ModBase, a database of annotated comparative protein structure models and associated resources

Autor: Andrej Sali, Ben Webb, Marc A. Marti-Renom, Rachel Karchin, David T. Barkan, Hannah Carter, Libusha Kelly, Fred P. Davis, Parminder Mankoo, David Eramian, Narayanan Eswar, Ursula Pieper

Publikováno v: Nucleic Acids Research
Nucleic Acids Research, 2013, 42 (D1), pp.D336-D346. ⟨10.1093/nar/gkt1144⟩
Nucleic Acids Research, Oxford University Press, 2013, 42 (D1), pp.D336-D346. ⟨10.1093/nar/gkt1144⟩

International audience; ModBase (http://salilab.org/modbase) is a database of annotated comparative protein structure models. The models are calculated by ModPipe, an auto- mated modeling pipeline that relies primarily on Modeller for fold assignment

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::40a2735948661a7cec74711881f165e9
https://hal-pasteur.archives-ouvertes.fr/pasteur-01414232

Subnanometer-resolution electron cryomicroscopy-based domain models for the cytoplasmic region of skeletal muscle RyR channel

Autor: Matthew L. Baker, Irina I. Serysheva, Susan L. Hamilton, David Eramian, Wah Chiu, Andrej Sali, Yao Cong, Maya Topf, Steven J. Ludtke

The skeletal muscle Ca 2+ release channel (RyR1), a homotetramer, regulates the release of Ca 2+ from the sarcoplasmic reticulum to initiate muscle contraction. In this work, we have delineated the RyR1 monomer boundaries in a subnanometer-resolution

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::46dd5f36ef376996e37c6d5028265271
https://europepmc.org/articles/PMC2474495/

Protein Structure Modeling with MODELLER

Autor: Narayanan Eswar, David Eramian, Ben Webb, Min-Yi Shen, Andrej Sali

Publikováno v: Methods in Molecular Biology ISBN: 9781588298096

Genome sequencing projects have resulted in a rapid increase in the number of known protein sequences. In contrast, only about one-hundredth of these sequences have been characterized using experimental structure determination methods. Computational

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_________::4e4ad7cf623c63cb571e8a07ee6b66be
https://doi.org/10.1007/978-1-60327-058-8_8

K317, R319, and E320 within the proximal C-terminus of the bradykinin B2 receptor form a motif important for phospholipase C and phospholipase A2 but not connective tissue growth factor related signaling

Autor: Peter Polgar, Dale F. Mierke, David Eramian, Bin Liu, Jun Yu, Linda Taylor

Publikováno v: Journal of cellular biochemistry. 92(3)

We showed previously that large domain exchanges between the bradykinin B2 (BKB2) and angiotensin II type 1a (AT1a) receptors can result in functional hybrids. However, when we proceeded to exchange the entire bradykinin B2 receptor (BKB2R) C-termina

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::69af97454503898f89e446db4884ae6a
https://pubmed.ncbi.nlm.nih.gov/15156566