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Rational Redesign of Inhibitors of Furin/kexin Processing Proteases.

Sheng wu hua xue yu sheng wu wu li xue bao Acta biochimica et biophysica Sinica

Ye YZ, Fei H, Ding DF.
PMID: 12040390
Sheng Wu Hua Xue Yu Sheng Wu Wu Li Xue Bao (Shanghai). 2001;33(5):504-512.

Furin/kexin processing proteases catalyze the proteolysis of large protein precursors involved in many biological processes, such as zymogen activation, peptide hormone synthesis, viral protein processing and receptor maturation, making them potential targets for therapeutic agents. Herein, homology modeling and...

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Ye YZ, Fei H, Ding DF. Rational Redesign of Inhibitors of Furin/kexin Processing Proteases. Sheng Wu Hua Xue Yu Sheng Wu Wu Li Xue Bao (Shanghai). 2001;33(5):504-512
Ye, Y. Z., Fei, H., & Ding, D. F. (2001). Rational Redesign of Inhibitors of Furin/kexin Processing Proteases. Sheng wu hua xue yu sheng wu wu li xue bao Acta biochimica et biophysica Sinica, 33(5), 504-512.
Ye, Yu-Zhen, et al. "Rational Redesign of Inhibitors of Furin/kexin Processing Proteases." Sheng wu hua xue yu sheng wu wu li xue bao Acta biochimica et biophysica Sinica vol. 33,5 (2001): 504-512.
Ye YZ, Fei H, Ding DF. Rational Redesign of Inhibitors of Furin/kexin Processing Proteases. Sheng Wu Hua Xue Yu Sheng Wu Wu Li Xue Bao (Shanghai). 2001;33(5):504-512. PMID: 12040390.
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A Vacuolar-Type H+-ATPase in a Nonvacuolar Organelle Is Required for the Sorting of Soluble Vacuolar Protein Precursors in Tobacco Cells.

The Plant cell

Matsuoka K, Higuchi T, Maeshima M, Nakamura K.
PMID: 12237363
Plant Cell. 1997 Apr;9(4):533-546. doi: 10.1105/tpc.9.4.533.

In plant cells, vacuolar matrix proteins are separated from the secretory proteins at the Golgi complex for transport to the vacuoles. To investigate the involvement of vacuolar-type ATPase (V-ATPase) in the vacuolar targeting of soluble proteins, we analyzed the...

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Matsuoka K, Higuchi T, Maeshima M, et al. A Vacuolar-Type H+-ATPase in a Nonvacuolar Organelle Is Required for the Sorting of Soluble Vacuolar Protein Precursors in Tobacco Cells. Plant Cell. 1997;9(4):533-546doi: 10.1105/tpc.9.4.533.
Matsuoka, K., Higuchi, T., Maeshima, M., & Nakamura, K. (1997). A Vacuolar-Type H+-ATPase in a Nonvacuolar Organelle Is Required for the Sorting of Soluble Vacuolar Protein Precursors in Tobacco Cells. The Plant cell, 9(4), 533-546. https://doi.org/10.1105/tpc.9.4.533
Matsuoka, K., et al. "A Vacuolar-Type H+-ATPase in a Nonvacuolar Organelle Is Required for the Sorting of Soluble Vacuolar Protein Precursors in Tobacco Cells." The Plant cell vol. 9,4 (1997): 533-546. doi: https://doi.org/10.1105/tpc.9.4.533
Matsuoka K, Higuchi T, Maeshima M, Nakamura K. A Vacuolar-Type H+-ATPase in a Nonvacuolar Organelle Is Required for the Sorting of Soluble Vacuolar Protein Precursors in Tobacco Cells. Plant Cell. 1997 Apr;9(4):533-546. doi: 10.1105/tpc.9.4.533. PMID: 12237363; PMCID: PMC156937.
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Creatine-induced activation of antioxidative defence in myotube cultures revealed by explorative NMR-based metabonomics and proteomics.

Journal of the International Society of Sports Nutrition

Young JF, Larsen LB, Malmendal A, Nielsen NC, Straadt IK, Oksbjerg N, Bertram HC.
PMID: 20205771
J Int Soc Sports Nutr. 2010 Feb 04;7(1):9. doi: 10.1186/1550-2783-7-9.

BACKGROUND: Creatine is a key intermediate in energy metabolism and supplementation of creatine has been used for increasing muscle mass, strength and endurance. Creatine supplementation has also been reported to trigger the skeletal muscle expression of insulin like growth...

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Young JF, Larsen LB, Malmendal A, et al. Creatine-induced activation of antioxidative defence in myotube cultures revealed by explorative NMR-based metabonomics and proteomics. J Int Soc Sports Nutr. 2010;7(1):9doi: 10.1186/1550-2783-7-9.
Young, J. F., Larsen, L. B., Malmendal, A., Nielsen, N. C., Straadt, I. K., Oksbjerg, N., & Bertram, H. C. (2010). Creatine-induced activation of antioxidative defence in myotube cultures revealed by explorative NMR-based metabonomics and proteomics. Journal of the International Society of Sports Nutrition, 7(1), 9. https://doi.org/10.1186/1550-2783-7-9
Young, Jette F, et al. "Creatine-induced activation of antioxidative defence in myotube cultures revealed by explorative NMR-based metabonomics and proteomics." Journal of the International Society of Sports Nutrition vol. 7,1 (2010): 9. doi: https://doi.org/10.1186/1550-2783-7-9
Young JF, Larsen LB, Malmendal A, Nielsen NC, Straadt IK, Oksbjerg N, Bertram HC. Creatine-induced activation of antioxidative defence in myotube cultures revealed by explorative NMR-based metabonomics and proteomics. J Int Soc Sports Nutr. 2010 Feb 04;7(1):9. doi: 10.1186/1550-2783-7-9. PMID: 20205771; PMCID: PMC2822831.
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Crystal structure of the severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) frameshifting pseudoknot.

RNA (New York, N.Y.)

Jones CP, Ferre-D'Amare AR.
PMID: 34845084
RNA. 2021 Nov 29; doi: 10.1261/rna.078825.121. Epub 2021 Nov 29.

SARS-CoV-2 produces two long viral protein precursors from one open reading frame using a highly conserved RNA pseudoknot that enhances programmed -1 ribosomal frameshifting. The 1.3 Å-resolution X-ray structure of the pseudoknot reveals three coaxially stacked helices buttressed by...

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Jones CP, Ferre-D'Amare AR. Crystal structure of the severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) frameshifting pseudoknot. RNA. 2021;doi: 10.1261/rna.078825.121.
Jones, C. P., & Ferre-D'Amare, A. R. (2021). Crystal structure of the severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) frameshifting pseudoknot. RNA (New York, N.Y.), . https://doi.org/10.1261/rna.078825.121
Jones, Christopher P, and Ferre-D'Amare, Adrian R. "Crystal structure of the severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) frameshifting pseudoknot." RNA (New York, N.Y.) vol. (2021). doi: https://doi.org/10.1261/rna.078825.121
Jones CP, Ferre-D'Amare AR. Crystal structure of the severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) frameshifting pseudoknot. RNA. 2021 Nov 29; doi: 10.1261/rna.078825.121. Epub 2021 Nov 29. PMID: 34845084.
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The proprotein convertase furin in cancer: more than an oncogene.

Oncogene

He Z, Khatib AM, Creemers JWM.
PMID: 34997216
Oncogene. 2022 Jan 07; doi: 10.1038/s41388-021-02175-9. Epub 2022 Jan 07.

Furin is the first discovered proprotein convertase member and is present in almost all mammalian cells. Therefore, by regulating the maturation of a wide range of proproteins, Furin expression and/or activity is involved in various physiological and pathophysiological processes...

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He Z, Khatib AM, Creemers JWM. The proprotein convertase furin in cancer: more than an oncogene. Oncogene. 2022;doi: 10.1038/s41388-021-02175-9.
He, Z., Khatib, A. M., & Creemers, J. W. M. (2022). The proprotein convertase furin in cancer: more than an oncogene. Oncogene, . https://doi.org/10.1038/s41388-021-02175-9
He, Zongsheng, et al. "The proprotein convertase furin in cancer: more than an oncogene." Oncogene vol. (2022). doi: https://doi.org/10.1038/s41388-021-02175-9
He Z, Khatib AM, Creemers JWM. The proprotein convertase furin in cancer: more than an oncogene. Oncogene. 2022 Jan 07; doi: 10.1038/s41388-021-02175-9. Epub 2022 Jan 07. PMID: 34997216.
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Peptidome: Chaos or Inevitability.

International journal of molecular sciences

Lyapina I, Ivanov V, Fesenko I.
PMID: 34884929
Int J Mol Sci. 2021 Dec 04;22(23). doi: 10.3390/ijms222313128.

Thousands of naturally occurring peptides differing in their origin, abundance and possible functions have been identified in the tissue and biological fluids of vertebrates, insects, fungi, plants and bacteria. These peptide pools are referred to as intracellular or extracellular...

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Lyapina I, Ivanov V, Fesenko I. Peptidome: Chaos or Inevitability. Int J Mol Sci. 2021;22(23)doi: 10.3390/ijms222313128.
Lyapina, I., Ivanov, V., & Fesenko, I. (2021). Peptidome: Chaos or Inevitability. International journal of molecular sciences, 22(23), . https://doi.org/10.3390/ijms222313128
Lyapina, Irina, et al. "Peptidome: Chaos or Inevitability." International journal of molecular sciences vol. 22,23 (2021). doi: https://doi.org/10.3390/ijms222313128
Lyapina I, Ivanov V, Fesenko I. Peptidome: Chaos or Inevitability. Int J Mol Sci. 2021 Dec 04;22(23). doi: 10.3390/ijms222313128. PMID: 34884929; PMCID: PMC8658490.
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Elucidating the endogenous synovial fluid proteome and peptidome of inflammatory arthritis using label-free mass spectrometry.

Clinical proteomics

Mahendran SM, Keystone EC, Krawetz RJ, Liang K, Diamandis EP, Chandran V.
PMID: 31160890
Clin Proteomics. 2019 May 30;16:23. doi: 10.1186/s12014-019-9243-3. eCollection 2019.

BACKGROUND: Inflammatory arthritis (IA) is an immunological disorder in which loss of immune tolerance to endogenous self-antigens perpetuates synovitis and eventual destruction of the underlying cartilage and bone. Pathological changes in the joint are expected to be represented by...

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Mahendran SM, Keystone EC, Krawetz RJ, et al. Elucidating the endogenous synovial fluid proteome and peptidome of inflammatory arthritis using label-free mass spectrometry. Clin Proteomics. 2019;16:23doi: 10.1186/s12014-019-9243-3.
Mahendran, S. M., Keystone, E. C., Krawetz, R. J., Liang, K., Diamandis, E. P., & Chandran, V. (2019). Elucidating the endogenous synovial fluid proteome and peptidome of inflammatory arthritis using label-free mass spectrometry. Clinical proteomics, 1623. https://doi.org/10.1186/s12014-019-9243-3
Mahendran, Shalini M, et al. "Elucidating the endogenous synovial fluid proteome and peptidome of inflammatory arthritis using label-free mass spectrometry." Clinical proteomics vol. 16 (2019): 23. doi: https://doi.org/10.1186/s12014-019-9243-3
Mahendran SM, Keystone EC, Krawetz RJ, Liang K, Diamandis EP, Chandran V. Elucidating the endogenous synovial fluid proteome and peptidome of inflammatory arthritis using label-free mass spectrometry. Clin Proteomics. 2019 May 30;16:23. doi: 10.1186/s12014-019-9243-3. eCollection 2019. PMID: 31160890; PMCID: PMC6542032.
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Duodenal amyloidosis secondary to ulcerative colitis.

Intestinal research

Park SW, Jee SR, Kim JH, Lee SH, Hwang JW, Jang JG, Lee DW, Seol SY.
PMID: 29422811
Intest Res. 2018 Jan;16(1):151-154. doi: 10.5217/ir.2018.16.1.151. Epub 2018 Jan 18.

Amyloidosis is defined as the extracellular deposition of non-branching fibrils composed of a variety of serum-protein precursors. Secondary amyloidosis is associated with several chronic inflammatory conditions, such as rheumatologic or intestinal diseases, familial Mediterranean fever, or chronic infectious diseases,...

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Park SW, Jee SR, Kim JH, et al. Duodenal amyloidosis secondary to ulcerative colitis. Intest Res. 2018;16(1):151-154doi: 10.5217/ir.2018.16.1.151.
Park, S. W., Jee, S. R., Kim, J. H., Lee, S. H., Hwang, J. W., Jang, J. G., Lee, D. W., & Seol, S. Y. (2018). Duodenal amyloidosis secondary to ulcerative colitis. Intestinal research, 16(1), 151-154. https://doi.org/10.5217/ir.2018.16.1.151
Park, Seung Woon, et al. "Duodenal amyloidosis secondary to ulcerative colitis." Intestinal research vol. 16,1 (2018): 151-154. doi: https://doi.org/10.5217/ir.2018.16.1.151
Park SW, Jee SR, Kim JH, Lee SH, Hwang JW, Jang JG, Lee DW, Seol SY. Duodenal amyloidosis secondary to ulcerative colitis. Intest Res. 2018 Jan;16(1):151-154. doi: 10.5217/ir.2018.16.1.151. Epub 2018 Jan 18. PMID: 29422811; PMCID: PMC5797263.
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A nuclear factor-binding domain in the 5'-untranslated region of the amyloid precursor protein promoter: implications for the regulation of gene expression.

BMC research notes

Vostrov AA, Taheny MJ, Izkhakov N, Quitschke WW.
PMID: 20205906
BMC Res Notes. 2010 Jan 12;3:4. doi: 10.1186/1756-0500-3-4.

BACKGROUND: The extracellular deposition of aggregated amyloid beta-protein is a neuropathological manifestation of Alzheimer disease and Down syndrome. The Amyloid beta-protein is derived from a group of larger differentially spliced proteins, the amyloid protein precursors (APP). Data suggests that...

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Vostrov AA, Taheny MJ, Izkhakov N, et al. A nuclear factor-binding domain in the 5'-untranslated region of the amyloid precursor protein promoter: implications for the regulation of gene expression. BMC Res Notes. 2010;3:4doi: 10.1186/1756-0500-3-4.
Vostrov, A. A., Taheny, M. J., Izkhakov, N., & Quitschke, W. W. (2010). A nuclear factor-binding domain in the 5'-untranslated region of the amyloid precursor protein promoter: implications for the regulation of gene expression. BMC research notes, 34. https://doi.org/10.1186/1756-0500-3-4
Vostrov, Alexander A, et al. "A nuclear factor-binding domain in the 5'-untranslated region of the amyloid precursor protein promoter: implications for the regulation of gene expression." BMC research notes vol. 3 (2010): 4. doi: https://doi.org/10.1186/1756-0500-3-4
Vostrov AA, Taheny MJ, Izkhakov N, Quitschke WW. A nuclear factor-binding domain in the 5'-untranslated region of the amyloid precursor protein promoter: implications for the regulation of gene expression. BMC Res Notes. 2010 Jan 12;3:4. doi: 10.1186/1756-0500-3-4. PMID: 20205906; PMCID: PMC2828463.
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Cytoplasmic chaperones in precursor targeting to mitochondria: the role of MSF and hsp 70.

Trends in cell biology

Mihara K, Omura T.
PMID: 15157486
Trends Cell Biol. 1996 Mar;6(3):104-8. doi: 10.1016/0962-8924(96)81000-2.

Despite extensive study since the early 1980s, the mechanism by which newly synthesized protein precursors are unfolded in the cytoplasm and targeted correctly to the mitochondrial surface prior to translocation through the mitochondrial membranes is understood poorly. Recently, an...

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Mihara K, Omura T. Cytoplasmic chaperones in precursor targeting to mitochondria: the role of MSF and hsp 70. Trends Cell Biol. 1996;6(3):104-8doi: 10.1016/0962-8924(96)81000-2.
Mihara, K., & Omura, T. (1996). Cytoplasmic chaperones in precursor targeting to mitochondria: the role of MSF and hsp 70. Trends in cell biology, 6(3), 104-8. https://doi.org/10.1016/0962-8924(96)81000-2
Mihara, K, and Omura, T. "Cytoplasmic chaperones in precursor targeting to mitochondria: the role of MSF and hsp 70." Trends in cell biology vol. 6,3 (1996): 104-8. doi: https://doi.org/10.1016/0962-8924(96)81000-2
Mihara K, Omura T. Cytoplasmic chaperones in precursor targeting to mitochondria: the role of MSF and hsp 70. Trends Cell Biol. 1996 Mar;6(3):104-8. doi: 10.1016/0962-8924(96)81000-2. PMID: 15157486.
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Altered islet prohormone processing: a cause or consequence of diabetes?.

Physiological reviews

Ramzy A, Kieffer TJ.
PMID: 34280055
Physiol Rev. 2022 Jan 01;102(1):155-208. doi: 10.1152/physrev.00008.2021. Epub 2021 Jul 19.

Peptide hormones are first produced as larger precursor prohormones that require endoproteolytic cleavage to liberate the mature hormones. A structurally conserved but functionally distinct family of nine prohormone convertase enzymes (PCs) are responsible for cleavage of protein precursors, of...

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Ramzy A, Kieffer TJ. Altered islet prohormone processing: a cause or consequence of diabetes?. Physiol Rev. 2021;102(1):155-208doi: 10.1152/physrev.00008.2021.
Ramzy, A., & Kieffer, T. J. (2022). Altered islet prohormone processing: a cause or consequence of diabetes?. Physiological reviews, 102(1), 155-208. https://doi.org/10.1152/physrev.00008.2021
Ramzy, Adam, and Kieffer, Timothy J. "Altered islet prohormone processing: a cause or consequence of diabetes?." Physiological reviews vol. 102,1 (2022): 155-208. doi: https://doi.org/10.1152/physrev.00008.2021
Ramzy A, Kieffer TJ. Altered islet prohormone processing: a cause or consequence of diabetes?. Physiol Rev. 2022 Jan 01;102(1):155-208. doi: 10.1152/physrev.00008.2021. Epub 2021 Jul 19. PMID: 34280055.
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Cytosolic Quality Control of Mitochondrial Protein Precursors-The Early Stages of the Organelle Biogenesis.

International journal of molecular sciences

Lenkiewicz AM, Krakowczyk M, Bragoszewski P.
PMID: 35008433
Int J Mol Sci. 2021 Dec 21;23(1). doi: 10.3390/ijms23010007.

With few exceptions, proteins that constitute the proteome of mitochondria originate outside of this organelle in precursor forms. Such protein precursors follow dedicated transportation paths to reach specific parts of mitochondria, where they complete their maturation and perform their...

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Lenkiewicz AM, Krakowczyk M, Bragoszewski P. Cytosolic Quality Control of Mitochondrial Protein Precursors-The Early Stages of the Organelle Biogenesis. Int J Mol Sci. 2021;23(1)doi: 10.3390/ijms23010007.
Lenkiewicz, A. M., Krakowczyk, M., & Bragoszewski, P. (2021). Cytosolic Quality Control of Mitochondrial Protein Precursors-The Early Stages of the Organelle Biogenesis. International journal of molecular sciences, 23(1), . https://doi.org/10.3390/ijms23010007
Lenkiewicz, Anna M, et al. "Cytosolic Quality Control of Mitochondrial Protein Precursors-The Early Stages of the Organelle Biogenesis." International journal of molecular sciences vol. 23,1 (2021). doi: https://doi.org/10.3390/ijms23010007
Lenkiewicz AM, Krakowczyk M, Bragoszewski P. Cytosolic Quality Control of Mitochondrial Protein Precursors-The Early Stages of the Organelle Biogenesis. Int J Mol Sci. 2021 Dec 21;23(1). doi: 10.3390/ijms23010007. PMID: 35008433.
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Showing 1 to 12 of 29 entries