| pubmed-article:1653647 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:1653647 | lifeskim:mentions | umls-concept:C1383501 | lld:lifeskim |
| pubmed-article:1653647 | lifeskim:mentions | umls-concept:C0450429 | lld:lifeskim |
| pubmed-article:1653647 | lifeskim:mentions | umls-concept:C0597357 | lld:lifeskim |
| pubmed-article:1653647 | lifeskim:mentions | umls-concept:C0033684 | lld:lifeskim |
| pubmed-article:1653647 | lifeskim:mentions | umls-concept:C0521447 | lld:lifeskim |
| pubmed-article:1653647 | lifeskim:mentions | umls-concept:C1710082 | lld:lifeskim |
| pubmed-article:1653647 | lifeskim:mentions | umls-concept:C1145667 | lld:lifeskim |
| pubmed-article:1653647 | lifeskim:mentions | umls-concept:C0887839 | lld:lifeskim |
| pubmed-article:1653647 | pubmed:issue | 5 | lld:pubmed |
| pubmed-article:1653647 | pubmed:dateCreated | 1991-10-11 | lld:pubmed |
| pubmed-article:1653647 | pubmed:abstractText | We have purified two major polypeptides of 54 and 56 kd from bovine erythrocytes that specifically bind the nuclear location sequence (NLS) of the SV40 large T antigen. When added to a permeabilized cell system for nuclear import, the purified proteins increase by 2- to 3-fold the nuclear accumulation of a fluorescent protein containing the large T antigen NLS. The import stimulation is saturable and dependent upon the presence of cytosol. Nuclear protein accumulation in vitro is sensitive to inactivation by N-ethylmaleimide (NEM). NEM inactivation can be overcome by addition of the purified NLS-binding proteins to the import system. NEM treatment of the purified proteins abolishes their ability to stimulate import but does not affect NLS binding. Our results indicate that the NLS-binding proteins are NEM-sensitive receptors for nuclear import. At least one other NEM-sensitive cytosolic activity and an NEM-insensitive cytosolic activity are also necessary for protein import in vitro. | lld:pubmed |
| pubmed-article:1653647 | pubmed:language | eng | lld:pubmed |
| pubmed-article:1653647 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:1653647 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:1653647 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
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| pubmed-article:1653647 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:1653647 | pubmed:month | Sep | lld:pubmed |
| pubmed-article:1653647 | pubmed:issn | 0092-8674 | lld:pubmed |
| pubmed-article:1653647 | pubmed:author | pubmed-author:GeraceLL | lld:pubmed |
| pubmed-article:1653647 | pubmed:author | pubmed-author:AdamS ASA | lld:pubmed |
| pubmed-article:1653647 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:1653647 | pubmed:day | 6 | lld:pubmed |
| pubmed-article:1653647 | pubmed:volume | 66 | lld:pubmed |
| pubmed-article:1653647 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:1653647 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:1653647 | pubmed:pagination | 837-47 | lld:pubmed |
| pubmed-article:1653647 | pubmed:dateRevised | 2006-11-15 | lld:pubmed |
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| pubmed-article:1653647 | pubmed:year | 1991 | lld:pubmed |
| pubmed-article:1653647 | pubmed:articleTitle | Cytosolic proteins that specifically bind nuclear location signals are receptors for nuclear import. | lld:pubmed |
| pubmed-article:1653647 | pubmed:affiliation | Department of Cell, Molecular and Structural Biology, Northwestern University Medical School, Chicago, Illinois 60611. | lld:pubmed |
| pubmed-article:1653647 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:1653647 | pubmed:publicationType | Research Support, U.S. Gov't, P.H.S. | lld:pubmed |
| pubmed-article:1653647 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
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