Zobrazeno 1 - 10
of 138
pro vyhledávání: '"CK Anders"'
Autor:
NK Ibrahim, S-C Tang, AJ Brenner, S Kesari, DE Piccioni, CK Anders, JA Carillo, P Chalasani, P Kabos, S Puhalla, AA Garcia, KH Tkaczuk, MS Ahluwalia, NJ Lakhani, P Kumthekar
Publikováno v:
Cancer Research. 77:P1-12
Background: The incidence of CNS metastatic disease in breast cancer patients (pts) seems to have increased in recent years with the improvement of systemic therapy. However, treatment options for CNS metastases have remained limited due to the inabi
Autor:
KD Swiger, JE Guglielmino, JD Labban, HS Rugo, SM Domchek, CK Anders, HCM Nelson, AA Hanson, H Dinerman, CC Henry
Publikováno v:
Cancer Research. 76:P5-09
Purpose: To ensure that people with breast cancer receive materials and programs that fit their needs for education, information, and support by identifying clinical, treatment, demographic, socioeconomic, and emotional characteristics targeting thei
The 16-22 amino acid fragment of the beta-amyloid peptide associated with the Alzheimer's disease, Abeta, is capable of forming amyloid fibrils. Here we study the aggregation mechanism of Abeta(16-22) peptides by unbiased thermodynamic simulations at
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::07f020e61e8ed3f166ff82669c6c24c6
http://arxiv.org/abs/q-bio/0409005
http://arxiv.org/abs/q-bio/0409005
An atomic protein model with a minimalistic potential is developed and then tested on an alpha-helix and a beta-hairpin, using exactly the same parameters for both peptides. We find that melting curves for these sequences to a good approximation can
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::1d873f4ab263f6b94cee72110bea3b34
http://arxiv.org/abs/q-bio/0312045
http://arxiv.org/abs/q-bio/0312045
A reduced protein model with five to six atoms per amino acid and five amino acid types is developed and tested on a three-helix-bundle protein, a 46-amino acid fragment from staphylococcal protein A. The model does not rely on the widely used Go app
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::10289e35ba8bb9431c48b8162cb551d0
http://arxiv.org/abs/cond-mat/0111291
http://arxiv.org/abs/cond-mat/0111291
We study the thermodynamic behavior of a model protein with 54 amino acids that is designed to form a three-helix bundle in its native state. The model contains three types of amino acids and five to six atoms per amino acid, and has the Ramachandran
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::98f4ad59f9484e8a36cef0f17c0a09cb
http://arxiv.org/abs/cond-mat/0107177
http://arxiv.org/abs/cond-mat/0107177
The thermodynamic behavior of a three-dimensional off-lattice model for protein folding is probed. The model has only two types of residues, hydrophobic and hydrophilic. In absence of local interactions, native structure formation does not occur for
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::797176a55791cbcb0373fd39de387bf5
http://arxiv.org/abs/physics/9610010
http://arxiv.org/abs/physics/9610010
Autor:
Dahlbom, Mats, Irb��ck, Anders
This paper is withdrawn.
Withdrawn
Withdrawn
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::cec2eb2322e47197c5fc521a7ca5e475
http://arxiv.org/abs/adap-org/9604002
http://arxiv.org/abs/adap-org/9604002
Autor:
Irb��ck, Anders, Potthast, Frank
See chem-ph/9505003.
Comment: Withdrawn, combined with chem-ph/9505003
Comment: Withdrawn, combined with chem-ph/9505003
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::819878b713adc8db7fa12071fae675ce
http://arxiv.org/abs/chem-ph/9505004
http://arxiv.org/abs/chem-ph/9505004
Publikováno v:
Journal of Physical Chemistry B; Aug2013, Vol. 117 Issue 31, p9194-9202, 9p