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Showing 1 to 12 of 164 entries
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Structural and Functional Characterization of Recombinant Isoforms of the Lentil Lipid Transfer Protein.

Acta naturae

Bogdanov IV, Finkina EI, Balandin SV, Melnikova DN, Stukacheva EA, Ovchinnikova TV.
PMID: 26483961
Acta Naturae. 2015 Jul-Sep;7(3):65-73.

The recombinant isoforms Lc-LTP1 and Lc-LTP3 of the lentil lipid transfer protein were overexpressed in E. coli cells. It was confirmed that both proteins are stabilized by four disulfide bonds and characterized by a high proportion of the α-helical...

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Bogdanov IV, Finkina EI, Balandin SV, et al. Structural and Functional Characterization of Recombinant Isoforms of the Lentil Lipid Transfer Protein. Acta Naturae. 2015;7(3):65-73
Bogdanov, I. V., Finkina, E. I., Balandin, S. V., Melnikova, D. N., Stukacheva, E. A., & Ovchinnikova, T. V. (2015). Structural and Functional Characterization of Recombinant Isoforms of the Lentil Lipid Transfer Protein. Acta naturae, 7(3), 65-73.
Bogdanov, I V, et al. "Structural and Functional Characterization of Recombinant Isoforms of the Lentil Lipid Transfer Protein." Acta naturae vol. 7,3 (2015): 65-73.
Bogdanov IV, Finkina EI, Balandin SV, Melnikova DN, Stukacheva EA, Ovchinnikova TV. Structural and Functional Characterization of Recombinant Isoforms of the Lentil Lipid Transfer Protein. Acta Naturae. 2015 Jul-Sep;7(3):65-73. PMID: 26483961; PMCID: PMC4610166.
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Lipoprotein assembly and function in an evolutionary perspective.

Biomolecular concepts

Van der Horst DJ, Rodenburg KW.
PMID: 25961995
Biomol Concepts. 2010 Aug 01;1(2):165-83. doi: 10.1515/bmc.2010.012.

Circulatory fat transport in animals relies on members of the large lipid transfer protein (LLTP) superfamily, including mammalian apolipoprotein B (apoB) and insect apolipophorin II/I (apoLp-II/I). ApoB and apoLp-II/I, constituting the structural (non-exchangeable) basis for the assembly of various...

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Van der Horst DJ, Rodenburg KW. Lipoprotein assembly and function in an evolutionary perspective. Biomol Concepts. 2010;1(2):165-83doi: 10.1515/bmc.2010.012.
Van der Horst, D. J., & Rodenburg, K. W. (2010). Lipoprotein assembly and function in an evolutionary perspective. Biomolecular concepts, 1(2), 165-83. https://doi.org/10.1515/bmc.2010.012
Van der Horst, Dick J, and Rodenburg, Kees W. "Lipoprotein assembly and function in an evolutionary perspective." Biomolecular concepts vol. 1,2 (2010): 165-83. doi: https://doi.org/10.1515/bmc.2010.012
Van der Horst DJ, Rodenburg KW. Lipoprotein assembly and function in an evolutionary perspective. Biomol Concepts. 2010 Aug 01;1(2):165-83. doi: 10.1515/bmc.2010.012. PMID: 25961995.
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Orthology Analysis and In Vivo Complementation Studies to Elucidate the Role of DIR1 during Systemic Acquired Resistance in Arabidopsis thaliana and Cucumis sativus.

Frontiers in plant science

Isaacs M, Carella P, Faubert J, Rose JK, Cameron RK.
PMID: 27200039
Front Plant Sci. 2016 May 03;7:566. doi: 10.3389/fpls.2016.00566. eCollection 2016.

AtDIR1 (Defective in Induced Resistance1) is an acidic lipid transfer protein essential for systemic acquired resistance (SAR) in Arabidopsis thaliana. Upon SAR induction, DIR1 moves from locally infected to distant uninfected leaves to activate defense priming; however, a molecular...

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Isaacs M, Carella P, Faubert J, et al. Orthology Analysis and In Vivo Complementation Studies to Elucidate the Role of DIR1 during Systemic Acquired Resistance in Arabidopsis thaliana and Cucumis sativus. Front Plant Sci. 2016;7:566doi: 10.3389/fpls.2016.00566.
Isaacs, M., Carella, P., Faubert, J., Rose, J. K., & Cameron, R. K. (2016). Orthology Analysis and In Vivo Complementation Studies to Elucidate the Role of DIR1 during Systemic Acquired Resistance in Arabidopsis thaliana and Cucumis sativus. Frontiers in plant science, 7566. https://doi.org/10.3389/fpls.2016.00566
Isaacs, Marisa, et al. "Orthology Analysis and In Vivo Complementation Studies to Elucidate the Role of DIR1 during Systemic Acquired Resistance in Arabidopsis thaliana and Cucumis sativus." Frontiers in plant science vol. 7 (2016): 566. doi: https://doi.org/10.3389/fpls.2016.00566
Isaacs M, Carella P, Faubert J, Rose JK, Cameron RK. Orthology Analysis and In Vivo Complementation Studies to Elucidate the Role of DIR1 during Systemic Acquired Resistance in Arabidopsis thaliana and Cucumis sativus. Front Plant Sci. 2016 May 03;7:566. doi: 10.3389/fpls.2016.00566. eCollection 2016. PMID: 27200039; PMCID: PMC4854023.
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Assessment of sensitization to grape and wine allergens as possible causes of adverse reactions to wine: a pilot study.

Clinical and translational allergy

Jaeckels N, Bellinghausen I, Fronk P, Heydenreich B, Saloga J, Decker H.
PMID: 26101585
Clin Transl Allergy. 2015 Jun 22;5:21. doi: 10.1186/s13601-015-0065-8. eCollection 2015.

BACKGROUND: In a recently performed survey with 4000 randomly selected persons, 68 (7.2 %) of 948 respondents reported intolerance and/or allergy-like symptoms to wine. The aim of this study was to analyze whether a real sensitization to wine proteins...

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Jaeckels N, Bellinghausen I, Fronk P, et al. Assessment of sensitization to grape and wine allergens as possible causes of adverse reactions to wine: a pilot study. Clin Transl Allergy. 2015;5:21doi: 10.1186/s13601-015-0065-8.
Jaeckels, N., Bellinghausen, I., Fronk, P., Heydenreich, B., Saloga, J., & Decker, H. (2015). Assessment of sensitization to grape and wine allergens as possible causes of adverse reactions to wine: a pilot study. Clinical and translational allergy, 521. https://doi.org/10.1186/s13601-015-0065-8
Jaeckels, Nadine, et al. "Assessment of sensitization to grape and wine allergens as possible causes of adverse reactions to wine: a pilot study." Clinical and translational allergy vol. 5 (2015): 21. doi: https://doi.org/10.1186/s13601-015-0065-8
Jaeckels N, Bellinghausen I, Fronk P, Heydenreich B, Saloga J, Decker H. Assessment of sensitization to grape and wine allergens as possible causes of adverse reactions to wine: a pilot study. Clin Transl Allergy. 2015 Jun 22;5:21. doi: 10.1186/s13601-015-0065-8. eCollection 2015. PMID: 26101585; PMCID: PMC4476230.
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Pattern Formation in the Arabidopsis Embryo Revealed by Position-Specific Lipid Transfer Protein Gene Expression.

The Plant cell

Vroemen CW, Langeveld S, Mayer U, Ripper G, Jurgens G, Van Kammen A, De Vries SC.
PMID: 12239400
Plant Cell. 1996 May;8(5):783-791. doi: 10.1105/tpc.8.5.783.

During Arabidopsis embryogenesis, the zygote divides asymmetrically in the future apical-basal axis; however, a radial axis is initiated only within the eight-celled embryo. Mutations in the GNOM, KNOLLE, and KEULE genes affect these processes: gnom zygotes tend to divide...

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Vroemen CW, Langeveld S, Mayer U, et al. Pattern Formation in the Arabidopsis Embryo Revealed by Position-Specific Lipid Transfer Protein Gene Expression. Plant Cell. 1996;8(5):783-791doi: 10.1105/tpc.8.5.783.
Vroemen, C. W., Langeveld, S., Mayer, U., Ripper, G., Jurgens, G., Van Kammen, A., & De Vries, S. C. (1996). Pattern Formation in the Arabidopsis Embryo Revealed by Position-Specific Lipid Transfer Protein Gene Expression. The Plant cell, 8(5), 783-791. https://doi.org/10.1105/tpc.8.5.783
Vroemen, C. W., et al. "Pattern Formation in the Arabidopsis Embryo Revealed by Position-Specific Lipid Transfer Protein Gene Expression." The Plant cell vol. 8,5 (1996): 783-791. doi: https://doi.org/10.1105/tpc.8.5.783
Vroemen CW, Langeveld S, Mayer U, Ripper G, Jurgens G, Van Kammen A, De Vries SC. Pattern Formation in the Arabidopsis Embryo Revealed by Position-Specific Lipid Transfer Protein Gene Expression. Plant Cell. 1996 May;8(5):783-791. doi: 10.1105/tpc.8.5.783. PMID: 12239400; PMCID: PMC161137.
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Lipid transfer proteins are encoded by a small multigene family in Arabidopsis thaliana.

Plant science : an international journal of experimental plant biology

Arondel12 V, Vergnolle2 C, Cantrel C, Kader J.
PMID: 10940464
Plant Sci. 2000 Aug 08;157(1):1-12. doi: 10.1016/s0168-9452(00)00232-6.

Lipid transfer proteins (LTPs) are small, basic and abundant proteins in higher plants. They are capable of binding fatty acids and of transferring phospholipids between membranes in vitro. LTPs from this family contain a signal peptide and are secreted...

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Arondel12 V, Vergnolle2 C, Cantrel C, et al. Lipid transfer proteins are encoded by a small multigene family in Arabidopsis thaliana. Plant Sci. 2000;157(1):1-12doi: 10.1016/s0168-9452(00)00232-6.
Arondel12, V., Vergnolle2, C., Cantrel, C., & Kader, J. (2000). Lipid transfer proteins are encoded by a small multigene family in Arabidopsis thaliana. Plant science : an international journal of experimental plant biology, 157(1), 1-12. https://doi.org/10.1016/s0168-9452(00)00232-6
Arondel12, et al. "Lipid transfer proteins are encoded by a small multigene family in Arabidopsis thaliana." Plant science : an international journal of experimental plant biology vol. 157,1 (2000): 1-12. doi: https://doi.org/10.1016/s0168-9452(00)00232-6
Arondel12 V, Vergnolle2 C, Cantrel C, Kader J. Lipid transfer proteins are encoded by a small multigene family in Arabidopsis thaliana. Plant Sci. 2000 Aug 08;157(1):1-12. doi: 10.1016/s0168-9452(00)00232-6. PMID: 10940464.
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Three pathogen-inducible genes encoding lipid transfer protein from pepper are differentially activated by pathogens, abiotic, and environmental stresses.

Plant, cell & environment

Jung HW, Kim W, Hwang BK.
PMID: 12803619
Plant Cell Environ. 2003 Jun;26(6):915-928. doi: 10.1046/j.1365-3040.2003.01024.x.

The three cDNA clones, CALTPI, CALTPII, and CALTPIII, corresponding to pepper lipid transfer protein (LTP) genes were isolated from a pepper (Capsicum annuum) cDNA library from hypersensitive response (HR) lesions of leaves infected with Xanthomonas campestris pv. vesicatoria. The...

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Jung HW, Kim W, Hwang BK. Three pathogen-inducible genes encoding lipid transfer protein from pepper are differentially activated by pathogens, abiotic, and environmental stresses. Plant Cell Environ. 2003;26(6):915-928doi: 10.1046/j.1365-3040.2003.01024.x.
Jung, H. W., Kim, W., & Hwang, B. K. (2003). Three pathogen-inducible genes encoding lipid transfer protein from pepper are differentially activated by pathogens, abiotic, and environmental stresses. Plant, cell & environment, 26(6), 915-928. https://doi.org/10.1046/j.1365-3040.2003.01024.x
Jung, HO WON, et al. "Three pathogen-inducible genes encoding lipid transfer protein from pepper are differentially activated by pathogens, abiotic, and environmental stresses." Plant, cell & environment vol. 26,6 (2003): 915-928. doi: https://doi.org/10.1046/j.1365-3040.2003.01024.x
Jung HW, Kim W, Hwang BK. Three pathogen-inducible genes encoding lipid transfer protein from pepper are differentially activated by pathogens, abiotic, and environmental stresses. Plant Cell Environ. 2003 Jun;26(6):915-928. doi: 10.1046/j.1365-3040.2003.01024.x. PMID: 12803619.
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In Vitro Antifungal Activity of a Radish (Raphanus sativus L.) Seed Protein Homologous to Nonspecific Lipid Transfer Proteins.

Plant physiology

Terras FR, Goderis IJ, Van Leuven F, Vanderleyden J, Cammue BP, Broekaert WF.
PMID: 16653017
Plant Physiol. 1992 Oct;100(2):1055-8. doi: 10.1104/pp.100.2.1055.

A basic 9-kD protein was purified from seeds of radish (Raphanus sativus L.). The 43 amino-terminal amino acids show extensive sequence identity with nonspecific lipid transfer proteins from other plant species. The radish seed nonspecific lipid transfer protein-like protein...

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Terras FR, Goderis IJ, Van Leuven F, et al. In Vitro Antifungal Activity of a Radish (Raphanus sativus L.) Seed Protein Homologous to Nonspecific Lipid Transfer Proteins. Plant Physiol. 1992;100(2):1055-8doi: 10.1104/pp.100.2.1055.
Terras, F. R., Goderis, I. J., Van Leuven, F., Vanderleyden, J., Cammue, B. P., & Broekaert, W. F. (1992). In Vitro Antifungal Activity of a Radish (Raphanus sativus L.) Seed Protein Homologous to Nonspecific Lipid Transfer Proteins. Plant physiology, 100(2), 1055-8. https://doi.org/10.1104/pp.100.2.1055
Terras, F R, et al. "In Vitro Antifungal Activity of a Radish (Raphanus sativus L.) Seed Protein Homologous to Nonspecific Lipid Transfer Proteins." Plant physiology vol. 100,2 (1992): 1055-8. doi: https://doi.org/10.1104/pp.100.2.1055
Terras FR, Goderis IJ, Van Leuven F, Vanderleyden J, Cammue BP, Broekaert WF. In Vitro Antifungal Activity of a Radish (Raphanus sativus L.) Seed Protein Homologous to Nonspecific Lipid Transfer Proteins. Plant Physiol. 1992 Oct;100(2):1055-8. doi: 10.1104/pp.100.2.1055. PMID: 16653017; PMCID: PMC1075666.
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Constitutive expression of Vitis vinifera thaumatin-like protein after in vitro selection and its role in anthracnose resistance.

Functional plant biology : FPB

Jayasankar S, Li Z, Gray DJ.
PMID: 32689093
Funct Plant Biol. 2003 Jan;30(11):1105-1115. doi: 10.1071/FP03066.

Anthracnose-resistant grapevine (Vitis vinifera L. cv. Chardonnay) plants were regenerated from embryogenic cultures that had been subjected to in vitro selection with culture filtrate of Elsinoe ampelina (de Bary) Shear. Three secreted proteins differentially expressed by in vitro-selected embryogenic...

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Jayasankar S, Li Z, Gray DJ. Constitutive expression of Vitis vinifera thaumatin-like protein after in vitro selection and its role in anthracnose resistance. Funct Plant Biol. 2003;30(11):1105-1115doi: 10.1071/FP03066.
Jayasankar, S., Li, Z., & Gray, D. J. (2003). Constitutive expression of Vitis vinifera thaumatin-like protein after in vitro selection and its role in anthracnose resistance. Functional plant biology : FPB, 30(11), 1105-1115. https://doi.org/10.1071/FP03066
Jayasankar, Subramanian, et al. "Constitutive expression of Vitis vinifera thaumatin-like protein after in vitro selection and its role in anthracnose resistance." Functional plant biology : FPB vol. 30,11 (2003): 1105-1115. doi: https://doi.org/10.1071/FP03066
Jayasankar S, Li Z, Gray DJ. Constitutive expression of Vitis vinifera thaumatin-like protein after in vitro selection and its role in anthracnose resistance. Funct Plant Biol. 2003 Jan;30(11):1105-1115. doi: 10.1071/FP03066. PMID: 32689093.
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Genome-wide identification and characterization of non-specific lipid transfer proteins in cabbage.

PeerJ

Ji J, Lv H, Yang L, Fang Z, Zhuang M, Zhang Y, Liu Y, Li Z.
PMID: 30128186
PeerJ. 2018 Aug 10;6:e5379. doi: 10.7717/peerj.5379. eCollection 2018.

Plant non-specific lipid transfer proteins (nsLTPs) are a group of small, secreted proteins that can reversibly bind and transport hydrophobic molecules. NsLTPs play an important role in plant development and resistance to stress. To date, little is known about...

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Ji J, Lv H, Yang L, et al. Genome-wide identification and characterization of non-specific lipid transfer proteins in cabbage. PeerJ. 2018;6:e5379doi: 10.7717/peerj.5379.
Ji, J., Lv, H., Yang, L., Fang, Z., Zhuang, M., Zhang, Y., Liu, Y., & Li, Z. (2018). Genome-wide identification and characterization of non-specific lipid transfer proteins in cabbage. PeerJ, 6e5379. https://doi.org/10.7717/peerj.5379
Ji, Jialei, et al. "Genome-wide identification and characterization of non-specific lipid transfer proteins in cabbage." PeerJ vol. 6 (2018): e5379. doi: https://doi.org/10.7717/peerj.5379
Ji J, Lv H, Yang L, Fang Z, Zhuang M, Zhang Y, Liu Y, Li Z. Genome-wide identification and characterization of non-specific lipid transfer proteins in cabbage. PeerJ. 2018 Aug 10;6:e5379. doi: 10.7717/peerj.5379. eCollection 2018. PMID: 30128186; PMCID: PMC6089208.
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Systematic analysis of the non-specific lipid transfer protein gene family in Nicotiana tabacum reveal its potential roles in stress responses.

Plant physiology and biochemistry : PPB

Yang Y, Li P, Liu C, Wang P, Cao P, Ye X, Li Q.
PMID: 35016104
Plant Physiol Biochem. 2022 Jan 05;172:33-47. doi: 10.1016/j.plaphy.2022.01.002. Epub 2022 Jan 05.

Plant non-specific lipid transfer proteins (nsLTPs) are characterized by an eight-cysteine motif backbone stabilized by four disulfide bonds; these proteins can bind or transfer lipids. NsLTPs play important roles in plant growth and development, and in the responses to...

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Yang Y, Li P, Liu C, et al. Systematic analysis of the non-specific lipid transfer protein gene family in Nicotiana tabacum reveal its potential roles in stress responses. Plant Physiol Biochem. 2022;172:33-47doi: 10.1016/j.plaphy.2022.01.002.
Yang, Y., Li, P., Liu, C., Wang, P., Cao, P., Ye, X., & Li, Q. (2022). Systematic analysis of the non-specific lipid transfer protein gene family in Nicotiana tabacum reveal its potential roles in stress responses. Plant physiology and biochemistry : PPB, 17233-47. https://doi.org/10.1016/j.plaphy.2022.01.002
Yang, Yongxia, et al. "Systematic analysis of the non-specific lipid transfer protein gene family in Nicotiana tabacum reveal its potential roles in stress responses." Plant physiology and biochemistry : PPB vol. 172 (2022): 33-47. doi: https://doi.org/10.1016/j.plaphy.2022.01.002
Yang Y, Li P, Liu C, Wang P, Cao P, Ye X, Li Q. Systematic analysis of the non-specific lipid transfer protein gene family in Nicotiana tabacum reveal its potential roles in stress responses. Plant Physiol Biochem. 2022 Jan 05;172:33-47. doi: 10.1016/j.plaphy.2022.01.002. Epub 2022 Jan 05. PMID: 35016104.
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TMEM106B in humans and Vac7 and Tag1 in yeast are predicted to be lipid transfer proteins.

Proteins

Levine TP.
PMID: 34347309
Proteins. 2022 Jan;90(1):164-175. doi: 10.1002/prot.26201. Epub 2021 Aug 12.

TMEM106B is an integral membrane protein of late endosomes and lysosomes involved in neuronal function, its overexpression being associated with familial frontotemporal lobar degeneration, and point mutation linked to hypomyelination. It has also been identified in multiple screens for...

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Levine TP. TMEM106B in humans and Vac7 and Tag1 in yeast are predicted to be lipid transfer proteins. Proteins. 2021;90(1):164-175doi: 10.1002/prot.26201.
Levine, T. P. (2022). TMEM106B in humans and Vac7 and Tag1 in yeast are predicted to be lipid transfer proteins. Proteins, 90(1), 164-175. https://doi.org/10.1002/prot.26201
Levine, Tim P. "TMEM106B in humans and Vac7 and Tag1 in yeast are predicted to be lipid transfer proteins." Proteins vol. 90,1 (2022): 164-175. doi: https://doi.org/10.1002/prot.26201
Levine TP. TMEM106B in humans and Vac7 and Tag1 in yeast are predicted to be lipid transfer proteins. Proteins. 2022 Jan;90(1):164-175. doi: 10.1002/prot.26201. Epub 2021 Aug 12. PMID: 34347309.
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