Late Embryogenesis Abundant Proteins (Record no. 44593)
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| 000 -LEADER | |
|---|---|
| fixed length control field | 02121nam a2200193Ia 4500 |
| 003 - CONTROL NUMBER IDENTIFIER | |
| control field | MX-MdCICY |
| 005 - DATE AND TIME OF LATEST TRANSACTION | |
| control field | 20250625140630.0 |
| 040 ## - CATALOGING SOURCE | |
| Transcribing agency | CICY |
| 090 ## - LOCALLY ASSIGNED LC-TYPE CALL NUMBER (OCLC); LOCAL CALL NUMBER (RLIN) | |
| Classification number (OCLC) (R) ; Classification number, CALL (RLIN) (NR) | B-10355 |
| 008 - FIXED-LENGTH DATA ELEMENTS--GENERAL INFORMATION | |
| fixed length control field | 250602s9999 xx |||||s2 |||| ||und|d |
| 245 10 - TITLE STATEMENT | |
| Title | Late Embryogenesis Abundant Proteins |
| 490 0# - SERIES STATEMENT | |
| Volume/sequential designation | Advances in Botanical Research, 48, p.211-255, 2008 |
| 520 3# - SUMMARY, ETC. | |
| Summary, etc. | During the late maturation stage of seed development, water content decreases greatly. One of the most striking characteristics of mature orthodox seeds is their ability to withstand severe desiccation. Mechanisms of plant drought/desiccation tolerance have been studied by numerous groups, and a broad range of molecules have been identified to play some roles. Examples are proline, oligosaccharide, and late embryogenesis abundant (LEA)proteins, and so on. LEA proteins were first described from mature cotton seeds decades ago. Since then, many LEA proteins were identified from vascular and nonvascular plants, fungi, algae, and microbes, as well as anhydrobiotic animals such as protozoa, nematodes, insects, and crustaceans, and so on. The extensive distribution of LEA genes among diverse taxa implies that these genes might be primitive yet important and therefore maintained by these species. As a result of evolution, they may have a certain universal function-osmoprotection. Hydrophilic LEAproteins are members of natively unfolded proteins in solution. After the removal of bulk cytoplasmic water, the structures of LEA proteins undergo desiccationinduced folding. These biophysical features suggest that LEA proteins may carry out a bipartite function under diVerent water states. During drought, LEA proteins may establish a water shell and decrease ion strength. After esiccation, they may enhance the bioglass strength and act as a water replacement to stabilize cellular components. |
| 700 12 - ADDED ENTRY--PERSONAL NAME | |
| Personal name | Shih, M. |
| 700 12 - ADDED ENTRY--PERSONAL NAME | |
| Personal name | Hoekstra, F.A. |
| 700 12 - ADDED ENTRY--PERSONAL NAME | |
| Personal name | Hsing, Y.C. |
| 856 40 - ELECTRONIC LOCATION AND ACCESS | |
| Uniform Resource Identifier | <a href="https://drive.google.com/file/d/1ywE4qgEZRiqmqkstmTCg3Qiw715j3kej/view?usp=drivesdk">https://drive.google.com/file/d/1ywE4qgEZRiqmqkstmTCg3Qiw715j3kej/view?usp=drivesdk</a> |
| Public note | Para ver el documento ingresa a Google con tu cuenta: @cicy.edu.mx |
| 942 ## - ADDED ENTRY ELEMENTS (KOHA) | |
| Source of classification or shelving scheme | Clasificación local |
| Koha item type | Documentos solicitados |
| Lost status | Source of classification or shelving scheme | Damaged status | Not for loan | Collection | Home library | Current library | Shelving location | Date acquired | Total checkouts | Full call number | Date last seen | Price effective from | Koha item type |
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| Clasificación local | Ref1 | CICY | CICY | Documento préstamo interbibliotecario | 25.06.2025 | B-10355 | 25.06.2025 | 25.06.2025 | Documentos solicitados |