Articles with "lea proteins" as a keyword



Photo from archive.org

Physicochemical Aspects of the Biological Functions of Trehalose and Group 3 LEA Proteins as Desiccation Protectants.

Sign Up to like & get
recommendations!
Published in 2018 at "Advances in experimental medicine and biology"

DOI: 10.1007/978-981-13-1244-1_15

Abstract: In this review, we first focus on the mechanism by which the larva of the sleeping chironomid, Polypedilum vanderplanki, survives an extremely dehydrated state and describe how trehalose and probably late embryogenesis abundant (LEA) proteins… read more here.

Keywords: desiccation protectants; lea proteins; group lea; lea ... See more keywords

LEA proteins are involved in cyst desiccation resistance and other abiotic stresses in Azotobacter vinelandii

Sign Up to like & get
recommendations!
Published in 2017 at "Cell Stress and Chaperones"

DOI: 10.1007/s12192-017-0781-1

Abstract: Late embryogenesis abundant (LEA) proteins constitute a large protein family that is closely associated with resistance to abiotic stresses in multiple organisms and protect cells against drought and other stresses. Azotobacter vinelandii is a soil… read more here.

Keywords: desiccation; resistance abiotic; abiotic stresses; lea ... See more keywords

Late Embryogenesis Abundant (LEA) proteins confer water stress tolerance to mammalian somatic cells.

Sign Up to like & get
recommendations!
Published in 2020 at "Cryobiology"

DOI: 10.1016/j.cryobiol.2020.01.009

Abstract: Late Embryogenesis Abundant (LEA) proteins are commonly found in plants and other organisms capable of undergoing severe and reversible dehydration, a phenomenon termed "anhydrobiosis". Here, we have produced a tagged version for three different LEA… read more here.

Keywords: abundant lea; tolerance mammalian; late embryogenesis; lea proteins ... See more keywords

Small LEA proteins mitigate air-water interface damage to fragile cryo-EM samples during plunge freezing

Sign Up to like & get
recommendations!
Published in 2024 at "Nature Communications"

DOI: 10.1038/s41467-024-52091-1

Abstract: Air-water interface (AWI) interactions during cryo-electron microscopy (cryo-EM) sample preparation cause significant sample loss, hindering structural biology research. Organisms like nematodes and tardigrades produce Late Embryogenesis Abundant (LEA) proteins to withstand desiccation stress. Here we… read more here.

Keywords: air water; damage; cryo; biology ... See more keywords

Effects of AavLEA1 Protein on Mouse Ovarian Tissue Cryopreservation by Vitrification.

Sign Up to like & get
recommendations!
Published in 2021 at "Biopreservation and biobanking"

DOI: 10.1089/bio.2021.0048

Abstract: Conventional ovarian tissue cryopreservation often destroys the structural, functional, and DNA integrity of the ovarian tissue. How to effectively retain the ultrastructure and subsequent function of ovarian tissue during cryopreservation has long been an issue… read more here.

Keywords: protein; ovarian tissue; tissue; tissue cryopreservation ... See more keywords

Improving vitrification efficiency of human in vitro matured oocytes by the addition of LEA proteins.

Sign Up to like & get
recommendations!
Published in 2024 at "Human reproduction"

DOI: 10.1093/humrep/deae065

Abstract: STUDY QUESTION Can the addition of late embryogenesis-abundant (LEA) proteins as a cryoprotective agent during the vitrification cryopreservation of in vitro matured oocytes enhance their developmental potential after fertilization? SUMMARY ANSWER LEA proteins improve the… read more here.

Keywords: vitrification; matured oocytes; lea; group ... See more keywords

Stress Regulatory capabilities discovered in late embryogenesis abundant (LEA) proteins expressed during pecan (Carya illinoinensis) kernel development

Sign Up to like & get
recommendations!
Published in 2025 at "BMC Genomics"

DOI: 10.1186/s12864-025-12040-8

Abstract: Pecan (Carya illinoinensis), a major North American tree nut crop, faces yield losses due to abiotic stressors like drought and salinity. Late embryogenesis abundant (LEA) proteins, known for stabilizing cellular components under desiccation, remain uncharacterized… read more here.

Keywords: late embryogenesis; carya illinoinensis; pecan carya; lea ... See more keywords

Physiological, Structural, and Functional Insights Into the Cryoprotection of Membranes by the Dehydrins

Sign Up to like & get
recommendations!
Published in 2022 at "Frontiers in Plant Science"

DOI: 10.3389/fpls.2022.886525

Abstract: Plants can be exposed to cold temperatures and have therefore evolved several mechanisms to prevent damage caused by freezing. One of the most important targets are membranes, which are particularly susceptible to cold damage. To… read more here.

Keywords: lea proteins; insights cryoprotection; functional insights; cryoprotection ... See more keywords
Photo from wikipedia

Characterization of the Heat-Stable Proteome during Seed Germination in Arabidopsis with Special Focus on LEA Proteins

Sign Up to like & get
recommendations!
Published in 2021 at "International Journal of Molecular Sciences"

DOI: 10.3390/ijms22158172

Abstract: During seed germination, desiccation tolerance is lost in the radicle with progressing radicle protrusion and seedling establishment. This process is accompanied by comprehensive changes in the metabolome and proteome. Germination of Arabidopsis seeds was investigated… read more here.

Keywords: seed; heat stable; germination; stable proteome ... See more keywords

Group 1 LEA Proteins in Durum Wheat: Evolution, Expression, and Roles in Abiotic Stress Tolerance

Sign Up to like & get
recommendations!
Published in 2025 at "Plants"

DOI: 10.3390/plants14182817

Abstract: Group 1 LEA proteins are involved in embryo water dynamics during the maturation stage of seed development and contribute to desiccation stress protection in vegetative and embryonic tissues. Nevertheless, their roles in durum wheat remain… read more here.

Keywords: wheat; stress; group lea; lea proteins ... See more keywords

Disordered proteins interact with the chemical environment to tune their protective function during drying

Sign Up to like & get
recommendations!
Published in 2024 at "eLife"

DOI: 10.7554/elife.97231

Abstract: The conformational ensemble and function of intrinsically disordered proteins (IDPs) are sensitive to their solution environment. The inherent malleability of disordered proteins, combined with the exposure of their residues, accounts for this sensitivity. One context… read more here.

Keywords: environment; desiccation; disordered proteins; lea proteins ... See more keywords