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Showing 25 to 29 of 29 entries
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Assembly of cell-wall glycoproteins of Chlamydomonas reinhardii: Oligosaccharides are added in medial and trans Golgi compartments.

Planta

Grief C, Shaw PJ.
PMID: 24227429
Planta. 1987 Jul;171(3):302-12. doi: 10.1007/BF00398675.

A series of monoclonal antibodies and a polyclonal antiserum have been used to investigate the localisation and pathway of biosynthesis of the cell-wall hydroxyproline-rich glycoprotein 2BII in the alga Chlamydomonas reinhardii. Glyco-protein precursors were detected within the endoplasmic reticulum...

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Grief C, Shaw PJ. Assembly of cell-wall glycoproteins of Chlamydomonas reinhardii: Oligosaccharides are added in medial and trans Golgi compartments. Planta. 1987;171(3):302-12doi: 10.1007/BF00398675.
Grief, C., & Shaw, P. J. (1987). Assembly of cell-wall glycoproteins of Chlamydomonas reinhardii: Oligosaccharides are added in medial and trans Golgi compartments. Planta, 171(3), 302-12. https://doi.org/10.1007/BF00398675
Grief, C, and Shaw, P J. "Assembly of cell-wall glycoproteins of Chlamydomonas reinhardii: Oligosaccharides are added in medial and trans Golgi compartments." Planta vol. 171,3 (1987): 302-12. doi: https://doi.org/10.1007/BF00398675
Grief C, Shaw PJ. Assembly of cell-wall glycoproteins of Chlamydomonas reinhardii: Oligosaccharides are added in medial and trans Golgi compartments. Planta. 1987 Jul;171(3):302-12. doi: 10.1007/BF00398675. PMID: 24227429.
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Storage protein accumulation patterns in somatic embryos of cotton (Gossypium hirsutum L.).

Plant cell reports

Shoemaker RC, Christofferson SE, Galbraith DW.
PMID: 24248439
Plant Cell Rep. 1987 Feb;6(1):12-5. doi: 10.1007/BF00269728.

The storage protein content of somatic embryos of Gossypium hirsutum L. cv. Coker 201 was determined using extinction level, antigen/antibody association detection methods. Mature storage protein was first detected in early globular-stage somatic embryos at a total concentration of...

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Shoemaker RC, Christofferson SE, Galbraith DW. Storage protein accumulation patterns in somatic embryos of cotton (Gossypium hirsutum L.). Plant Cell Rep. 1987;6(1):12-5doi: 10.1007/BF00269728.
Shoemaker, R. C., Christofferson, S. E., & Galbraith, D. W. (1987). Storage protein accumulation patterns in somatic embryos of cotton (Gossypium hirsutum L.). Plant cell reports, 6(1), 12-5. https://doi.org/10.1007/BF00269728
Shoemaker, R C, et al. "Storage protein accumulation patterns in somatic embryos of cotton (Gossypium hirsutum L.)." Plant cell reports vol. 6,1 (1987): 12-5. doi: https://doi.org/10.1007/BF00269728
Shoemaker RC, Christofferson SE, Galbraith DW. Storage protein accumulation patterns in somatic embryos of cotton (Gossypium hirsutum L.). Plant Cell Rep. 1987 Feb;6(1):12-5. doi: 10.1007/BF00269728. PMID: 24248439.
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Loss of Proprotein Convertase Furin in Mammary Gland Impairs proIGF1R and proIR Processing and Suppresses Tumorigenesis in Triple Negative Breast Cancer.

Cancers

He Z, Khatib AM, Creemers JWM.
PMID: 32962246
Cancers (Basel). 2020 Sep 20;12(9). doi: 10.3390/cancers12092686.

In triple negative breast cancer (TNBC) cell lines, the proprotein convertase Furin cleaves and then activates several protein precursors involved in oncogenesis. However, the in vivo role of Furin in the mammary gland and how mammary gland-specific Furin knockout...

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He Z, Khatib AM, Creemers JWM. Loss of Proprotein Convertase Furin in Mammary Gland Impairs proIGF1R and proIR Processing and Suppresses Tumorigenesis in Triple Negative Breast Cancer. Cancers (Basel). 2020;12(9)doi: 10.3390/cancers12092686.
He, Z., Khatib, A. M., & Creemers, J. W. M. (2020). Loss of Proprotein Convertase Furin in Mammary Gland Impairs proIGF1R and proIR Processing and Suppresses Tumorigenesis in Triple Negative Breast Cancer. Cancers, 12(9), . https://doi.org/10.3390/cancers12092686
He, Zongsheng, et al. "Loss of Proprotein Convertase Furin in Mammary Gland Impairs proIGF1R and proIR Processing and Suppresses Tumorigenesis in Triple Negative Breast Cancer." Cancers vol. 12,9 (2020). doi: https://doi.org/10.3390/cancers12092686
He Z, Khatib AM, Creemers JWM. Loss of Proprotein Convertase Furin in Mammary Gland Impairs proIGF1R and proIR Processing and Suppresses Tumorigenesis in Triple Negative Breast Cancer. Cancers (Basel). 2020 Sep 20;12(9). doi: 10.3390/cancers12092686. PMID: 32962246; PMCID: PMC7563341.
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Outer and inner mitochondrial membrane proteins TOMM40 and TIMM50 are intensively concentrated and localized at Purkinje and pyramidal neurons in the New Zealand white rabbit brain.

Anatomical record (Hoboken, N.J. : 2007)

Farouk SM, Abdellatif AM, Metwally E.
PMID: 34041863
Anat Rec (Hoboken). 2022 Jan;305(1):209-221. doi: 10.1002/ar.24689. Epub 2021 Jun 05.

Mitochondria are involved in a variety of developmental processes and neurodegenerative diseases. The translocase complexes of the outer and inner mitochondrial membranes (TOM and TIM) are protein complexes involved in transporting protein precursors across mitochondrial membranes. Although rabbits are...

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Farouk SM, Abdellatif AM, Metwally E. Outer and inner mitochondrial membrane proteins TOMM40 and TIMM50 are intensively concentrated and localized at Purkinje and pyramidal neurons in the New Zealand white rabbit brain. Anat Rec (Hoboken). 2021;305(1):209-221doi: 10.1002/ar.24689.
Farouk, S. M., Abdellatif, A. M., & Metwally, E. (2022). Outer and inner mitochondrial membrane proteins TOMM40 and TIMM50 are intensively concentrated and localized at Purkinje and pyramidal neurons in the New Zealand white rabbit brain. Anatomical record (Hoboken, N.J. : 2007), 305(1), 209-221. https://doi.org/10.1002/ar.24689
Farouk, Sameh M, et al. "Outer and inner mitochondrial membrane proteins TOMM40 and TIMM50 are intensively concentrated and localized at Purkinje and pyramidal neurons in the New Zealand white rabbit brain." Anatomical record (Hoboken, N.J. : 2007) vol. 305,1 (2022): 209-221. doi: https://doi.org/10.1002/ar.24689
Farouk SM, Abdellatif AM, Metwally E. Outer and inner mitochondrial membrane proteins TOMM40 and TIMM50 are intensively concentrated and localized at Purkinje and pyramidal neurons in the New Zealand white rabbit brain. Anat Rec (Hoboken). 2022 Jan;305(1):209-221. doi: 10.1002/ar.24689. Epub 2021 Jun 05. PMID: 34041863.
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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.
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Showing 25 to 29 of 29 entries