d-ribose and pathogenesis of Alzheimer’s disease
It is estimated that the global prevalence of dementia will rise as high as 24 million and predicted to be double in every 20 years which is attributed to the fact that the ageing population is increasing and so more individuals are at risk of developing neurodegenerative diseases like Alzheimer’s....
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| Veröffentlicht in: | Molecular biology reports 2020-03, Vol.47 (3), p.2289-2299 |
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| creator | Javed, Mehjbeen Ahmad, Md. Irshad Javed, Hina Naseem, Sufia |
| description | It is estimated that the global prevalence of dementia will rise as high as 24 million and predicted to be double in every 20 years which is attributed to the fact that the ageing population is increasing and so more individuals are at risk of developing neurodegenerative diseases like Alzheimer’s. Many scientists favored glycation of proteins such as tau, amyloid beta (Aβ) etc. as one of the important risk factor in Alzheimer’s disease (AD). Since,
d
-ribose shows highest glycation ability among other sugars hence, produces advanced glycation end products (AGEs) rapidly. However, there are several other mechanisms suggested by researchers through which
d
-ribose may cause cognitive impairments. There is a concern related to diabetic patients since they also suffer from
d
-ribose metabolism, may be more prone to AD risk. Thus, it is imperative that the pathogenesis and the pathways involved in AD progression are explored in the light of ribosylation and AGEs formation for identifying suitable diagnostics marker for early diagnosis or finding promising therapeutic outcomes. |
| doi_str_mv | 10.1007/s11033-020-05243-7 |
| format | Article |
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d
-ribose shows highest glycation ability among other sugars hence, produces advanced glycation end products (AGEs) rapidly. However, there are several other mechanisms suggested by researchers through which
d
-ribose may cause cognitive impairments. There is a concern related to diabetic patients since they also suffer from
d
-ribose metabolism, may be more prone to AD risk. Thus, it is imperative that the pathogenesis and the pathways involved in AD progression are explored in the light of ribosylation and AGEs formation for identifying suitable diagnostics marker for early diagnosis or finding promising therapeutic outcomes.</description><identifier>ISSN: 0301-4851</identifier><identifier>EISSN: 1573-4978</identifier><identifier>DOI: 10.1007/s11033-020-05243-7</identifier><identifier>PMID: 31933261</identifier><language>eng</language><publisher>Dordrecht: Springer Netherlands</publisher><subject>Advanced glycosylation end products ; Aging ; Alzheimer Disease - etiology ; Alzheimer Disease - metabolism ; Alzheimer Disease - pathology ; Alzheimer Disease - physiopathology ; Alzheimer's disease ; Amyloid beta-Peptides - metabolism ; Amyloid beta-Protein Precursor - genetics ; Amyloid beta-Protein Precursor - metabolism ; Animal Anatomy ; Animal Biochemistry ; Animals ; Biomedical and Life Sciences ; Cognitive ability ; D-Ribose ; Dementia disorders ; Diabetes mellitus ; Disease Management ; Disease Susceptibility ; Glycation End Products, Advanced - metabolism ; Glycosylation ; Histology ; Humans ; Life Sciences ; Morphology ; Neurodegenerative diseases ; Neurodegenerative Diseases - etiology ; Neurodegenerative Diseases - metabolism ; Neurodegenerative Diseases - pathology ; Neurodegenerative Diseases - physiopathology ; Neurons - metabolism ; Neurons - pathology ; Pathogenesis ; Protein Processing, Post-Translational ; Proteolysis ; Receptor for Advanced Glycation End Products - metabolism ; Review ; Ribose - chemistry ; Ribose - metabolism ; Ribosylation ; Risk factors ; Signal Transduction ; Structure-Activity Relationship ; Tau protein</subject><ispartof>Molecular biology reports, 2020-03, Vol.47 (3), p.2289-2299</ispartof><rights>Springer Nature B.V. 2020</rights><rights>Molecular Biology Reports is a copyright of Springer, (2020). All Rights Reserved.</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c375t-1e27d0ea7928a23051a03975375ea7a47f65a46b925a23657eaaf328eea905d93</citedby><cites>FETCH-LOGICAL-c375t-1e27d0ea7928a23051a03975375ea7a47f65a46b925a23657eaaf328eea905d93</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://link.springer.com/content/pdf/10.1007/s11033-020-05243-7$$EPDF$$P50$$Gspringer$$H</linktopdf><linktohtml>$$Uhttps://link.springer.com/10.1007/s11033-020-05243-7$$EHTML$$P50$$Gspringer$$H</linktohtml><link.rule.ids>314,780,784,27924,27925,41488,42557,51319</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/31933261$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Javed, Mehjbeen</creatorcontrib><creatorcontrib>Ahmad, Md. Irshad</creatorcontrib><creatorcontrib>Javed, Hina</creatorcontrib><creatorcontrib>Naseem, Sufia</creatorcontrib><title>d-ribose and pathogenesis of Alzheimer’s disease</title><title>Molecular biology reports</title><addtitle>Mol Biol Rep</addtitle><addtitle>Mol Biol Rep</addtitle><description>It is estimated that the global prevalence of dementia will rise as high as 24 million and predicted to be double in every 20 years which is attributed to the fact that the ageing population is increasing and so more individuals are at risk of developing neurodegenerative diseases like Alzheimer’s. Many scientists favored glycation of proteins such as tau, amyloid beta (Aβ) etc. as one of the important risk factor in Alzheimer’s disease (AD). Since,
d
-ribose shows highest glycation ability among other sugars hence, produces advanced glycation end products (AGEs) rapidly. However, there are several other mechanisms suggested by researchers through which
d
-ribose may cause cognitive impairments. There is a concern related to diabetic patients since they also suffer from
d
-ribose metabolism, may be more prone to AD risk. Thus, it is imperative that the pathogenesis and the pathways involved in AD progression are explored in the light of ribosylation and AGEs formation for identifying suitable diagnostics marker for early diagnosis or finding promising therapeutic outcomes.</description><subject>Advanced glycosylation end products</subject><subject>Aging</subject><subject>Alzheimer Disease - etiology</subject><subject>Alzheimer Disease - metabolism</subject><subject>Alzheimer Disease - pathology</subject><subject>Alzheimer Disease - physiopathology</subject><subject>Alzheimer's disease</subject><subject>Amyloid beta-Peptides - metabolism</subject><subject>Amyloid beta-Protein Precursor - genetics</subject><subject>Amyloid beta-Protein Precursor - metabolism</subject><subject>Animal Anatomy</subject><subject>Animal Biochemistry</subject><subject>Animals</subject><subject>Biomedical and Life Sciences</subject><subject>Cognitive ability</subject><subject>D-Ribose</subject><subject>Dementia disorders</subject><subject>Diabetes mellitus</subject><subject>Disease Management</subject><subject>Disease Susceptibility</subject><subject>Glycation End Products, Advanced - metabolism</subject><subject>Glycosylation</subject><subject>Histology</subject><subject>Humans</subject><subject>Life Sciences</subject><subject>Morphology</subject><subject>Neurodegenerative diseases</subject><subject>Neurodegenerative Diseases - etiology</subject><subject>Neurodegenerative Diseases - metabolism</subject><subject>Neurodegenerative Diseases - pathology</subject><subject>Neurodegenerative Diseases - physiopathology</subject><subject>Neurons - metabolism</subject><subject>Neurons - pathology</subject><subject>Pathogenesis</subject><subject>Protein Processing, Post-Translational</subject><subject>Proteolysis</subject><subject>Receptor for Advanced Glycation End Products - metabolism</subject><subject>Review</subject><subject>Ribose - chemistry</subject><subject>Ribose - metabolism</subject><subject>Ribosylation</subject><subject>Risk factors</subject><subject>Signal Transduction</subject><subject>Structure-Activity Relationship</subject><subject>Tau protein</subject><issn>0301-4851</issn><issn>1573-4978</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2020</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><sourceid>ABUWG</sourceid><sourceid>AFKRA</sourceid><sourceid>AZQEC</sourceid><sourceid>BENPR</sourceid><sourceid>CCPQU</sourceid><sourceid>DWQXO</sourceid><sourceid>GNUQQ</sourceid><recordid>eNp9kL1OwzAQxy0EoqXwAgwoErPhzhfHyVhVFJAqscBsuc2lTdUmxW4HmHgNXo8nwZACG9NJ9_-SfkKcI1whgLkOiEAkQYEErVKS5kD0URuSaWHyQ9EHApRprrEnTkJYAkCKRh-LHmFBpDLsC1VKX0_bwIlrymTjtot2zg2HOiRtlQxXrwuu1-w_3t5DUtaBXeBTcVS5VeCz_R2Ip_HN4-hOTh5u70fDiZyR0VuJrEwJ7EyhcqcINDqgwugoxqdLTZVpl2bTQukoZ9qwcxWpnNkVoMuCBuKy69349nnHYWuX7c43cdIqMmAQ01xFl-pcM9-G4LmyG1-vnX-xCPYLk-0w2YjJfmOyJoYu9tW76ZrL38gPl2igzhCi1MzZ_23_U_sJoKRxQQ</recordid><startdate>20200301</startdate><enddate>20200301</enddate><creator>Javed, Mehjbeen</creator><creator>Ahmad, Md. Irshad</creator><creator>Javed, Hina</creator><creator>Naseem, Sufia</creator><general>Springer Netherlands</general><general>Springer Nature B.V</general><scope>CGR</scope><scope>CUY</scope><scope>CVF</scope><scope>ECM</scope><scope>EIF</scope><scope>NPM</scope><scope>AAYXX</scope><scope>CITATION</scope><scope>3V.</scope><scope>7TK</scope><scope>7TM</scope><scope>7X7</scope><scope>7XB</scope><scope>88A</scope><scope>88E</scope><scope>88I</scope><scope>8AO</scope><scope>8FD</scope><scope>8FE</scope><scope>8FH</scope><scope>8FI</scope><scope>8FJ</scope><scope>8FK</scope><scope>ABUWG</scope><scope>AFKRA</scope><scope>AZQEC</scope><scope>BBNVY</scope><scope>BENPR</scope><scope>BHPHI</scope><scope>CCPQU</scope><scope>DWQXO</scope><scope>FR3</scope><scope>FYUFA</scope><scope>GHDGH</scope><scope>GNUQQ</scope><scope>HCIFZ</scope><scope>K9.</scope><scope>LK8</scope><scope>M0S</scope><scope>M1P</scope><scope>M2P</scope><scope>M7P</scope><scope>P64</scope><scope>PQEST</scope><scope>PQQKQ</scope><scope>PQUKI</scope><scope>PRINS</scope><scope>Q9U</scope><scope>RC3</scope></search><sort><creationdate>20200301</creationdate><title>d-ribose and pathogenesis of Alzheimer’s disease</title><author>Javed, Mehjbeen ; Ahmad, Md. Irshad ; Javed, Hina ; Naseem, Sufia</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c375t-1e27d0ea7928a23051a03975375ea7a47f65a46b925a23657eaaf328eea905d93</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2020</creationdate><topic>Advanced glycosylation end products</topic><topic>Aging</topic><topic>Alzheimer Disease - etiology</topic><topic>Alzheimer Disease - metabolism</topic><topic>Alzheimer Disease - pathology</topic><topic>Alzheimer Disease - physiopathology</topic><topic>Alzheimer's disease</topic><topic>Amyloid beta-Peptides - metabolism</topic><topic>Amyloid beta-Protein Precursor - genetics</topic><topic>Amyloid beta-Protein Precursor - metabolism</topic><topic>Animal Anatomy</topic><topic>Animal Biochemistry</topic><topic>Animals</topic><topic>Biomedical and Life Sciences</topic><topic>Cognitive ability</topic><topic>D-Ribose</topic><topic>Dementia disorders</topic><topic>Diabetes mellitus</topic><topic>Disease Management</topic><topic>Disease Susceptibility</topic><topic>Glycation End Products, Advanced - metabolism</topic><topic>Glycosylation</topic><topic>Histology</topic><topic>Humans</topic><topic>Life Sciences</topic><topic>Morphology</topic><topic>Neurodegenerative diseases</topic><topic>Neurodegenerative Diseases - etiology</topic><topic>Neurodegenerative Diseases - metabolism</topic><topic>Neurodegenerative Diseases - pathology</topic><topic>Neurodegenerative Diseases - physiopathology</topic><topic>Neurons - metabolism</topic><topic>Neurons - pathology</topic><topic>Pathogenesis</topic><topic>Protein Processing, Post-Translational</topic><topic>Proteolysis</topic><topic>Receptor for Advanced Glycation End Products - metabolism</topic><topic>Review</topic><topic>Ribose - chemistry</topic><topic>Ribose - metabolism</topic><topic>Ribosylation</topic><topic>Risk factors</topic><topic>Signal Transduction</topic><topic>Structure-Activity Relationship</topic><topic>Tau protein</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Javed, Mehjbeen</creatorcontrib><creatorcontrib>Ahmad, Md. 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Irshad</au><au>Javed, Hina</au><au>Naseem, Sufia</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>d-ribose and pathogenesis of Alzheimer’s disease</atitle><jtitle>Molecular biology reports</jtitle><stitle>Mol Biol Rep</stitle><addtitle>Mol Biol Rep</addtitle><date>2020-03-01</date><risdate>2020</risdate><volume>47</volume><issue>3</issue><spage>2289</spage><epage>2299</epage><pages>2289-2299</pages><issn>0301-4851</issn><eissn>1573-4978</eissn><abstract>It is estimated that the global prevalence of dementia will rise as high as 24 million and predicted to be double in every 20 years which is attributed to the fact that the ageing population is increasing and so more individuals are at risk of developing neurodegenerative diseases like Alzheimer’s. Many scientists favored glycation of proteins such as tau, amyloid beta (Aβ) etc. as one of the important risk factor in Alzheimer’s disease (AD). Since,
d
-ribose shows highest glycation ability among other sugars hence, produces advanced glycation end products (AGEs) rapidly. However, there are several other mechanisms suggested by researchers through which
d
-ribose may cause cognitive impairments. There is a concern related to diabetic patients since they also suffer from
d
-ribose metabolism, may be more prone to AD risk. Thus, it is imperative that the pathogenesis and the pathways involved in AD progression are explored in the light of ribosylation and AGEs formation for identifying suitable diagnostics marker for early diagnosis or finding promising therapeutic outcomes.</abstract><cop>Dordrecht</cop><pub>Springer Netherlands</pub><pmid>31933261</pmid><doi>10.1007/s11033-020-05243-7</doi><tpages>11</tpages></addata></record> |
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| subjects | Advanced glycosylation end products Aging Alzheimer Disease - etiology Alzheimer Disease - metabolism Alzheimer Disease - pathology Alzheimer Disease - physiopathology Alzheimer's disease Amyloid beta-Peptides - metabolism Amyloid beta-Protein Precursor - genetics Amyloid beta-Protein Precursor - metabolism Animal Anatomy Animal Biochemistry Animals Biomedical and Life Sciences Cognitive ability D-Ribose Dementia disorders Diabetes mellitus Disease Management Disease Susceptibility Glycation End Products, Advanced - metabolism Glycosylation Histology Humans Life Sciences Morphology Neurodegenerative diseases Neurodegenerative Diseases - etiology Neurodegenerative Diseases - metabolism Neurodegenerative Diseases - pathology Neurodegenerative Diseases - physiopathology Neurons - metabolism Neurons - pathology Pathogenesis Protein Processing, Post-Translational Proteolysis Receptor for Advanced Glycation End Products - metabolism Review Ribose - chemistry Ribose - metabolism Ribosylation Risk factors Signal Transduction Structure-Activity Relationship Tau protein |
| title | d-ribose and pathogenesis of Alzheimer’s disease |
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