Advanced Search
Display options
Filter resources
Text Availability
Article type
Publication date
Species
Language
Sex
Age
Showing 13 to 24 of 29 entries
Sorted by: Best Match Show Resources per page
How do Chaperones Bind (Partly) Unfolded Client Proteins?.

Frontiers in molecular biosciences

Sučec I, Bersch B, Schanda P.
PMID: 34760928
Front Mol Biosci. 2021 Oct 25;8:762005. doi: 10.3389/fmolb.2021.762005. eCollection 2021.

Molecular chaperones are central to cellular protein homeostasis. Dynamic disorder is a key feature of the complexes of molecular chaperones and their client proteins, and it facilitates the client release towards a folded state or the handover to downstream...

Cite
Sučec I, Bersch B, Schanda P. How do Chaperones Bind (Partly) Unfolded Client Proteins?. Front Mol Biosci. 2021;8:762005doi: 10.3389/fmolb.2021.762005.
Sučec, I., Bersch, B., & Schanda, P. (2021). How do Chaperones Bind (Partly) Unfolded Client Proteins?. Frontiers in molecular biosciences, 8762005. https://doi.org/10.3389/fmolb.2021.762005
Sučec, Iva, et al. "How do Chaperones Bind (Partly) Unfolded Client Proteins?." Frontiers in molecular biosciences vol. 8 (2021): 762005. doi: https://doi.org/10.3389/fmolb.2021.762005
Sučec I, Bersch B, Schanda P. How do Chaperones Bind (Partly) Unfolded Client Proteins?. Front Mol Biosci. 2021 Oct 25;8:762005. doi: 10.3389/fmolb.2021.762005. eCollection 2021. PMID: 34760928; PMCID: PMC8573040.
Copy Download .nbib Format: NLM
Procathepsin and acid phosphatase are stored in Musca domestica yolk spheres.

Journal of insect physiology

Ribolla PE, Bijovsky AT, de Bianchi AG.
PMID: 11119768
J Insect Physiol. 2001 Mar;47(3):225-232. doi: 10.1016/s0022-1910(00)00114-1.

Yolk spheres present in mature invertebrate oocytes are composed of yolk proteins and proteolytic enzymes. In the fly Musca domestica, yolk proteins are degraded during embryogenesis by a cathepsin-like proteinase that is stored as a zymogen. An acid phosphatase...

Cite
Ribolla PE, Bijovsky AT, de Bianchi AG. Procathepsin and acid phosphatase are stored in Musca domestica yolk spheres. J Insect Physiol. 2001;47(3):225-232doi: 10.1016/s0022-1910(00)00114-1.
Ribolla, P. E., Bijovsky, A. T., & de Bianchi AG. (2001). Procathepsin and acid phosphatase are stored in Musca domestica yolk spheres. Journal of insect physiology, 47(3), 225-232. https://doi.org/10.1016/s0022-1910(00)00114-1
Ribolla, et al. "Procathepsin and acid phosphatase are stored in Musca domestica yolk spheres." Journal of insect physiology vol. 47,3 (2001): 225-232. doi: https://doi.org/10.1016/s0022-1910(00)00114-1
Ribolla PE, Bijovsky AT, de Bianchi AG. Procathepsin and acid phosphatase are stored in Musca domestica yolk spheres. J Insect Physiol. 2001 Mar;47(3):225-232. doi: 10.1016/s0022-1910(00)00114-1. PMID: 11119768.
Copy Download .nbib Format: NLM
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...

Cite
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.
Copy Download .nbib Format: NLM
Effects of infusing milk precursors into the artery on rumen fermentation in lactating cows.

Animal nutrition (Zhongguo xu mu shou yi xue hui)

Wang X, Ao C, Khas-Erdene, Liu S, Bai C, Zhang F, Zhang Y, Gao P.
PMID: 29767029
Anim Nutr. 2016 Jun;2(2):105-110. doi: 10.1016/j.aninu.2016.03.002. Epub 2016 Mar 18.

This experiment was conducted to investigate the effects of infusing milk precursors into the external pudic artery on rumen fermentation in lactating dairy cows. Eight multiparous Holstein cows were randomly assigned to Group A (experimental group) and Group B...

Cite
Wang X, Ao C, Khas-Erdene, et al. Effects of infusing milk precursors into the artery on rumen fermentation in lactating cows. Anim Nutr. 2016;2(2):105-110doi: 10.1016/j.aninu.2016.03.002.
Wang, X., Ao, C., Khas-Erdene, Liu, S., Bai, C., Zhang, F., Zhang, Y., & Gao, P. (2016). Effects of infusing milk precursors into the artery on rumen fermentation in lactating cows. Animal nutrition (Zhongguo xu mu shou yi xue hui), 2(2), 105-110. https://doi.org/10.1016/j.aninu.2016.03.002
Wang, Xianjue, et al. "Effects of infusing milk precursors into the artery on rumen fermentation in lactating cows." Animal nutrition (Zhongguo xu mu shou yi xue hui) vol. 2,2 (2016): 105-110. doi: https://doi.org/10.1016/j.aninu.2016.03.002
Wang X, Ao C, Khas-Erdene, Liu S, Bai C, Zhang F, Zhang Y, Gao P. Effects of infusing milk precursors into the artery on rumen fermentation in lactating cows. Anim Nutr. 2016 Jun;2(2):105-110. doi: 10.1016/j.aninu.2016.03.002. Epub 2016 Mar 18. PMID: 29767029; PMCID: PMC5941015.
Copy Download .nbib Format: NLM
Teneurin Structures Are Composed of Ancient Bacterial Protein Domains.

Frontiers in neuroscience

Jackson VA, Busby JN, Janssen BJC, Lott JS, Seiradake E.
PMID: 30930731
Front Neurosci. 2019 Mar 13;13:183. doi: 10.3389/fnins.2019.00183. eCollection 2019.

Pioneering bioinformatic analysis using sequence data revealed that teneurins evolved from bacterial tyrosine-aspartate (YD)-repeat protein precursors. Here, we discuss how structures of the C-terminal domain of teneurins, determined using

Cite
Jackson VA, Busby JN, Janssen BJC, et al. Teneurin Structures Are Composed of Ancient Bacterial Protein Domains. Front Neurosci. 2019;13:183doi: 10.3389/fnins.2019.00183.
Jackson, V. A., Busby, J. N., Janssen, B. J. C., Lott, J. S., & Seiradake, E. (2019). Teneurin Structures Are Composed of Ancient Bacterial Protein Domains. Frontiers in neuroscience, 13183. https://doi.org/10.3389/fnins.2019.00183
Jackson, Verity A, et al. "Teneurin Structures Are Composed of Ancient Bacterial Protein Domains." Frontiers in neuroscience vol. 13 (2019): 183. doi: https://doi.org/10.3389/fnins.2019.00183
Jackson VA, Busby JN, Janssen BJC, Lott JS, Seiradake E. Teneurin Structures Are Composed of Ancient Bacterial Protein Domains. Front Neurosci. 2019 Mar 13;13:183. doi: 10.3389/fnins.2019.00183. eCollection 2019. PMID: 30930731; PMCID: PMC6425310.
Copy Download .nbib Format: NLM
Insights Into the Origin of Life: Did It Begin from HCN and H.

ACS central science

Das T, Ghule S, Vanka K.
PMID: 31572780
ACS Cent Sci. 2019 Sep 25;5(9):1532-1540. doi: 10.1021/acscentsci.9b00520. Epub 2019 Aug 07.

The seminal Urey-Miller experiments showed that molecules crucial to life such as HCN could have formed in the reducing atmosphere of the Hadean Earth and then dissolved in the oceans. Subsequent proponents of the "RNA World" hypothesis have shown...

Cite
Das T, Ghule S, Vanka K. Insights Into the Origin of Life: Did It Begin from HCN and H. ACS Cent Sci. 2019;5(9):1532-1540doi: 10.1021/acscentsci.9b00520.
Das, T., Ghule, S., & Vanka, K. (2019). Insights Into the Origin of Life: Did It Begin from HCN and H. ACS central science, 5(9), 1532-1540. https://doi.org/10.1021/acscentsci.9b00520
Das, Tamal, et al. "Insights Into the Origin of Life: Did It Begin from HCN and H." ACS central science vol. 5,9 (2019): 1532-1540. doi: https://doi.org/10.1021/acscentsci.9b00520
Das T, Ghule S, Vanka K. Insights Into the Origin of Life: Did It Begin from HCN and H. ACS Cent Sci. 2019 Sep 25;5(9):1532-1540. doi: 10.1021/acscentsci.9b00520. Epub 2019 Aug 07. PMID: 31572780; PMCID: PMC6764159.
Copy Download .nbib Format: NLM
Involvement of .

Frontiers in physiology

Elgendy AM, Mohamed AA, Duvic B, Tufail M, Takeda M.
PMID: 34526913
Front Physiol. 2021 Aug 30;12:723072. doi: 10.3389/fphys.2021.723072. eCollection 2021.

Vitellogenins (Vgs) are yolk protein precursors that are regulated by juvenile hormone (JH) and/or 20-hydroxyecdysone (20E) in insects. JH acts as the principal gonadotropin that stimulates vitellogenesis in hemimetabolous insects. In this study, we cloned and characterized the

Cite
Elgendy AM, Mohamed AA, Duvic B, et al. Involvement of . Front Physiol. 2021;12:723072doi: 10.3389/fphys.2021.723072.
Elgendy, A. M., Mohamed, A. A., Duvic, B., Tufail, M., & Takeda, M. (2021). Involvement of . Frontiers in physiology, 12723072. https://doi.org/10.3389/fphys.2021.723072
Elgendy, Azza M, et al. "Involvement of ." Frontiers in physiology vol. 12 (2021): 723072. doi: https://doi.org/10.3389/fphys.2021.723072
Elgendy AM, Mohamed AA, Duvic B, Tufail M, Takeda M. Involvement of . Front Physiol. 2021 Aug 30;12:723072. doi: 10.3389/fphys.2021.723072. eCollection 2021. PMID: 34526913; PMCID: PMC8435907.
Copy Download .nbib Format: NLM
Developmental Biochemistry of Cottonseed Embryogenesis and Germination : XIII. REGULATION OF BIOSYNTHESIS OF PRINCIPAL STORAGE PROTEINS.

Plant physiology

Dure L, Galau GA.
PMID: 16661868
Plant Physiol. 1981 Jul;68(1):187-94. doi: 10.1104/pp.68.1.187.

The synthesis of the principal cottonseed storage proteins during embryogenesis has been followed by analyses of stained protein gels and of fluorographs of protein synthesized in vivo and from purified RNA in vitro in the wheat germ system. The...

Cite
Dure L, Galau GA. Developmental Biochemistry of Cottonseed Embryogenesis and Germination : XIII. REGULATION OF BIOSYNTHESIS OF PRINCIPAL STORAGE PROTEINS. Plant Physiol. 1981;68(1):187-94doi: 10.1104/pp.68.1.187.
Dure, L., & Galau, G. A. (1981). Developmental Biochemistry of Cottonseed Embryogenesis and Germination : XIII. REGULATION OF BIOSYNTHESIS OF PRINCIPAL STORAGE PROTEINS. Plant physiology, 68(1), 187-94. https://doi.org/10.1104/pp.68.1.187
Dure, L, and Galau, G A. "Developmental Biochemistry of Cottonseed Embryogenesis and Germination : XIII. REGULATION OF BIOSYNTHESIS OF PRINCIPAL STORAGE PROTEINS." Plant physiology vol. 68,1 (1981): 187-94. doi: https://doi.org/10.1104/pp.68.1.187
Dure L, Galau GA. Developmental Biochemistry of Cottonseed Embryogenesis and Germination : XIII. REGULATION OF BIOSYNTHESIS OF PRINCIPAL STORAGE PROTEINS. Plant Physiol. 1981 Jul;68(1):187-94. doi: 10.1104/pp.68.1.187. PMID: 16661868; PMCID: PMC425913.
Copy Download .nbib Format: NLM
Four-way regulation of mosquito yolk protein precursor genes by juvenile hormone-, ecdysone-, nutrient-, and insulin-like peptide signaling pathways.

Frontiers in physiology

Hansen IA, Attardo GM, Rodriguez SD, Drake LL.
PMID: 24688471
Front Physiol. 2014 Mar 20;5:103. doi: 10.3389/fphys.2014.00103. eCollection 2014.

Anautogenous mosquito females require a meal of vertebrate blood in order to initiate the production of yolk protein precursors by the fat body. Yolk protein precursor gene expression is tightly repressed in a state-of-arrest before blood meal-related signals activate...

Cite
Hansen IA, Attardo GM, Rodriguez SD, et al. Four-way regulation of mosquito yolk protein precursor genes by juvenile hormone-, ecdysone-, nutrient-, and insulin-like peptide signaling pathways. Front Physiol. 2014;5:103doi: 10.3389/fphys.2014.00103.
Hansen, I. A., Attardo, G. M., Rodriguez, S. D., & Drake, L. L. (2014). Four-way regulation of mosquito yolk protein precursor genes by juvenile hormone-, ecdysone-, nutrient-, and insulin-like peptide signaling pathways. Frontiers in physiology, 5103. https://doi.org/10.3389/fphys.2014.00103
Hansen, Immo A, et al. "Four-way regulation of mosquito yolk protein precursor genes by juvenile hormone-, ecdysone-, nutrient-, and insulin-like peptide signaling pathways." Frontiers in physiology vol. 5 (2014): 103. doi: https://doi.org/10.3389/fphys.2014.00103
Hansen IA, Attardo GM, Rodriguez SD, Drake LL. Four-way regulation of mosquito yolk protein precursor genes by juvenile hormone-, ecdysone-, nutrient-, and insulin-like peptide signaling pathways. Front Physiol. 2014 Mar 20;5:103. doi: 10.3389/fphys.2014.00103. eCollection 2014. PMID: 24688471; PMCID: PMC3960487.
Copy Download .nbib Format: NLM
Proprotein convertase 1/3-mediated down-regulation of brain-derived neurotrophic factor in cortical neurons induced by oxygen-glucose deprivation.

Neural regeneration research

Zhang XY, Liu F, Chen Y, Guo WC, Zhang ZH.
PMID: 31823886
Neural Regen Res. 2020 Jun;15(6):1066-1070. doi: 10.4103/1673-5374.270314.

Brain-derived neurotrophic factor (BDNF) has robust effects on synaptogenesis, neuronal differentiation and synaptic transmission and plasticity. The maturation of BDNF is a complex process. Proprotein convertase 1/3 (PC1/3) has a key role in the cleavage of protein precursors that...

Cite
Zhang XY, Liu F, Chen Y, et al. Proprotein convertase 1/3-mediated down-regulation of brain-derived neurotrophic factor in cortical neurons induced by oxygen-glucose deprivation. Neural Regen Res. 2020;15(6):1066-1070doi: 10.4103/1673-5374.270314.
Zhang, X. Y., Liu, F., Chen, Y., Guo, W. C., & Zhang, Z. H. (2020). Proprotein convertase 1/3-mediated down-regulation of brain-derived neurotrophic factor in cortical neurons induced by oxygen-glucose deprivation. Neural regeneration research, 15(6), 1066-1070. https://doi.org/10.4103/1673-5374.270314
Zhang, Xiang-Yang, et al. "Proprotein convertase 1/3-mediated down-regulation of brain-derived neurotrophic factor in cortical neurons induced by oxygen-glucose deprivation." Neural regeneration research vol. 15,6 (2020): 1066-1070. doi: https://doi.org/10.4103/1673-5374.270314
Zhang XY, Liu F, Chen Y, Guo WC, Zhang ZH. Proprotein convertase 1/3-mediated down-regulation of brain-derived neurotrophic factor in cortical neurons induced by oxygen-glucose deprivation. Neural Regen Res. 2020 Jun;15(6):1066-1070. doi: 10.4103/1673-5374.270314. PMID: 31823886; PMCID: PMC7034267.
Copy Download .nbib Format: NLM
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...

Cite
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.
Copy Download .nbib Format: NLM
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...

Cite
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; PMCID: PMC8745001.
Copy Download .nbib Format: NLM
Showing 13 to 24 of 29 entries