schliessen

Filtern

 

Bibliotheken

Protein folding and misfolding

The manner in which a newly synthesized chain of amino acids transforms itself into a perfectly folded protein depends both on the intrinsic properties of the amino-acid sequence and on multiple contributing influences from the crowded cellular milieu. Folding and unfolding are crucial ways of regul... Full description

Journal Title: Nature Dec 18-Dec 25, 2003, Vol.426(6968), pp.884-90
Main Author: Dobson, Christopher
Format: Electronic Article Electronic Article
Language: English
Subjects:
ID: ISSN: 00280836 ; E-ISSN: 14764687
Zum Text:
SendSend as email Add to Book BagAdd to Book Bag
Staff View
recordid: proquest204513759
title: Protein folding and misfolding
format: Article
creator:
  • Dobson, Christopher
subjects:
  • Evolution, Molecular–Chemistry
  • Humans–Metabolism
  • Plaque, Amyloid–Chemistry
  • Plaque, Amyloid–Metabolism
  • Protein Conformation–Metabolism
  • Protein Denaturation–Metabolism
  • Protein Folding–Metabolism
  • Proteins–Metabolism
  • Proteins–Metabolism
  • Proteins
  • Amino Acids
  • Biochemistry
  • Proteins
ispartof: Nature, Dec 18-Dec 25, 2003, Vol.426(6968), pp.884-90
description: The manner in which a newly synthesized chain of amino acids transforms itself into a perfectly folded protein depends both on the intrinsic properties of the amino-acid sequence and on multiple contributing influences from the crowded cellular milieu. Folding and unfolding are crucial ways of regulating biological activity and targeting proteins to different cellular locations. Aggregation of misfolded proteins that escape the cellular quality-control mechanisms is a common feature of a wide range of highly debilitating and increasingly prevalent diseases. [PUBLICATION ]
language: eng
source:
identifier: ISSN: 00280836 ; E-ISSN: 14764687
fulltext: fulltext
issn:
  • 00280836
  • 0028-0836
  • 14764687
  • 1476-4687
url: Link


@attributes
ID575364875
RANK0.07
NO1
SEARCH_ENGINEprimo_central_multiple_fe
SEARCH_ENGINE_TYPEPrimo Central Search Engine
LOCALfalse
PrimoNMBib
record
control
sourcerecordid204513759
sourceidproquest
recordidTN_proquest204513759
sourcesystemPC
pqid204513759
galeid187811155
display
typearticle
titleProtein folding and misfolding
creatorDobson, Christopher
ispartofNature, Dec 18-Dec 25, 2003, Vol.426(6968), pp.884-90
identifierISSN: 00280836 ; E-ISSN: 14764687
subjectEvolution, Molecular–Chemistry ; Humans–Metabolism ; Plaque, Amyloid–Chemistry ; Plaque, Amyloid–Metabolism ; Protein Conformation–Metabolism ; Protein Denaturation–Metabolism ; Protein Folding–Metabolism ; Proteins–Metabolism ; Proteins–Metabolism ; Proteins ; Amino Acids ; Biochemistry ; Proteins
descriptionThe manner in which a newly synthesized chain of amino acids transforms itself into a perfectly folded protein depends both on the intrinsic properties of the amino-acid sequence and on multiple contributing influences from the crowded cellular milieu. Folding and unfolding are crucial ways of regulating biological activity and targeting proteins to different cellular locations. Aggregation of misfolded proteins that escape the cellular quality-control mechanisms is a common feature of a wide range of highly debilitating and increasingly prevalent diseases. [PUBLICATION ]
languageeng
source
version10
lds50peer_reviewed
links
openurl$$Topenurl_article
openurlfulltext$$Topenurlfull_article
linktorsrc$$Uhttp://search.proquest.com/docview/204513759/?pq-origsite=primo$$EView_record_in_ProQuest_(subscribers_only)
search
creatorcontribDobson, Christopher
titleProtein folding and misfolding
descriptionThe manner in which a newly synthesized chain of amino acids transforms itself into a perfectly folded protein depends both on the intrinsic properties of the amino-acid sequence and on multiple contributing influences from the crowded cellular milieu. Folding and unfolding are crucial ways of regulating biological activity and targeting proteins to different cellular locations. Aggregation of misfolded proteins that escape the cellular quality-control mechanisms is a common feature of a wide range of highly debilitating and increasingly prevalent diseases. [PUBLICATION ]
subject
0Evolution, Molecular–Chemistry
1Humans–Metabolism
2Plaque, Amyloid–Chemistry
3Plaque, Amyloid–Metabolism
4Protein Conformation–Metabolism
5Protein Denaturation–Metabolism
6Protein Folding–Metabolism
7Proteins–Metabolism
8Proteins
9Amino Acids
10Biochemistry
general
0English
1Nature Publishing Group
2Medical Database
3ProQuest Science Journals
4STEM Database (ProQuest)
5Health & Medical Collection (Alumni edition)
6Medical Database (Alumni edition)
7Nursing & Allied Health Database (Alumni edition)
8Psychology Database (Alumni edition)
9Science Database (Alumni edition)
10ProQuest Pharma Collection
11Health & Medical Collection
12Psychology Database
13Nursing & Allied Health Database
14ProQuest Biology Journals
15ProQuest Agriculture Journals
16Ecology Abstracts
17Entomology Abstracts
18Animal Behavior Abstracts
19Neurosciences Abstracts
20ProQuest Public Health
21Aquatic Science Journals
22Materials Science Database
23Advanced Technologies & Aerospace Database
24Engineering Database
25Biological Science Database
26Environmental Science Database (ProQuest)
27Earth, Atmospheric & Aquatic Science Database (ProQuest)
28Engineering Research Database
29Technology Research Database
30ProQuest Nursing & Allied Health Source
31ProQuest Research Library
32Environment Abstracts
33ProQuest Agricultural Science Collection
34ProQuest Aquatic Science Collection
35ProQuest Atmospheric Science Collection
36ProQuest Biological Science Collection
37ProQuest Central
38ProQuest Earth Science Collection
39ProQuest Engineering Collection
40ProQuest Environmental Science Collection
41ProQuest Advanced Technologies & Aerospace Collection
42ProQuest Hospital Collection
43ProQuest Materials Science Collection
44ProQuest Natural Science Collection
45ProQuest Technology Collection
46Research Library (Alumni edition)
47Hospital Premium Collection (Alumni edition)
48ProQuest SciTech Collection
49ProQuest Health & Medical Complete
50ProQuest Medical Library
51ProQuest Psychology Journals
52Agricultural & Environmental Science Database
53Earth, Atmospheric & Aquatic Science Database
54Materials Science & Engineering Database
55Natural Science Collection
56ProQuest Central (new)
57ProQuest Central K-12
58ProQuest Central Korea
59Research Library Prep
60SciTech Premium Collection
61Technology Collection
62Health Research Premium Collection
63Health Research Premium Collection (Alumni edition)
64ProQuest Central Essentials
65eLibrary
66ProQuest One Academic
67Environmental Science Index (ProQuest)
68Biological Science Index (ProQuest)
69Environmental Science Collection (ProQuest)
70Materials Science Collection (ProQuest)
71Engineering Collection (ProQuest)
sourceidproquest
recordidproquest204513759
issn
000280836
10028-0836
214764687
31476-4687
rsrctypearticle
creationdate2003
addtitleNature
searchscope
01000084
11000273
21000283
31005631
41005660
51005662
61006072
71006385
81006454
91006759
101006761
111006762
121006763
131006764
141006765
151006772
161006815
171006993
181007015
191007067
201007106
211007107
221007108
231007160
241007385
251007396
261007403
271007420
281007431
291007444
301007447
311007490
321007515
331007529
341007531
351007536
361007538
371007552
381007617
391007844
401007845
411007849
421007851
431007852
441007853
451007856
461007902
471007918
481007945
491008008
501009127
511009191
521009714
531009715
5410000002
5510000004
5610000005
5710000006
5810000013
5910000015
6010000020
6110000022
6210000025
6310000029
6410000032
6510000034
6610000035
6710000036
6810000037
6910000038
7010000039
7110000040
7210000041
7310000043
7410000045
7510000047
7610000049
7710000050
7810000053
7910000064
8010000117
8110000118
8210000119
8310000120
8410000155
8510000156
8610000157
8710000158
8810000160
8910000161
9010000164
9110000198
9210000200
9310000202
9410000209
9510000217
9610000233
9710000234
9810000238
9910000244
10010000250
10110000253
10210000255
10310000256
10410000257
10510000258
10610000259
10710000260
10810000265
10910000268
11010000270
11110000271
11210000281
11310000293
11410000302
11510000348
11610000349
11710000350
11810000354
11910000355
12010000356
12110000360
122proquest
scope
01000084
11000273
21000283
31005631
41005660
51005662
61006072
71006385
81006454
91006759
101006761
111006762
121006763
131006764
141006765
151006772
161006815
171006993
181007015
191007067
201007106
211007107
221007108
231007160
241007385
251007396
261007403
271007420
281007431
291007444
301007447
311007490
321007515
331007529
341007531
351007536
361007538
371007552
381007617
391007844
401007845
411007849
421007851
431007852
441007853
451007856
461007902
471007918
481007945
491008008
501009127
511009191
521009714
531009715
5410000002
5510000004
5610000005
5710000006
5810000013
5910000015
6010000020
6110000022
6210000025
6310000029
6410000032
6510000034
6610000035
6710000036
6810000037
6910000038
7010000039
7110000040
7210000041
7310000043
7410000045
7510000047
7610000049
7710000050
7810000053
7910000064
8010000117
8110000118
8210000119
8310000120
8410000155
8510000156
8610000157
8710000158
8810000160
8910000161
9010000164
9110000198
9210000200
9310000202
9410000209
9510000217
9610000233
9710000234
9810000238
9910000244
100...
lsr43
01000084false
11000273true
21000283true
31005631true
41005660true
51005662true
61006072true
71006385true
81006454true
91006759true
101006761true
111006762true
121006763true
131006764true
141006765true
151006772true
161006815true
171006993true
181007015true
191007067true
201007106true
211007107true
221007108true
231007160true
241007385false
251007396false
261007403false
271007420false
281007431false
291007444false
301007447false
311007490false
321007515false
331007529false
341007531false
351007536false
361007538false
371007552false
381007617true
391007844true
401007845true
411007849true
421007851true
431007852true
441007853true
451007856true
461007902true
471007918false
481007945true
491008008true
501009127true
511009191true
521009714true
531009715true
5410000002false
5510000004false
5610000005false
5710000006false
5810000013false
5910000015false
6010000020true
6110000022false
6210000025true
6310000029false
6410000032false
6510000034true
6610000035true
6710000036true
6810000037true
6910000038true
7010000039true
7110000040true
7210000041true
7310000043true
7410000045true
7510000047true
7610000049true
7710000050true
7810000053true
7910000064true
8010000117true
8110000118true
8210000119true
8310000120true
8410000155true
8510000156true
8610000157true
8710000158true
8810000160true
8910000161true
9010000164true
9110000198false
9210000200false
9310000202false
9410000209false
9510000217false
9610000233true
9710000234true
9810000238true
9910000244true
100...
startdate20031218
enddate20031218
citationpf 884 pt 90 vol 426 issue 6968
lsr30VSR-Enriched:[doi, pqid, galeid, pages]
sort
titleProtein folding and misfolding
authorDobson, Christopher
creationdate20031218
lso0120031218
facets
frbrgroupid5875136318187134471
frbrtype5
newrecords20180124
languageeng
creationdate2003
topic
0Evolution, Molecular–Chemistry
1Humans–Metabolism
2Plaque, Amyloid–Chemistry
3Plaque, Amyloid–Metabolism
4Protein Conformation–Metabolism
5Protein Denaturation–Metabolism
6Protein Folding–Metabolism
7Proteins–Metabolism
8Proteins
9Amino Acids
10Biochemistry
collection
0Medical Database
1ProQuest Science Journals
2STEM Database (ProQuest)
3Health & Medical Collection (Alumni edition)
4Medical Database (Alumni edition)
5Nursing & Allied Health Database (Alumni edition)
6Psychology Database (Alumni edition)
7Science Database (Alumni edition)
8ProQuest Pharma Collection
9Health & Medical Collection
10Psychology Database
11Nursing & Allied Health Database
12ProQuest Biology Journals
13ProQuest Agriculture Journals
14Ecology Abstracts
15Entomology Abstracts
16Animal Behavior Abstracts
17Neurosciences Abstracts
18ProQuest Public Health
19Aquatic Science Journals
20Materials Science Database
21Advanced Technologies & Aerospace Database
22Engineering Database
23Biological Science Database
24Environmental Science Database (ProQuest)
25Earth, Atmospheric & Aquatic Science Database (ProQuest)
26Engineering Research Database
27Technology Research Database
28ProQuest Nursing & Allied Health Source
29ProQuest Research Library
30Environment Abstracts
31ProQuest Agricultural Science Collection
32ProQuest Aquatic Science Collection
33ProQuest Atmospheric Science Collection
34ProQuest Biological Science Collection
35ProQuest Central
36ProQuest Earth Science Collection
37ProQuest Engineering Collection
38ProQuest Environmental Science Collection
39ProQuest Advanced Technologies & Aerospace Collection
40ProQuest Hospital Collection
41ProQuest Materials Science Collection
42ProQuest Natural Science Collection
43ProQuest Technology Collection
44Research Library (Alumni edition)
45Hospital Premium Collection (Alumni edition)
46ProQuest SciTech Collection
47ProQuest Health & Medical Complete
48ProQuest Medical Library
49ProQuest Psychology Journals
50Agricultural & Environmental Science Database
51Earth, Atmospheric & Aquatic Science Database
52Materials Science & Engineering Database
53Natural Science Collection
54ProQuest Central (new)
55ProQuest Central K-12
56ProQuest Central Korea
57Research Library Prep
58SciTech Premium Collection
59Technology Collection
60Health Research Premium Collection
61Health Research Premium Collection (Alumni edition)
62ProQuest Central Essentials
63eLibrary
64ProQuest One Academic
65Environmental Science Index (ProQuest)
66Biological Science Index (ProQuest)
67Environmental Science Collection (ProQuest)
68Materials Science Collection (ProQuest)
69Engineering Collection (ProQuest)
prefilterarticles
rsrctypearticles
creatorcontribDobson, Christopher
jtitleNature
toplevelpeer_reviewed
delivery
delcategoryRemote Search Resource
fulltextfulltext
addata
aulastDobson
aufirstChristopher
auDobson, Christopher
atitleProtein folding and misfolding
jtitleNature
risdate20031218
volume426
issue6968
spage884
epage90
pages884-890
issn00280836
eissn14764687
formatjournal
genrearticle
ristypeJOUR
abstractThe manner in which a newly synthesized chain of amino acids transforms itself into a perfectly folded protein depends both on the intrinsic properties of the amino-acid sequence and on multiple contributing influences from the crowded cellular milieu. Folding and unfolding are crucial ways of regulating biological activity and targeting proteins to different cellular locations. Aggregation of misfolded proteins that escape the cellular quality-control mechanisms is a common feature of a wide range of highly debilitating and increasingly prevalent diseases. [PUBLICATION ABSTRACT]
copLondon
pubNature Publishing Group
urlhttp://search.proquest.com/docview/204513759/
doi10.1038/nature02261
date2003-12-18