語系:
繁體中文
English
說明(常見問題)
登入
回首頁
切換:
標籤
|
MARC模式
|
ISBD
Lipids in Protein Misfolding
~
Gursky, Olga.
Lipids in Protein Misfolding
紀錄類型:
書目-語言資料,印刷品 : Monograph/item
正題名/作者:
Lipids in Protein Misfolding/ edited by Olga Gursky.
其他作者:
Gursky, Olga.
面頁冊數:
XIII, 260 p. 83 illus., 57 illus. in color.online resource. :
Contained By:
Springer Nature eBook
標題:
Proteins . -
電子資源:
https://doi.org/10.1007/978-3-319-17344-3
ISBN:
9783319173443
Lipids in Protein Misfolding
Lipids in Protein Misfolding
[electronic resource] /edited by Olga Gursky. - 1st ed. 2015. - XIII, 260 p. 83 illus., 57 illus. in color.online resource. - Advances in Experimental Medicine and Biology,8550065-2598 ;. - Advances in Experimental Medicine and Biology,889.
Role of Lipids in Folding, Misfolding and Function of Integral Membrane Proteins -- Protein Misfolding in Lipid-Mimetic Environments.- Lipids in Amyloid-β Processing, Aggregation, and Toxicity -- Role of Cholesterol and Phospholipids in Amylin Misfolding, Aggregation and Etiology of Islet Amyloidosis -- Stability, Oligomerization, and Amyloidogenicity of Apo Serum Amyloid A -- Interactions of Lipid Membranes with Fibrillar Protein Aggregates -- The Role of Lipid in Misfolding and Amyloid Fibril Formation by Apolipoprotein C-II -- Amyloid-Forming Properties of Human Apolipoproteins: Sequence Analyses and Structural Insights -- Computational Approaches to Identification of Aggregation Sites and the Mechanism of Amyloid Growth -- Role of Syndecans in Lipid Metabolism and Human Diseases.
This book addresses molecular mechanisms of protein misfolding and the role of lipids and related molecules in these complex processes. The focus is on the biophysical and structural studies of proteins that are involved in major human disorders such as Alzheimer’s disease, systemic amyloidoses, diabetes II, inflammation and atherosclerosis. Misfolding often results from protein mutations or modifications. Misfolding of membrane proteins can cause topological changes that target the proteins for degradation. Misfolding of soluble globular proteins and peptides converts them into β-sheet-rich aggregates and amyloid fibrils. This process can disrupt the structural integrity of the lipid membranes and thereby contribute to amyloid toxicity. In turn, lipids and lipid-associated molecules such as apolipoproteins and heparan sulfate proteoglycans, which are ubiquitous constituents of amyloid plaques, can influence protein misfolding via diverse mechanisms that are addressed in this book. The book features chapters describing the role of lipids in the misfolding of a wide range of proteins, including small peptides, globular proteins, lipid surface-binding proteins, and integral membrane proteins. The role of individual lipid molecules, lipid surfaces, and the membrane field is addressed, including specific and non-specific interactions with protein oligomers and mature fibrils. Distinct effects of various lipids on the nucleation and growth of amyloid fibrils are discussed. Modern computational approaches to the analysis of amyloid formation are addressed. The book should be useful to experts in the field but is also accessible to novices.
ISBN: 9783319173443
Standard No.: 10.1007/978-3-319-17344-3doiSubjects--Topical Terms:
1253493
Proteins .
LC Class. No.: QD431-431.7
Dewey Class. No.: 572.633
Lipids in Protein Misfolding
LDR
:03893nam a22004095i 4500
001
963766
003
DE-He213
005
20200702152104.0
007
cr nn 008mamaa
008
201211s2015 gw | s |||| 0|eng d
020
$a
9783319173443
$9
978-3-319-17344-3
024
7
$a
10.1007/978-3-319-17344-3
$2
doi
035
$a
978-3-319-17344-3
050
4
$a
QD431-431.7
072
7
$a
PSBC
$2
bicssc
072
7
$a
SCI007000
$2
bisacsh
072
7
$a
PSB
$2
thema
082
0 4
$a
572.633
$2
23
245
1 0
$a
Lipids in Protein Misfolding
$h
[electronic resource] /
$c
edited by Olga Gursky.
250
$a
1st ed. 2015.
264
1
$a
Cham :
$b
Springer International Publishing :
$b
Imprint: Springer,
$c
2015.
300
$a
XIII, 260 p. 83 illus., 57 illus. in color.
$b
online resource.
336
$a
text
$b
txt
$2
rdacontent
337
$a
computer
$b
c
$2
rdamedia
338
$a
online resource
$b
cr
$2
rdacarrier
347
$a
text file
$b
PDF
$2
rda
490
1
$a
Advances in Experimental Medicine and Biology,
$x
0065-2598 ;
$v
855
505
0
$a
Role of Lipids in Folding, Misfolding and Function of Integral Membrane Proteins -- Protein Misfolding in Lipid-Mimetic Environments.- Lipids in Amyloid-β Processing, Aggregation, and Toxicity -- Role of Cholesterol and Phospholipids in Amylin Misfolding, Aggregation and Etiology of Islet Amyloidosis -- Stability, Oligomerization, and Amyloidogenicity of Apo Serum Amyloid A -- Interactions of Lipid Membranes with Fibrillar Protein Aggregates -- The Role of Lipid in Misfolding and Amyloid Fibril Formation by Apolipoprotein C-II -- Amyloid-Forming Properties of Human Apolipoproteins: Sequence Analyses and Structural Insights -- Computational Approaches to Identification of Aggregation Sites and the Mechanism of Amyloid Growth -- Role of Syndecans in Lipid Metabolism and Human Diseases.
520
$a
This book addresses molecular mechanisms of protein misfolding and the role of lipids and related molecules in these complex processes. The focus is on the biophysical and structural studies of proteins that are involved in major human disorders such as Alzheimer’s disease, systemic amyloidoses, diabetes II, inflammation and atherosclerosis. Misfolding often results from protein mutations or modifications. Misfolding of membrane proteins can cause topological changes that target the proteins for degradation. Misfolding of soluble globular proteins and peptides converts them into β-sheet-rich aggregates and amyloid fibrils. This process can disrupt the structural integrity of the lipid membranes and thereby contribute to amyloid toxicity. In turn, lipids and lipid-associated molecules such as apolipoproteins and heparan sulfate proteoglycans, which are ubiquitous constituents of amyloid plaques, can influence protein misfolding via diverse mechanisms that are addressed in this book. The book features chapters describing the role of lipids in the misfolding of a wide range of proteins, including small peptides, globular proteins, lipid surface-binding proteins, and integral membrane proteins. The role of individual lipid molecules, lipid surfaces, and the membrane field is addressed, including specific and non-specific interactions with protein oligomers and mature fibrils. Distinct effects of various lipids on the nucleation and growth of amyloid fibrils are discussed. Modern computational approaches to the analysis of amyloid formation are addressed. The book should be useful to experts in the field but is also accessible to novices.
650
0
$a
Proteins .
$3
1253493
650
0
$a
Medicine.
$3
644133
650
0
$a
Bioorganic chemistry.
$3
743635
650
1 4
$a
Protein Structure.
$3
782128
650
2 4
$a
Biomedicine, general.
$3
1253757
650
2 4
$a
Bioorganic Chemistry.
$3
677511
700
1
$a
Gursky, Olga.
$4
edt
$4
http://id.loc.gov/vocabulary/relators/edt
$3
1066893
710
2
$a
SpringerLink (Online service)
$3
593884
773
0
$t
Springer Nature eBook
776
0 8
$i
Printed edition:
$z
9783319173450
776
0 8
$i
Printed edition:
$z
9783319173436
776
0 8
$i
Printed edition:
$z
9783319372051
830
0
$a
Advances in Experimental Medicine and Biology,
$x
0065-2598 ;
$v
889
$3
1253792
856
4 0
$u
https://doi.org/10.1007/978-3-319-17344-3
912
$a
ZDB-2-SBL
912
$a
ZDB-2-SXB
950
$a
Biomedical and Life Sciences (SpringerNature-11642)
950
$a
Biomedical and Life Sciences (R0) (SpringerNature-43708)
筆 0 讀者評論
多媒體
評論
新增評論
分享你的心得
Export
取書館別
處理中
...
變更密碼[密碼必須為2種組合(英文和數字)及長度為10碼以上]
登入