492.
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The development of human serum albumin-based drugs and relevant fusion proteins for cancer therapy.

International journal of biological macromolecules

Tao HY, Wang RQ, Sheng WJ, Zhen YS.
PMID: 34284054
Int J Biol Macromol. 2021 Sep 30;187:24-34. doi: 10.1016/j.ijbiomac.2021.07.080. Epub 2021 Jul 17.

Human serum albumin (HSA)-based therapeutics have attracted tremendous attention in the development of anticancer agents. The versatile properties of HSA make HSA-based therapeutics possess improved pharmacokinetics, extended circulation half-life, enhanced efficacy, reduced toxicity, etc. Generally, the HSA-based therapeutics systems...

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Tao HY, Wang RQ, Sheng WJ, et al. The development of human serum albumin-based drugs and relevant fusion proteins for cancer therapy. Int J Biol Macromol. 2021;187:24-34doi: 10.1016/j.ijbiomac.2021.07.080.
Tao, H. Y., Wang, R. Q., Sheng, W. J., & Zhen, Y. S. (2021). The development of human serum albumin-based drugs and relevant fusion proteins for cancer therapy. International journal of biological macromolecules, 18724-34. https://doi.org/10.1016/j.ijbiomac.2021.07.080
Tao, Hong-Yu, et al. "The development of human serum albumin-based drugs and relevant fusion proteins for cancer therapy." International journal of biological macromolecules vol. 187 (2021): 24-34. doi: https://doi.org/10.1016/j.ijbiomac.2021.07.080
Tao HY, Wang RQ, Sheng WJ, Zhen YS. The development of human serum albumin-based drugs and relevant fusion proteins for cancer therapy. Int J Biol Macromol. 2021 Sep 30;187:24-34. doi: 10.1016/j.ijbiomac.2021.07.080. Epub 2021 Jul 17. PMID: 34284054.
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Transgenic plants expressing ω-ACTX-Hv1a and snowdrop lectin (GNA) fusion protein show enhanced resistance to aphids.

Frontiers in plant science

Nakasu EY, Edwards MG, Fitches E, Gatehouse JA, Gatehouse AM.
PMID: 25506351
Front Plant Sci. 2014 Nov 28;5:673. doi: 10.3389/fpls.2014.00673. eCollection 2014.

Recombinant fusion proteins containing arthropod toxins have been developed as a new class of biopesticides. The recombinant fusion protein Hv1a/GNA, containing the spider venom toxin ω-ACTX-Hv1a linked to snowdrop lectin (GNA) was shown to reduce survival of the peach-potato...

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Nakasu EY, Edwards MG, Fitches E, et al. Transgenic plants expressing ω-ACTX-Hv1a and snowdrop lectin (GNA) fusion protein show enhanced resistance to aphids. Front Plant Sci. 2014;5:673doi: 10.3389/fpls.2014.00673.
Nakasu, E. Y., Edwards, M. G., Fitches, E., Gatehouse, J. A., & Gatehouse, A. M. (2014). Transgenic plants expressing ω-ACTX-Hv1a and snowdrop lectin (GNA) fusion protein show enhanced resistance to aphids. Frontiers in plant science, 5673. https://doi.org/10.3389/fpls.2014.00673
Nakasu, Erich Y T, et al. "Transgenic plants expressing ω-ACTX-Hv1a and snowdrop lectin (GNA) fusion protein show enhanced resistance to aphids." Frontiers in plant science vol. 5 (2014): 673. doi: https://doi.org/10.3389/fpls.2014.00673
Nakasu EY, Edwards MG, Fitches E, Gatehouse JA, Gatehouse AM. Transgenic plants expressing ω-ACTX-Hv1a and snowdrop lectin (GNA) fusion protein show enhanced resistance to aphids. Front Plant Sci. 2014 Nov 28;5:673. doi: 10.3389/fpls.2014.00673. eCollection 2014. PMID: 25506351; PMCID: PMC4246675.
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Outcome of Clinical Trials with New Extended Half-Life FVIII/IX Concentrates.

Journal of clinical medicine

Mancuso ME, Santagostino E.
PMID: 28350322
J Clin Med. 2017 Mar 28;6(4). doi: 10.3390/jcm6040039.

The development of a new generation of coagulation factors with improved pharmacokinetic profile will change the paradigm of treatment of persons with hemophilia (PWH). The standard treatment in PWH is represented by regular long-term prophylaxis that, given intravenously twice...

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Mancuso ME, Santagostino E. Outcome of Clinical Trials with New Extended Half-Life FVIII/IX Concentrates. J Clin Med. 2017;6(4)doi: 10.3390/jcm6040039.
Mancuso, M. E., & Santagostino, E. (2017). Outcome of Clinical Trials with New Extended Half-Life FVIII/IX Concentrates. Journal of clinical medicine, 6(4), . https://doi.org/10.3390/jcm6040039
Mancuso, Maria Elisa, and Santagostino, Elena. "Outcome of Clinical Trials with New Extended Half-Life FVIII/IX Concentrates." Journal of clinical medicine vol. 6,4 (2017). doi: https://doi.org/10.3390/jcm6040039
Mancuso ME, Santagostino E. Outcome of Clinical Trials with New Extended Half-Life FVIII/IX Concentrates. J Clin Med. 2017 Mar 28;6(4). doi: 10.3390/jcm6040039. PMID: 28350322; PMCID: PMC5406771.
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Newcastle Disease Virus Hemagglutinin Neuraminidase as a Potential Cancer Targeting Agent.

Journal of Cancer

Baradaran A, Yusoff K, Shafee N, Rahim RA.
PMID: 26918060
J Cancer. 2016 Jan 29;7(4):462-6. doi: 10.7150/jca.13566. eCollection 2016.

The hemagglutinin-neuraminidase (HN) protein of Newcastle disease virus (NDV) with its immunotherapeutic activities and sialic acid binding abilities is a promising cancer adjuvant. The HN was surfaced displayed on Lactococcus lactis and its cancer targeting ability was investigated via...

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Baradaran A, Yusoff K, Shafee N, et al. Newcastle Disease Virus Hemagglutinin Neuraminidase as a Potential Cancer Targeting Agent. J Cancer. 2016;7(4):462-6doi: 10.7150/jca.13566.
Baradaran, A., Yusoff, K., Shafee, N., & Rahim, R. A. (2016). Newcastle Disease Virus Hemagglutinin Neuraminidase as a Potential Cancer Targeting Agent. Journal of Cancer, 7(4), 462-6. https://doi.org/10.7150/jca.13566
Baradaran, Ali, et al. "Newcastle Disease Virus Hemagglutinin Neuraminidase as a Potential Cancer Targeting Agent." Journal of Cancer vol. 7,4 (2016): 462-6. doi: https://doi.org/10.7150/jca.13566
Baradaran A, Yusoff K, Shafee N, Rahim RA. Newcastle Disease Virus Hemagglutinin Neuraminidase as a Potential Cancer Targeting Agent. J Cancer. 2016 Jan 29;7(4):462-6. doi: 10.7150/jca.13566. eCollection 2016. PMID: 26918060; PMCID: PMC4749367.
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Characterizing the putative mitogen-activated protein kinase (.

Biotechnology reports (Amsterdam, Netherlands)

Kumar RR, Dubey K, Arora K, Dalal M, Rai GK, Mishra D, Chaturvedi KK, Rai A, Kumar SN, Singh B, Chinnusamy V, Praveen S.
PMID: 33659194
Biotechnol Rep (Amst). 2021 Feb 05;29:e00597. doi: 10.1016/j.btre.2021.e00597. eCollection 2021 Mar.

Wheat, being sensitive to terminal heat, causes drastic reduction in grain quality and yield. MAPK cascade regulates the network of defense mechanism operated inside plant system. Here, we have identified 21 novel MAPKs through gel-based proteomics and RNA-seq data...

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Kumar RR, Dubey K, Arora K, et al. Characterizing the putative mitogen-activated protein kinase (. Biotechnol Rep (Amst). 2021;29:e00597doi: 10.1016/j.btre.2021.e00597.
Kumar, R. R., Dubey, K., Arora, K., Dalal, M., Rai, G. K., Mishra, D., Chaturvedi, K. K., Rai, A., Kumar, S. N., Singh, B., Chinnusamy, V., & Praveen, S. (2021). Characterizing the putative mitogen-activated protein kinase (. Biotechnology reports (Amsterdam, Netherlands), 29e00597. https://doi.org/10.1016/j.btre.2021.e00597
Kumar, Ranjeet R, et al. "Characterizing the putative mitogen-activated protein kinase (." Biotechnology reports (Amsterdam, Netherlands) vol. 29 (2021): e00597. doi: https://doi.org/10.1016/j.btre.2021.e00597
Kumar RR, Dubey K, Arora K, Dalal M, Rai GK, Mishra D, Chaturvedi KK, Rai A, Kumar SN, Singh B, Chinnusamy V, Praveen S. Characterizing the putative mitogen-activated protein kinase (. Biotechnol Rep (Amst). 2021 Feb 05;29:e00597. doi: 10.1016/j.btre.2021.e00597. eCollection 2021 Mar. PMID: 33659194; PMCID: PMC7890154.
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Showing 13 to 22 of 22 entries