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Construction of Amyloid PDB Files Database

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2017
bazaamiloida.pdf (2.030Mb)
Authors
Stanković, Ivana
Hall, Michael B.
Zarić, Snežana D.
Article (Published version)
Metadata
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Abstract
Amyloids are insoluble proteins of a cross-β structure found as deposits in many diseases. They are largely examined structurally, but there is a lack of a unique structural database for amyloid proteins resolved with atomic resolution. We present a constructed amyloid database made on keyword criterion as well as structural features of amyloids described in literature. The searching filter performed by python programming, gave the total number of 109 structures. This database can help further structural general and statistical analysis of amyloids, that can lead to understanding of disease mechanisms related to amyloid proteins.
Keywords:
Amyloid / Database / PDB
Source:
IPSI Transactions on Internet Research, 2017, 13, 1, 49-8-
Publisher:
  • Belgrade : IPSI
Funding / projects:
  • Noncovalent interactions of pi-systems and their role in molecular recognition (RS-172065)
  • NPRP grant from the Qatar National Research Fund (a member of the Qatar Foundation) [grant number NPRP8-425-1-087]

ISSN: 1820-4503

[ Google Scholar ]
Handle
https://hdl.handle.net/21.15107/rcub_cer_6084
URI
https://cer.ihtm.bg.ac.rs/handle/123456789/6084
http://ipsitransactions.org/journals/papers/tir/2017jan/p6.pdf
Collections
  • Radovi istraživača / Researchers' publications
Institution/Community
IHTM
TY  - JOUR
AU  - Stanković, Ivana
AU  - Hall, Michael B.
AU  - Zarić, Snežana D.
PY  - 2017
UR  - https://cer.ihtm.bg.ac.rs/handle/123456789/6084
UR  - http://ipsitransactions.org/journals/papers/tir/2017jan/p6.pdf
AB  - Amyloids are insoluble proteins of a
cross-β structure found as deposits in many
diseases. They are largely examined structurally,
but there is a lack of a unique structural database
for amyloid proteins resolved with atomic
resolution. We present a constructed amyloid
database made on keyword criterion as well as
structural features of amyloids described in
literature. The searching filter performed by python
programming, gave the total number of 109
structures. This database can help further
structural general and statistical analysis of
amyloids, that can lead to understanding of
disease mechanisms related to amyloid proteins.
PB  - Belgrade : IPSI
T2  - IPSI Transactions on Internet Research
T1  - Construction of Amyloid PDB Files Database
VL  - 13
IS  - 1
SP  - 49-8
UR  - https://hdl.handle.net/21.15107/rcub_cer_6084
ER  - 
@article{
author = "Stanković, Ivana and Hall, Michael B. and Zarić, Snežana D.",
year = "2017",
abstract = "Amyloids are insoluble proteins of a
cross-β structure found as deposits in many
diseases. They are largely examined structurally,
but there is a lack of a unique structural database
for amyloid proteins resolved with atomic
resolution. We present a constructed amyloid
database made on keyword criterion as well as
structural features of amyloids described in
literature. The searching filter performed by python
programming, gave the total number of 109
structures. This database can help further
structural general and statistical analysis of
amyloids, that can lead to understanding of
disease mechanisms related to amyloid proteins.",
publisher = "Belgrade : IPSI",
journal = "IPSI Transactions on Internet Research",
title = "Construction of Amyloid PDB Files Database",
volume = "13",
number = "1",
pages = "49-8",
url = "https://hdl.handle.net/21.15107/rcub_cer_6084"
}
Stanković, I., Hall, M. B.,& Zarić, S. D.. (2017). Construction of Amyloid PDB Files Database. in IPSI Transactions on Internet Research
Belgrade : IPSI., 13(1), 49-8.
https://hdl.handle.net/21.15107/rcub_cer_6084
Stanković I, Hall MB, Zarić SD. Construction of Amyloid PDB Files Database. in IPSI Transactions on Internet Research. 2017;13(1):49-8.
https://hdl.handle.net/21.15107/rcub_cer_6084 .
Stanković, Ivana, Hall, Michael B., Zarić, Snežana D., "Construction of Amyloid PDB Files Database" in IPSI Transactions on Internet Research, 13, no. 1 (2017):49-8,
https://hdl.handle.net/21.15107/rcub_cer_6084 .

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