Форма представления | Статьи в зарубежных журналах и сборниках |
Год публикации | 2014 |
Язык | русский |
|
Балабан Нэлли Павловна, автор
Маргулис Анна Борисовна, автор
Рудакова Наталья Леонидовна, автор
Тойменцева Анна Александровна, автор
Шагимарданова Елена Ильясовна, автор
Шарипова Маргарита Рашидовна, автор
|
Библиографическое описание на языке оригинала |
Danilova YV, Shagimardanova EI, Margulis AB, Toymentseva AA, Balaban NP, Rudakova NL, Rizvanov AA, Sharipova MR, Palotás A. Bacterial enzymes effectively digest Alzheimer's β-amyloid peptide.Brain Res Bull. 2014, 108, P.113-117. |
Аннотация |
Aggregated
-amyloid peptides play key roles in the development of Alzheimer?s disease, and recent
evidence suggests that microbial particles, among others, can facilitate their polymerization. Bacterial
enzymes, however, have been proved to be beneficial in degrading pathological fibrillar structures in
clinical settings, such as strepto-kinases in resolving blood-clots. The purpose of this study was to investigate
the ability of bacterial substances to effectively hydrolyze
-amyloid peptides. Degrading products
of several proteinases from Bacillus pumilus were evaluated using MALDI-TOF mass-spectrometry, and
their toxicity was assessed in vitro using cell-culture assays and morphological studies. These enzymes
have proved to be non-toxic and were demonstrated to cleave through the functional domains of
-
amyloid peptide. By yielding inactive fragments, proteinases of Bacillus pumilus may be used as candidate
anti-amyloid agents. |
Ключевые слова |
Bacillus pumilus, extracellular proteinases, Alzheimer's β-amyloid, MALDI-TOF mass-spectrometry |
Название журнала |
BRAIN RES BULL
|
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Полная запись метаданных |
Поле DC |
Значение |
Язык |
dc.contributor.author |
Балабан Нэлли Павловна |
ru_RU |
dc.contributor.author |
Маргулис Анна Борисовна |
ru_RU |
dc.contributor.author |
Рудакова Наталья Леонидовна |
ru_RU |
dc.contributor.author |
Тойменцева Анна Александровна |
ru_RU |
dc.contributor.author |
Шагимарданова Елена Ильясовна |
ru_RU |
dc.contributor.author |
Шарипова Маргарита Рашидовна |
ru_RU |
dc.date.accessioned |
2014-01-01T00:00:00Z |
ru_RU |
dc.date.available |
2014-01-01T00:00:00Z |
ru_RU |
dc.date.issued |
2014 |
ru_RU |
dc.identifier.citation |
Danilova YV, Shagimardanova EI, Margulis AB, Toymentseva AA, Balaban NP, Rudakova NL, Rizvanov AA, Sharipova MR, Palotás A. Bacterial enzymes effectively digest Alzheimer's β-amyloid peptide.Brain Res Bull. 2014, 108, P.113-117. |
ru_RU |
dc.identifier.uri |
https://repository.kpfu.ru/?p_id=90034 |
ru_RU |
dc.description.abstract |
BRAIN RES BULL |
ru_RU |
dc.description.abstract |
Aggregated
-amyloid peptides play key roles in the development of Alzheimer?s disease, and recent
evidence suggests that microbial particles, among others, can facilitate their polymerization. Bacterial
enzymes, however, have been proved to be beneficial in degrading pathological fibrillar structures in
clinical settings, such as strepto-kinases in resolving blood-clots. The purpose of this study was to investigate
the ability of bacterial substances to effectively hydrolyze
-amyloid peptides. Degrading products
of several proteinases from Bacillus pumilus were evaluated using MALDI-TOF mass-spectrometry, and
their toxicity was assessed in vitro using cell-culture assays and morphological studies. These enzymes
have proved to be non-toxic and were demonstrated to cleave through the functional domains of
-
amyloid peptide. By yielding inactive fragments, proteinases of Bacillus pumilus may be used as candidate
anti-amyloid agents. |
ru_RU |
dc.language.iso |
ru |
ru_RU |
dc.subject |
Bacillus pumilus |
ru_RU |
dc.subject |
extracellular proteinases |
ru_RU |
dc.subject |
Alzheimer's β-amyloid |
ru_RU |
dc.subject |
MALDI-TOF mass-spectrometry |
ru_RU |
dc.title |
Bacterial enzymes effectively digest Alzheimer's β-amyloid peptide. |
ru_RU |
dc.type |
Статьи в зарубежных журналах и сборниках |
ru_RU |
|