| pubmed-article:1931951 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:1931951 | lifeskim:mentions | umls-concept:C0020792 | lld:lifeskim |
| pubmed-article:1931951 | lifeskim:mentions | umls-concept:C0033684 | lld:lifeskim |
| pubmed-article:1931951 | lifeskim:mentions | umls-concept:C0080021 | lld:lifeskim |
| pubmed-article:1931951 | lifeskim:mentions | umls-concept:C0699900 | lld:lifeskim |
| pubmed-article:1931951 | lifeskim:mentions | umls-concept:C0243125 | lld:lifeskim |
| pubmed-article:1931951 | lifeskim:mentions | umls-concept:C1514468 | lld:lifeskim |
| pubmed-article:1931951 | lifeskim:mentions | umls-concept:C0475264 | lld:lifeskim |
| pubmed-article:1931951 | lifeskim:mentions | umls-concept:C0348080 | lld:lifeskim |
| pubmed-article:1931951 | lifeskim:mentions | umls-concept:C1707271 | lld:lifeskim |
| pubmed-article:1931951 | pubmed:issue | 42 | lld:pubmed |
| pubmed-article:1931951 | pubmed:dateCreated | 1991-11-25 | lld:pubmed |
| pubmed-article:1931951 | pubmed:abstractText | Illumination of a suspension of thylakoids with light at high intensity causes inhibition of the photosystem II electron transport activity and loss from the membrane of the D1 protein of the photosystem II reaction center. Impairment of the electron transport activity and depletion of D1 protein from the thylakoid membrane of pea were investigated with reference to the presence or absence of oxygen in the suspension. The breakdown products of the D1 protein were identified by immunoblotting with anti-D1 polyclonal antibodies which were proven to recognize mainly the C-terminal region of the protein. The results obtained show that (i) the light-induced inactivation of the photosystem II electron transport activity under anaerobic conditions is faster than in the presence of oxygen; (ii) depletion of D1 protein is observed on a longer time scale with respect to loss of electron transport activity and is faster when photoinhibition is performed in the presence of oxygen; (iii) C-terminal fragments of D1 are only observed when photoinhibition is carried out anaerobically and are mainly localized in the stroma-exposed regions; and (iv) the fragments observed after anaerobic photoinhibition are quickly degraded on further illumination of the thylakoid suspension in the presence of oxygen. | lld:pubmed |
| pubmed-article:1931951 | pubmed:language | eng | lld:pubmed |
| pubmed-article:1931951 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:1931951 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:1931951 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:1931951 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:1931951 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:1931951 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:1931951 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:1931951 | pubmed:month | Oct | lld:pubmed |
| pubmed-article:1931951 | pubmed:issn | 0006-2960 | lld:pubmed |
| pubmed-article:1931951 | pubmed:author | pubmed-author:GiacomettiG... | lld:pubmed |
| pubmed-article:1931951 | pubmed:author | pubmed-author:RigoniFF | lld:pubmed |
| pubmed-article:1931951 | pubmed:author | pubmed-author:BarbatoRR | lld:pubmed |
| pubmed-article:1931951 | pubmed:author | pubmed-author:FrisoGG | lld:pubmed |
| pubmed-article:1931951 | pubmed:author | pubmed-author:GiardiM TMT | lld:pubmed |
| pubmed-article:1931951 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:1931951 | pubmed:day | 22 | lld:pubmed |
| pubmed-article:1931951 | pubmed:volume | 30 | lld:pubmed |
| pubmed-article:1931951 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:1931951 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:1931951 | pubmed:pagination | 10220-6 | lld:pubmed |
| pubmed-article:1931951 | pubmed:dateRevised | 2003-11-14 | lld:pubmed |
| pubmed-article:1931951 | pubmed:meshHeading | pubmed-meshheading:1931951-... | lld:pubmed |
| pubmed-article:1931951 | pubmed:meshHeading | pubmed-meshheading:1931951-... | lld:pubmed |
| pubmed-article:1931951 | pubmed:meshHeading | pubmed-meshheading:1931951-... | lld:pubmed |
| pubmed-article:1931951 | pubmed:meshHeading | pubmed-meshheading:1931951-... | lld:pubmed |
| pubmed-article:1931951 | pubmed:meshHeading | pubmed-meshheading:1931951-... | lld:pubmed |
| pubmed-article:1931951 | pubmed:meshHeading | pubmed-meshheading:1931951-... | lld:pubmed |
| pubmed-article:1931951 | pubmed:meshHeading | pubmed-meshheading:1931951-... | lld:pubmed |
| pubmed-article:1931951 | pubmed:meshHeading | pubmed-meshheading:1931951-... | lld:pubmed |
| pubmed-article:1931951 | pubmed:meshHeading | pubmed-meshheading:1931951-... | lld:pubmed |
| pubmed-article:1931951 | pubmed:meshHeading | pubmed-meshheading:1931951-... | lld:pubmed |
| pubmed-article:1931951 | pubmed:year | 1991 | lld:pubmed |
| pubmed-article:1931951 | pubmed:articleTitle | Breakdown of the photosystem II reaction center D1 protein under photoinhibitory conditions: identification and localization of the C-terminal degradation products. | lld:pubmed |
| pubmed-article:1931951 | pubmed:affiliation | Dipartimento di Biologia, Università di Padova, Italy. | lld:pubmed |
| pubmed-article:1931951 | pubmed:publicationType | Journal Article | lld:pubmed |
| http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:1931951 | lld:pubmed |
| http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:1931951 | lld:pubmed |
| http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:1931951 | lld:pubmed |
| http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:1931951 | lld:pubmed |
