Disaggregases, molecular chaperones that resolubilize protein aggregates
The process of folding is a seminal event in the life of a protein, as it is essential for proper protein function and therefore cell physiology. Inappropriate folding, or misfolding, can not only lead to loss of function, but also to the formation of protein aggregates, an insoluble association of...
Ausführliche Beschreibung
Gespeichert in:
| Autor*in: |
Mokry, David Z [verfasserIn] |
|---|
| Format: |
Artikel |
|---|---|
| Sprache: |
Englisch |
| Erschienen: |
2015 |
|---|
| Schlagwörter: |
|---|
| Übergeordnetes Werk: |
Enthalten in: Anais da Academia Brasileira de Ciências - Rio de Janeiro, 1929, 87(2015), 2, Seite 1273 |
|---|---|
| Übergeordnetes Werk: |
volume:87 ; year:2015 ; number:2 ; pages:1273 |
| Links: |
|---|
| Katalog-ID: |
OLC1963744519 |
|---|
| LEADER | 01000caa a2200265 4500 | ||
|---|---|---|---|
| 001 | OLC1963744519 | ||
| 003 | DE-627 | ||
| 005 | 20230511115854.0 | ||
| 007 | tu | ||
| 008 | 160206s2015 xx ||||| 00| ||eng c | ||
| 028 | 5 | 2 | |a PQ20160617 |
| 035 | |a (DE-627)OLC1963744519 | ||
| 035 | |a (DE-599)GBVOLC1963744519 | ||
| 035 | |a (PRQ)p1322-1153e5c8740327233cd6c4a94789770d88b7543633f1511e54203c6a41ce65ea3 | ||
| 035 | |a (KEY)0020595820150000087000201273disaggregasesmolecularchaperonesthatresolubilizepr | ||
| 040 | |a DE-627 |b ger |c DE-627 |e rakwb | ||
| 041 | |a eng | ||
| 082 | 0 | 4 | |a 000 |q DNB |
| 082 | 0 | 4 | |a 500 |q AVZ |
| 084 | |a 30.00 |2 bkl | ||
| 100 | 1 | |a Mokry, David Z |e verfasserin |4 aut | |
| 245 | 1 | 0 | |a Disaggregases, molecular chaperones that resolubilize protein aggregates |
| 264 | 1 | |c 2015 | |
| 336 | |a Text |b txt |2 rdacontent | ||
| 337 | |a ohne Hilfsmittel zu benutzen |b n |2 rdamedia | ||
| 338 | |a Band |b nc |2 rdacarrier | ||
| 520 | |a The process of folding is a seminal event in the life of a protein, as it is essential for proper protein function and therefore cell physiology. Inappropriate folding, or misfolding, can not only lead to loss of function, but also to the formation of protein aggregates, an insoluble association of polypeptides that harm cell physiology, either by themselves or in the process of formation. Several biological processes have evolved to prevent and eliminate the existence of non-functional and amyloidogenic aggregates, as they are associated with several human pathologies. Molecular chaperones and heat shock proteins are specialized in controlling the quality of the proteins in the cell, specifically by aiding proper folding, and dissolution and clearance of already formed protein aggregates. The latter is a function of disaggregases, mainly represented by the ClpB/Hsp104 subfamily of molecular chaperones, that are ubiquitous in all organisms but, surprisingly, have no orthologs in the cytosol of metazoan cells. This review aims to describe the characteristics of disaggregases and to discuss the function of yeast Hsp104, a disaggregase that is also involved in prion propagation and inheritance. | ||
| 650 | 4 | |a disaggregase | |
| 650 | 4 | |a shock protein | |
| 650 | 4 | |a prion | |
| 650 | 4 | |a molecular chaperones | |
| 650 | 4 | |a protein folding | |
| 650 | 4 | |a amyloid | |
| 700 | 1 | |a Abrahão, Josielle |4 oth | |
| 700 | 1 | |a Ramos, Carlos H.I |4 oth | |
| 773 | 0 | 8 | |i Enthalten in |t Anais da Academia Brasileira de Ciências |d Rio de Janeiro, 1929 |g 87(2015), 2, Seite 1273 |w (DE-627)129938955 |w (DE-600)391417-3 |w (DE-576)015500713 |x 0001-3765 |7 nnns |
| 773 | 1 | 8 | |g volume:87 |g year:2015 |g number:2 |g pages:1273 |
| 856 | 4 | 2 | |u http://www.scielo.br/scielo.php?script=sci_arttext&pid=S0001-37652015000301273 |
| 856 | 4 | 2 | |u http://www.ncbi.nlm.nih.gov/pubmed/26312418 |
| 912 | |a GBV_USEFLAG_A | ||
| 912 | |a SYSFLAG_A | ||
| 912 | |a GBV_OLC | ||
| 912 | |a SSG-OLC-PHY | ||
| 912 | |a SSG-OLC-CHE | ||
| 912 | |a SSG-OLC-IBA | ||
| 912 | |a SSG-OLC-PHA | ||
| 912 | |a SSG-OLC-DE-84 | ||
| 912 | |a GBV_ILN_40 | ||
| 912 | |a GBV_ILN_62 | ||
| 912 | |a GBV_ILN_156 | ||
| 912 | |a GBV_ILN_2399 | ||
| 936 | b | k | |a 30.00 |q AVZ |
| 951 | |a AR | ||
| 952 | |d 87 |j 2015 |e 2 |h 1273 | ||
| author_variant |
d z m dz dzm |
|---|---|
| matchkey_str |
article:00013765:2015----::iageaemlclrhprnshteouiie |
| hierarchy_sort_str |
2015 |
| bklnumber |
30.00 |
| publishDate |
2015 |
| allfields |
PQ20160617 (DE-627)OLC1963744519 (DE-599)GBVOLC1963744519 (PRQ)p1322-1153e5c8740327233cd6c4a94789770d88b7543633f1511e54203c6a41ce65ea3 (KEY)0020595820150000087000201273disaggregasesmolecularchaperonesthatresolubilizepr DE-627 ger DE-627 rakwb eng 000 DNB 500 AVZ 30.00 bkl Mokry, David Z verfasserin aut Disaggregases, molecular chaperones that resolubilize protein aggregates 2015 Text txt rdacontent ohne Hilfsmittel zu benutzen n rdamedia Band nc rdacarrier The process of folding is a seminal event in the life of a protein, as it is essential for proper protein function and therefore cell physiology. Inappropriate folding, or misfolding, can not only lead to loss of function, but also to the formation of protein aggregates, an insoluble association of polypeptides that harm cell physiology, either by themselves or in the process of formation. Several biological processes have evolved to prevent and eliminate the existence of non-functional and amyloidogenic aggregates, as they are associated with several human pathologies. Molecular chaperones and heat shock proteins are specialized in controlling the quality of the proteins in the cell, specifically by aiding proper folding, and dissolution and clearance of already formed protein aggregates. The latter is a function of disaggregases, mainly represented by the ClpB/Hsp104 subfamily of molecular chaperones, that are ubiquitous in all organisms but, surprisingly, have no orthologs in the cytosol of metazoan cells. This review aims to describe the characteristics of disaggregases and to discuss the function of yeast Hsp104, a disaggregase that is also involved in prion propagation and inheritance. disaggregase shock protein prion molecular chaperones protein folding amyloid Abrahão, Josielle oth Ramos, Carlos H.I oth Enthalten in Anais da Academia Brasileira de Ciências Rio de Janeiro, 1929 87(2015), 2, Seite 1273 (DE-627)129938955 (DE-600)391417-3 (DE-576)015500713 0001-3765 nnns volume:87 year:2015 number:2 pages:1273 http://www.scielo.br/scielo.php?script=sci_arttext&pid=S0001-37652015000301273 http://www.ncbi.nlm.nih.gov/pubmed/26312418 GBV_USEFLAG_A SYSFLAG_A GBV_OLC SSG-OLC-PHY SSG-OLC-CHE SSG-OLC-IBA SSG-OLC-PHA SSG-OLC-DE-84 GBV_ILN_40 GBV_ILN_62 GBV_ILN_156 GBV_ILN_2399 30.00 AVZ AR 87 2015 2 1273 |
| spelling |
PQ20160617 (DE-627)OLC1963744519 (DE-599)GBVOLC1963744519 (PRQ)p1322-1153e5c8740327233cd6c4a94789770d88b7543633f1511e54203c6a41ce65ea3 (KEY)0020595820150000087000201273disaggregasesmolecularchaperonesthatresolubilizepr DE-627 ger DE-627 rakwb eng 000 DNB 500 AVZ 30.00 bkl Mokry, David Z verfasserin aut Disaggregases, molecular chaperones that resolubilize protein aggregates 2015 Text txt rdacontent ohne Hilfsmittel zu benutzen n rdamedia Band nc rdacarrier The process of folding is a seminal event in the life of a protein, as it is essential for proper protein function and therefore cell physiology. Inappropriate folding, or misfolding, can not only lead to loss of function, but also to the formation of protein aggregates, an insoluble association of polypeptides that harm cell physiology, either by themselves or in the process of formation. Several biological processes have evolved to prevent and eliminate the existence of non-functional and amyloidogenic aggregates, as they are associated with several human pathologies. Molecular chaperones and heat shock proteins are specialized in controlling the quality of the proteins in the cell, specifically by aiding proper folding, and dissolution and clearance of already formed protein aggregates. The latter is a function of disaggregases, mainly represented by the ClpB/Hsp104 subfamily of molecular chaperones, that are ubiquitous in all organisms but, surprisingly, have no orthologs in the cytosol of metazoan cells. This review aims to describe the characteristics of disaggregases and to discuss the function of yeast Hsp104, a disaggregase that is also involved in prion propagation and inheritance. disaggregase shock protein prion molecular chaperones protein folding amyloid Abrahão, Josielle oth Ramos, Carlos H.I oth Enthalten in Anais da Academia Brasileira de Ciências Rio de Janeiro, 1929 87(2015), 2, Seite 1273 (DE-627)129938955 (DE-600)391417-3 (DE-576)015500713 0001-3765 nnns volume:87 year:2015 number:2 pages:1273 http://www.scielo.br/scielo.php?script=sci_arttext&pid=S0001-37652015000301273 http://www.ncbi.nlm.nih.gov/pubmed/26312418 GBV_USEFLAG_A SYSFLAG_A GBV_OLC SSG-OLC-PHY SSG-OLC-CHE SSG-OLC-IBA SSG-OLC-PHA SSG-OLC-DE-84 GBV_ILN_40 GBV_ILN_62 GBV_ILN_156 GBV_ILN_2399 30.00 AVZ AR 87 2015 2 1273 |
| allfields_unstemmed |
PQ20160617 (DE-627)OLC1963744519 (DE-599)GBVOLC1963744519 (PRQ)p1322-1153e5c8740327233cd6c4a94789770d88b7543633f1511e54203c6a41ce65ea3 (KEY)0020595820150000087000201273disaggregasesmolecularchaperonesthatresolubilizepr DE-627 ger DE-627 rakwb eng 000 DNB 500 AVZ 30.00 bkl Mokry, David Z verfasserin aut Disaggregases, molecular chaperones that resolubilize protein aggregates 2015 Text txt rdacontent ohne Hilfsmittel zu benutzen n rdamedia Band nc rdacarrier The process of folding is a seminal event in the life of a protein, as it is essential for proper protein function and therefore cell physiology. Inappropriate folding, or misfolding, can not only lead to loss of function, but also to the formation of protein aggregates, an insoluble association of polypeptides that harm cell physiology, either by themselves or in the process of formation. Several biological processes have evolved to prevent and eliminate the existence of non-functional and amyloidogenic aggregates, as they are associated with several human pathologies. Molecular chaperones and heat shock proteins are specialized in controlling the quality of the proteins in the cell, specifically by aiding proper folding, and dissolution and clearance of already formed protein aggregates. The latter is a function of disaggregases, mainly represented by the ClpB/Hsp104 subfamily of molecular chaperones, that are ubiquitous in all organisms but, surprisingly, have no orthologs in the cytosol of metazoan cells. This review aims to describe the characteristics of disaggregases and to discuss the function of yeast Hsp104, a disaggregase that is also involved in prion propagation and inheritance. disaggregase shock protein prion molecular chaperones protein folding amyloid Abrahão, Josielle oth Ramos, Carlos H.I oth Enthalten in Anais da Academia Brasileira de Ciências Rio de Janeiro, 1929 87(2015), 2, Seite 1273 (DE-627)129938955 (DE-600)391417-3 (DE-576)015500713 0001-3765 nnns volume:87 year:2015 number:2 pages:1273 http://www.scielo.br/scielo.php?script=sci_arttext&pid=S0001-37652015000301273 http://www.ncbi.nlm.nih.gov/pubmed/26312418 GBV_USEFLAG_A SYSFLAG_A GBV_OLC SSG-OLC-PHY SSG-OLC-CHE SSG-OLC-IBA SSG-OLC-PHA SSG-OLC-DE-84 GBV_ILN_40 GBV_ILN_62 GBV_ILN_156 GBV_ILN_2399 30.00 AVZ AR 87 2015 2 1273 |
| allfieldsGer |
PQ20160617 (DE-627)OLC1963744519 (DE-599)GBVOLC1963744519 (PRQ)p1322-1153e5c8740327233cd6c4a94789770d88b7543633f1511e54203c6a41ce65ea3 (KEY)0020595820150000087000201273disaggregasesmolecularchaperonesthatresolubilizepr DE-627 ger DE-627 rakwb eng 000 DNB 500 AVZ 30.00 bkl Mokry, David Z verfasserin aut Disaggregases, molecular chaperones that resolubilize protein aggregates 2015 Text txt rdacontent ohne Hilfsmittel zu benutzen n rdamedia Band nc rdacarrier The process of folding is a seminal event in the life of a protein, as it is essential for proper protein function and therefore cell physiology. Inappropriate folding, or misfolding, can not only lead to loss of function, but also to the formation of protein aggregates, an insoluble association of polypeptides that harm cell physiology, either by themselves or in the process of formation. Several biological processes have evolved to prevent and eliminate the existence of non-functional and amyloidogenic aggregates, as they are associated with several human pathologies. Molecular chaperones and heat shock proteins are specialized in controlling the quality of the proteins in the cell, specifically by aiding proper folding, and dissolution and clearance of already formed protein aggregates. The latter is a function of disaggregases, mainly represented by the ClpB/Hsp104 subfamily of molecular chaperones, that are ubiquitous in all organisms but, surprisingly, have no orthologs in the cytosol of metazoan cells. This review aims to describe the characteristics of disaggregases and to discuss the function of yeast Hsp104, a disaggregase that is also involved in prion propagation and inheritance. disaggregase shock protein prion molecular chaperones protein folding amyloid Abrahão, Josielle oth Ramos, Carlos H.I oth Enthalten in Anais da Academia Brasileira de Ciências Rio de Janeiro, 1929 87(2015), 2, Seite 1273 (DE-627)129938955 (DE-600)391417-3 (DE-576)015500713 0001-3765 nnns volume:87 year:2015 number:2 pages:1273 http://www.scielo.br/scielo.php?script=sci_arttext&pid=S0001-37652015000301273 http://www.ncbi.nlm.nih.gov/pubmed/26312418 GBV_USEFLAG_A SYSFLAG_A GBV_OLC SSG-OLC-PHY SSG-OLC-CHE SSG-OLC-IBA SSG-OLC-PHA SSG-OLC-DE-84 GBV_ILN_40 GBV_ILN_62 GBV_ILN_156 GBV_ILN_2399 30.00 AVZ AR 87 2015 2 1273 |
| allfieldsSound |
PQ20160617 (DE-627)OLC1963744519 (DE-599)GBVOLC1963744519 (PRQ)p1322-1153e5c8740327233cd6c4a94789770d88b7543633f1511e54203c6a41ce65ea3 (KEY)0020595820150000087000201273disaggregasesmolecularchaperonesthatresolubilizepr DE-627 ger DE-627 rakwb eng 000 DNB 500 AVZ 30.00 bkl Mokry, David Z verfasserin aut Disaggregases, molecular chaperones that resolubilize protein aggregates 2015 Text txt rdacontent ohne Hilfsmittel zu benutzen n rdamedia Band nc rdacarrier The process of folding is a seminal event in the life of a protein, as it is essential for proper protein function and therefore cell physiology. Inappropriate folding, or misfolding, can not only lead to loss of function, but also to the formation of protein aggregates, an insoluble association of polypeptides that harm cell physiology, either by themselves or in the process of formation. Several biological processes have evolved to prevent and eliminate the existence of non-functional and amyloidogenic aggregates, as they are associated with several human pathologies. Molecular chaperones and heat shock proteins are specialized in controlling the quality of the proteins in the cell, specifically by aiding proper folding, and dissolution and clearance of already formed protein aggregates. The latter is a function of disaggregases, mainly represented by the ClpB/Hsp104 subfamily of molecular chaperones, that are ubiquitous in all organisms but, surprisingly, have no orthologs in the cytosol of metazoan cells. This review aims to describe the characteristics of disaggregases and to discuss the function of yeast Hsp104, a disaggregase that is also involved in prion propagation and inheritance. disaggregase shock protein prion molecular chaperones protein folding amyloid Abrahão, Josielle oth Ramos, Carlos H.I oth Enthalten in Anais da Academia Brasileira de Ciências Rio de Janeiro, 1929 87(2015), 2, Seite 1273 (DE-627)129938955 (DE-600)391417-3 (DE-576)015500713 0001-3765 nnns volume:87 year:2015 number:2 pages:1273 http://www.scielo.br/scielo.php?script=sci_arttext&pid=S0001-37652015000301273 http://www.ncbi.nlm.nih.gov/pubmed/26312418 GBV_USEFLAG_A SYSFLAG_A GBV_OLC SSG-OLC-PHY SSG-OLC-CHE SSG-OLC-IBA SSG-OLC-PHA SSG-OLC-DE-84 GBV_ILN_40 GBV_ILN_62 GBV_ILN_156 GBV_ILN_2399 30.00 AVZ AR 87 2015 2 1273 |
| language |
English |
| source |
Enthalten in Anais da Academia Brasileira de Ciências 87(2015), 2, Seite 1273 volume:87 year:2015 number:2 pages:1273 |
| sourceStr |
Enthalten in Anais da Academia Brasileira de Ciências 87(2015), 2, Seite 1273 volume:87 year:2015 number:2 pages:1273 |
| format_phy_str_mv |
Article |
| institution |
findex.gbv.de |
| topic_facet |
disaggregase shock protein prion molecular chaperones protein folding amyloid |
| dewey-raw |
000 |
| isfreeaccess_bool |
false |
| container_title |
Anais da Academia Brasileira de Ciências |
| authorswithroles_txt_mv |
Mokry, David Z @@aut@@ Abrahão, Josielle @@oth@@ Ramos, Carlos H.I @@oth@@ |
| publishDateDaySort_date |
2015-01-01T00:00:00Z |
| hierarchy_top_id |
129938955 |
| dewey-sort |
0 |
| id |
OLC1963744519 |
| language_de |
englisch |
| fullrecord |
<?xml version="1.0" encoding="UTF-8"?><collection xmlns="http://www.loc.gov/MARC21/slim"><record><leader>01000caa a2200265 4500</leader><controlfield tag="001">OLC1963744519</controlfield><controlfield tag="003">DE-627</controlfield><controlfield tag="005">20230511115854.0</controlfield><controlfield tag="007">tu</controlfield><controlfield tag="008">160206s2015 xx ||||| 00| ||eng c</controlfield><datafield tag="028" ind1="5" ind2="2"><subfield code="a">PQ20160617</subfield></datafield><datafield tag="035" ind1=" " ind2=" "><subfield code="a">(DE-627)OLC1963744519</subfield></datafield><datafield tag="035" ind1=" " ind2=" "><subfield code="a">(DE-599)GBVOLC1963744519</subfield></datafield><datafield tag="035" ind1=" " ind2=" "><subfield code="a">(PRQ)p1322-1153e5c8740327233cd6c4a94789770d88b7543633f1511e54203c6a41ce65ea3</subfield></datafield><datafield tag="035" ind1=" " ind2=" "><subfield code="a">(KEY)0020595820150000087000201273disaggregasesmolecularchaperonesthatresolubilizepr</subfield></datafield><datafield tag="040" ind1=" " ind2=" "><subfield code="a">DE-627</subfield><subfield code="b">ger</subfield><subfield code="c">DE-627</subfield><subfield code="e">rakwb</subfield></datafield><datafield tag="041" ind1=" " ind2=" "><subfield code="a">eng</subfield></datafield><datafield tag="082" ind1="0" ind2="4"><subfield code="a">000</subfield><subfield code="q">DNB</subfield></datafield><datafield tag="082" ind1="0" ind2="4"><subfield code="a">500</subfield><subfield code="q">AVZ</subfield></datafield><datafield tag="084" ind1=" " ind2=" "><subfield code="a">30.00</subfield><subfield code="2">bkl</subfield></datafield><datafield tag="100" ind1="1" ind2=" "><subfield code="a">Mokry, David Z</subfield><subfield code="e">verfasserin</subfield><subfield code="4">aut</subfield></datafield><datafield tag="245" ind1="1" ind2="0"><subfield code="a">Disaggregases, molecular chaperones that resolubilize protein aggregates</subfield></datafield><datafield tag="264" ind1=" " ind2="1"><subfield code="c">2015</subfield></datafield><datafield tag="336" ind1=" " ind2=" "><subfield code="a">Text</subfield><subfield code="b">txt</subfield><subfield code="2">rdacontent</subfield></datafield><datafield tag="337" ind1=" " ind2=" "><subfield code="a">ohne Hilfsmittel zu benutzen</subfield><subfield code="b">n</subfield><subfield code="2">rdamedia</subfield></datafield><datafield tag="338" ind1=" " ind2=" "><subfield code="a">Band</subfield><subfield code="b">nc</subfield><subfield code="2">rdacarrier</subfield></datafield><datafield tag="520" ind1=" " ind2=" "><subfield code="a">The process of folding is a seminal event in the life of a protein, as it is essential for proper protein function and therefore cell physiology. Inappropriate folding, or misfolding, can not only lead to loss of function, but also to the formation of protein aggregates, an insoluble association of polypeptides that harm cell physiology, either by themselves or in the process of formation. Several biological processes have evolved to prevent and eliminate the existence of non-functional and amyloidogenic aggregates, as they are associated with several human pathologies. Molecular chaperones and heat shock proteins are specialized in controlling the quality of the proteins in the cell, specifically by aiding proper folding, and dissolution and clearance of already formed protein aggregates. The latter is a function of disaggregases, mainly represented by the ClpB/Hsp104 subfamily of molecular chaperones, that are ubiquitous in all organisms but, surprisingly, have no orthologs in the cytosol of metazoan cells. This review aims to describe the characteristics of disaggregases and to discuss the function of yeast Hsp104, a disaggregase that is also involved in prion propagation and inheritance.</subfield></datafield><datafield tag="650" ind1=" " ind2="4"><subfield code="a">disaggregase</subfield></datafield><datafield tag="650" ind1=" " ind2="4"><subfield code="a">shock protein</subfield></datafield><datafield tag="650" ind1=" " ind2="4"><subfield code="a">prion</subfield></datafield><datafield tag="650" ind1=" " ind2="4"><subfield code="a">molecular chaperones</subfield></datafield><datafield tag="650" ind1=" " ind2="4"><subfield code="a">protein folding</subfield></datafield><datafield tag="650" ind1=" " ind2="4"><subfield code="a">amyloid</subfield></datafield><datafield tag="700" ind1="1" ind2=" "><subfield code="a">Abrahão, Josielle</subfield><subfield code="4">oth</subfield></datafield><datafield tag="700" ind1="1" ind2=" "><subfield code="a">Ramos, Carlos H.I</subfield><subfield code="4">oth</subfield></datafield><datafield tag="773" ind1="0" ind2="8"><subfield code="i">Enthalten in</subfield><subfield code="t">Anais da Academia Brasileira de Ciências</subfield><subfield code="d">Rio de Janeiro, 1929</subfield><subfield code="g">87(2015), 2, Seite 1273</subfield><subfield code="w">(DE-627)129938955</subfield><subfield code="w">(DE-600)391417-3</subfield><subfield code="w">(DE-576)015500713</subfield><subfield code="x">0001-3765</subfield><subfield code="7">nnns</subfield></datafield><datafield tag="773" ind1="1" ind2="8"><subfield code="g">volume:87</subfield><subfield code="g">year:2015</subfield><subfield code="g">number:2</subfield><subfield code="g">pages:1273</subfield></datafield><datafield tag="856" ind1="4" ind2="2"><subfield code="u">http://www.scielo.br/scielo.php?script=sci_arttext&pid=S0001-37652015000301273</subfield></datafield><datafield tag="856" ind1="4" ind2="2"><subfield code="u">http://www.ncbi.nlm.nih.gov/pubmed/26312418</subfield></datafield><datafield tag="912" ind1=" " ind2=" "><subfield code="a">GBV_USEFLAG_A</subfield></datafield><datafield tag="912" ind1=" " ind2=" "><subfield code="a">SYSFLAG_A</subfield></datafield><datafield tag="912" ind1=" " ind2=" "><subfield code="a">GBV_OLC</subfield></datafield><datafield tag="912" ind1=" " ind2=" "><subfield code="a">SSG-OLC-PHY</subfield></datafield><datafield tag="912" ind1=" " ind2=" "><subfield code="a">SSG-OLC-CHE</subfield></datafield><datafield tag="912" ind1=" " ind2=" "><subfield code="a">SSG-OLC-IBA</subfield></datafield><datafield tag="912" ind1=" " ind2=" "><subfield code="a">SSG-OLC-PHA</subfield></datafield><datafield tag="912" ind1=" " ind2=" "><subfield code="a">SSG-OLC-DE-84</subfield></datafield><datafield tag="912" ind1=" " ind2=" "><subfield code="a">GBV_ILN_40</subfield></datafield><datafield tag="912" ind1=" " ind2=" "><subfield code="a">GBV_ILN_62</subfield></datafield><datafield tag="912" ind1=" " ind2=" "><subfield code="a">GBV_ILN_156</subfield></datafield><datafield tag="912" ind1=" " ind2=" "><subfield code="a">GBV_ILN_2399</subfield></datafield><datafield tag="936" ind1="b" ind2="k"><subfield code="a">30.00</subfield><subfield code="q">AVZ</subfield></datafield><datafield tag="951" ind1=" " ind2=" "><subfield code="a">AR</subfield></datafield><datafield tag="952" ind1=" " ind2=" "><subfield code="d">87</subfield><subfield code="j">2015</subfield><subfield code="e">2</subfield><subfield code="h">1273</subfield></datafield></record></collection>
|
| author |
Mokry, David Z |
| spellingShingle |
Mokry, David Z ddc 000 ddc 500 bkl 30.00 misc disaggregase misc shock protein misc prion misc molecular chaperones misc protein folding misc amyloid Disaggregases, molecular chaperones that resolubilize protein aggregates |
| authorStr |
Mokry, David Z |
| ppnlink_with_tag_str_mv |
@@773@@(DE-627)129938955 |
| format |
Article |
| dewey-ones |
000 - Computer science, information & general works 500 - Natural sciences & mathematics |
| delete_txt_mv |
keep |
| author_role |
aut |
| collection |
OLC |
| remote_str |
false |
| illustrated |
Not Illustrated |
| issn |
0001-3765 |
| topic_title |
000 DNB 500 AVZ 30.00 bkl Disaggregases, molecular chaperones that resolubilize protein aggregates disaggregase shock protein prion molecular chaperones protein folding amyloid |
| topic |
ddc 000 ddc 500 bkl 30.00 misc disaggregase misc shock protein misc prion misc molecular chaperones misc protein folding misc amyloid |
| topic_unstemmed |
ddc 000 ddc 500 bkl 30.00 misc disaggregase misc shock protein misc prion misc molecular chaperones misc protein folding misc amyloid |
| topic_browse |
ddc 000 ddc 500 bkl 30.00 misc disaggregase misc shock protein misc prion misc molecular chaperones misc protein folding misc amyloid |
| format_facet |
Aufsätze Gedruckte Aufsätze |
| format_main_str_mv |
Text Zeitschrift/Artikel |
| carriertype_str_mv |
nc |
| author2_variant |
j a ja c h r ch chr |
| hierarchy_parent_title |
Anais da Academia Brasileira de Ciências |
| hierarchy_parent_id |
129938955 |
| dewey-tens |
000 - Computer science, knowledge & systems 500 - Science |
| hierarchy_top_title |
Anais da Academia Brasileira de Ciências |
| isfreeaccess_txt |
false |
| familylinks_str_mv |
(DE-627)129938955 (DE-600)391417-3 (DE-576)015500713 |
| title |
Disaggregases, molecular chaperones that resolubilize protein aggregates |
| ctrlnum |
(DE-627)OLC1963744519 (DE-599)GBVOLC1963744519 (PRQ)p1322-1153e5c8740327233cd6c4a94789770d88b7543633f1511e54203c6a41ce65ea3 (KEY)0020595820150000087000201273disaggregasesmolecularchaperonesthatresolubilizepr |
| title_full |
Disaggregases, molecular chaperones that resolubilize protein aggregates |
| author_sort |
Mokry, David Z |
| journal |
Anais da Academia Brasileira de Ciências |
| journalStr |
Anais da Academia Brasileira de Ciências |
| lang_code |
eng |
| isOA_bool |
false |
| dewey-hundreds |
000 - Computer science, information & general works 500 - Science |
| recordtype |
marc |
| publishDateSort |
2015 |
| contenttype_str_mv |
txt |
| container_start_page |
1273 |
| author_browse |
Mokry, David Z |
| container_volume |
87 |
| class |
000 DNB 500 AVZ 30.00 bkl |
| format_se |
Aufsätze |
| author-letter |
Mokry, David Z |
| dewey-full |
000 500 |
| title_sort |
disaggregases, molecular chaperones that resolubilize protein aggregates |
| title_auth |
Disaggregases, molecular chaperones that resolubilize protein aggregates |
| abstract |
The process of folding is a seminal event in the life of a protein, as it is essential for proper protein function and therefore cell physiology. Inappropriate folding, or misfolding, can not only lead to loss of function, but also to the formation of protein aggregates, an insoluble association of polypeptides that harm cell physiology, either by themselves or in the process of formation. Several biological processes have evolved to prevent and eliminate the existence of non-functional and amyloidogenic aggregates, as they are associated with several human pathologies. Molecular chaperones and heat shock proteins are specialized in controlling the quality of the proteins in the cell, specifically by aiding proper folding, and dissolution and clearance of already formed protein aggregates. The latter is a function of disaggregases, mainly represented by the ClpB/Hsp104 subfamily of molecular chaperones, that are ubiquitous in all organisms but, surprisingly, have no orthologs in the cytosol of metazoan cells. This review aims to describe the characteristics of disaggregases and to discuss the function of yeast Hsp104, a disaggregase that is also involved in prion propagation and inheritance. |
| abstractGer |
The process of folding is a seminal event in the life of a protein, as it is essential for proper protein function and therefore cell physiology. Inappropriate folding, or misfolding, can not only lead to loss of function, but also to the formation of protein aggregates, an insoluble association of polypeptides that harm cell physiology, either by themselves or in the process of formation. Several biological processes have evolved to prevent and eliminate the existence of non-functional and amyloidogenic aggregates, as they are associated with several human pathologies. Molecular chaperones and heat shock proteins are specialized in controlling the quality of the proteins in the cell, specifically by aiding proper folding, and dissolution and clearance of already formed protein aggregates. The latter is a function of disaggregases, mainly represented by the ClpB/Hsp104 subfamily of molecular chaperones, that are ubiquitous in all organisms but, surprisingly, have no orthologs in the cytosol of metazoan cells. This review aims to describe the characteristics of disaggregases and to discuss the function of yeast Hsp104, a disaggregase that is also involved in prion propagation and inheritance. |
| abstract_unstemmed |
The process of folding is a seminal event in the life of a protein, as it is essential for proper protein function and therefore cell physiology. Inappropriate folding, or misfolding, can not only lead to loss of function, but also to the formation of protein aggregates, an insoluble association of polypeptides that harm cell physiology, either by themselves or in the process of formation. Several biological processes have evolved to prevent and eliminate the existence of non-functional and amyloidogenic aggregates, as they are associated with several human pathologies. Molecular chaperones and heat shock proteins are specialized in controlling the quality of the proteins in the cell, specifically by aiding proper folding, and dissolution and clearance of already formed protein aggregates. The latter is a function of disaggregases, mainly represented by the ClpB/Hsp104 subfamily of molecular chaperones, that are ubiquitous in all organisms but, surprisingly, have no orthologs in the cytosol of metazoan cells. This review aims to describe the characteristics of disaggregases and to discuss the function of yeast Hsp104, a disaggregase that is also involved in prion propagation and inheritance. |
| collection_details |
GBV_USEFLAG_A SYSFLAG_A GBV_OLC SSG-OLC-PHY SSG-OLC-CHE SSG-OLC-IBA SSG-OLC-PHA SSG-OLC-DE-84 GBV_ILN_40 GBV_ILN_62 GBV_ILN_156 GBV_ILN_2399 |
| container_issue |
2 |
| title_short |
Disaggregases, molecular chaperones that resolubilize protein aggregates |
| url |
http://www.scielo.br/scielo.php?script=sci_arttext&pid=S0001-37652015000301273 http://www.ncbi.nlm.nih.gov/pubmed/26312418 |
| remote_bool |
false |
| author2 |
Abrahão, Josielle Ramos, Carlos H.I |
| author2Str |
Abrahão, Josielle Ramos, Carlos H.I |
| ppnlink |
129938955 |
| mediatype_str_mv |
n |
| isOA_txt |
false |
| hochschulschrift_bool |
false |
| author2_role |
oth oth |
| up_date |
2024-07-04T06:24:55.780Z |
| _version_ |
1803628624761323520 |
| fullrecord_marcxml |
<?xml version="1.0" encoding="UTF-8"?><collection xmlns="http://www.loc.gov/MARC21/slim"><record><leader>01000caa a2200265 4500</leader><controlfield tag="001">OLC1963744519</controlfield><controlfield tag="003">DE-627</controlfield><controlfield tag="005">20230511115854.0</controlfield><controlfield tag="007">tu</controlfield><controlfield tag="008">160206s2015 xx ||||| 00| ||eng c</controlfield><datafield tag="028" ind1="5" ind2="2"><subfield code="a">PQ20160617</subfield></datafield><datafield tag="035" ind1=" " ind2=" "><subfield code="a">(DE-627)OLC1963744519</subfield></datafield><datafield tag="035" ind1=" " ind2=" "><subfield code="a">(DE-599)GBVOLC1963744519</subfield></datafield><datafield tag="035" ind1=" " ind2=" "><subfield code="a">(PRQ)p1322-1153e5c8740327233cd6c4a94789770d88b7543633f1511e54203c6a41ce65ea3</subfield></datafield><datafield tag="035" ind1=" " ind2=" "><subfield code="a">(KEY)0020595820150000087000201273disaggregasesmolecularchaperonesthatresolubilizepr</subfield></datafield><datafield tag="040" ind1=" " ind2=" "><subfield code="a">DE-627</subfield><subfield code="b">ger</subfield><subfield code="c">DE-627</subfield><subfield code="e">rakwb</subfield></datafield><datafield tag="041" ind1=" " ind2=" "><subfield code="a">eng</subfield></datafield><datafield tag="082" ind1="0" ind2="4"><subfield code="a">000</subfield><subfield code="q">DNB</subfield></datafield><datafield tag="082" ind1="0" ind2="4"><subfield code="a">500</subfield><subfield code="q">AVZ</subfield></datafield><datafield tag="084" ind1=" " ind2=" "><subfield code="a">30.00</subfield><subfield code="2">bkl</subfield></datafield><datafield tag="100" ind1="1" ind2=" "><subfield code="a">Mokry, David Z</subfield><subfield code="e">verfasserin</subfield><subfield code="4">aut</subfield></datafield><datafield tag="245" ind1="1" ind2="0"><subfield code="a">Disaggregases, molecular chaperones that resolubilize protein aggregates</subfield></datafield><datafield tag="264" ind1=" " ind2="1"><subfield code="c">2015</subfield></datafield><datafield tag="336" ind1=" " ind2=" "><subfield code="a">Text</subfield><subfield code="b">txt</subfield><subfield code="2">rdacontent</subfield></datafield><datafield tag="337" ind1=" " ind2=" "><subfield code="a">ohne Hilfsmittel zu benutzen</subfield><subfield code="b">n</subfield><subfield code="2">rdamedia</subfield></datafield><datafield tag="338" ind1=" " ind2=" "><subfield code="a">Band</subfield><subfield code="b">nc</subfield><subfield code="2">rdacarrier</subfield></datafield><datafield tag="520" ind1=" " ind2=" "><subfield code="a">The process of folding is a seminal event in the life of a protein, as it is essential for proper protein function and therefore cell physiology. Inappropriate folding, or misfolding, can not only lead to loss of function, but also to the formation of protein aggregates, an insoluble association of polypeptides that harm cell physiology, either by themselves or in the process of formation. Several biological processes have evolved to prevent and eliminate the existence of non-functional and amyloidogenic aggregates, as they are associated with several human pathologies. Molecular chaperones and heat shock proteins are specialized in controlling the quality of the proteins in the cell, specifically by aiding proper folding, and dissolution and clearance of already formed protein aggregates. The latter is a function of disaggregases, mainly represented by the ClpB/Hsp104 subfamily of molecular chaperones, that are ubiquitous in all organisms but, surprisingly, have no orthologs in the cytosol of metazoan cells. This review aims to describe the characteristics of disaggregases and to discuss the function of yeast Hsp104, a disaggregase that is also involved in prion propagation and inheritance.</subfield></datafield><datafield tag="650" ind1=" " ind2="4"><subfield code="a">disaggregase</subfield></datafield><datafield tag="650" ind1=" " ind2="4"><subfield code="a">shock protein</subfield></datafield><datafield tag="650" ind1=" " ind2="4"><subfield code="a">prion</subfield></datafield><datafield tag="650" ind1=" " ind2="4"><subfield code="a">molecular chaperones</subfield></datafield><datafield tag="650" ind1=" " ind2="4"><subfield code="a">protein folding</subfield></datafield><datafield tag="650" ind1=" " ind2="4"><subfield code="a">amyloid</subfield></datafield><datafield tag="700" ind1="1" ind2=" "><subfield code="a">Abrahão, Josielle</subfield><subfield code="4">oth</subfield></datafield><datafield tag="700" ind1="1" ind2=" "><subfield code="a">Ramos, Carlos H.I</subfield><subfield code="4">oth</subfield></datafield><datafield tag="773" ind1="0" ind2="8"><subfield code="i">Enthalten in</subfield><subfield code="t">Anais da Academia Brasileira de Ciências</subfield><subfield code="d">Rio de Janeiro, 1929</subfield><subfield code="g">87(2015), 2, Seite 1273</subfield><subfield code="w">(DE-627)129938955</subfield><subfield code="w">(DE-600)391417-3</subfield><subfield code="w">(DE-576)015500713</subfield><subfield code="x">0001-3765</subfield><subfield code="7">nnns</subfield></datafield><datafield tag="773" ind1="1" ind2="8"><subfield code="g">volume:87</subfield><subfield code="g">year:2015</subfield><subfield code="g">number:2</subfield><subfield code="g">pages:1273</subfield></datafield><datafield tag="856" ind1="4" ind2="2"><subfield code="u">http://www.scielo.br/scielo.php?script=sci_arttext&pid=S0001-37652015000301273</subfield></datafield><datafield tag="856" ind1="4" ind2="2"><subfield code="u">http://www.ncbi.nlm.nih.gov/pubmed/26312418</subfield></datafield><datafield tag="912" ind1=" " ind2=" "><subfield code="a">GBV_USEFLAG_A</subfield></datafield><datafield tag="912" ind1=" " ind2=" "><subfield code="a">SYSFLAG_A</subfield></datafield><datafield tag="912" ind1=" " ind2=" "><subfield code="a">GBV_OLC</subfield></datafield><datafield tag="912" ind1=" " ind2=" "><subfield code="a">SSG-OLC-PHY</subfield></datafield><datafield tag="912" ind1=" " ind2=" "><subfield code="a">SSG-OLC-CHE</subfield></datafield><datafield tag="912" ind1=" " ind2=" "><subfield code="a">SSG-OLC-IBA</subfield></datafield><datafield tag="912" ind1=" " ind2=" "><subfield code="a">SSG-OLC-PHA</subfield></datafield><datafield tag="912" ind1=" " ind2=" "><subfield code="a">SSG-OLC-DE-84</subfield></datafield><datafield tag="912" ind1=" " ind2=" "><subfield code="a">GBV_ILN_40</subfield></datafield><datafield tag="912" ind1=" " ind2=" "><subfield code="a">GBV_ILN_62</subfield></datafield><datafield tag="912" ind1=" " ind2=" "><subfield code="a">GBV_ILN_156</subfield></datafield><datafield tag="912" ind1=" " ind2=" "><subfield code="a">GBV_ILN_2399</subfield></datafield><datafield tag="936" ind1="b" ind2="k"><subfield code="a">30.00</subfield><subfield code="q">AVZ</subfield></datafield><datafield tag="951" ind1=" " ind2=" "><subfield code="a">AR</subfield></datafield><datafield tag="952" ind1=" " ind2=" "><subfield code="d">87</subfield><subfield code="j">2015</subfield><subfield code="e">2</subfield><subfield code="h">1273</subfield></datafield></record></collection>
|
| score |
7.402446 |