Zobrazeno 1 - 8
of 8
pro vyhledávání: '"Daniel J. Rigotti"'
Autor:
Yang Chao, Eric N Shiozaki, Srinivasa M Srinivasula, Daniel J Rigotti, Robert Fairman, Yigong Shi
Publikováno v:
PLoS Biology, Vol 3, Iss 6, p e183 (2005)
Caspases are responsible for the execution of programmed cell death (apoptosis) and must undergo proteolytic activation, in response to apoptotic stimuli, to function. The mechanism of initiator caspase activation has been generalized by the induced
Externí odkaz:
https://doaj.org/article/b7444b12980f46d3a4315f937f8695de
Autor:
Robert Fairman, Sarah H. Lawrence, Daniel J. Rigotti, Eileen K. Jaffe, Andrew Wasson, Bashkim Kokona
Publikováno v:
Biochemistry. 47:10649-10656
The enzyme porphobilinogen synthase (PBGS) can exist in different nonadditive homooligomeric assemblies, and under appropriate conditions, the distribution of these assemblies can respond to ligands such as metals or substrate. PBGS from most organis
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::e25576b00c98290aefefc2e16700bc42
https://doi.org/10.1021/bi801128d
https://doi.org/10.1021/bi801128d
Publikováno v:
Journal of Biological Chemistry. 278:14121-14133
The endoplasmic reticulum/Golgi SNARE rbet1 cycles between the endoplasmic reticulum and Golgi and is essential for cargo transport in the secretory pathway. Although the quaternary SNARE complex containing rbet1 is known to function in membrane fusi
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::b719aa402211bfb9820e50c064cc023d
https://doi.org/10.1074/jbc.m300659200
https://doi.org/10.1074/jbc.m300659200
Publikováno v:
Biochemistry. 41:13360-13369
A set of peptides derived from the N-terminal domain of the ribosomal protein L9 (NTL9) have been characterized in an effort to define the minimum unit of this domain required to fold and to provide model peptides for the analysis of electrostatic in
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::9505e039099a61156e5b95b803aa3695
https://doi.org/10.1021/bi026410c
https://doi.org/10.1021/bi026410c
Autor:
Carl D. Lederman, Robert S. Manning, Theresa Horne, Walter F. Smith, Suzanne Amador Kane, Robert Fairman, Daniel J. Rigotti, Karl A. Johnson, Bashkim Kokona, Eric K. Acton
Publikováno v:
Analytical biochemistry. 346(2)
We describe a quantitative analysis of Acanthamoeba castellanii myosin II rod domain images collected from atomic force microscope experiments. These images reveal that the rod domain forms a novel filament structure, most likely requiring unusual he
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::24ac80ef1ab30b208563cf81abfaae94
https://pubmed.ncbi.nlm.nih.gov/16213459
https://pubmed.ncbi.nlm.nih.gov/16213459
Autor:
Daniel J. Rigotti, Robert Fairman, Eric N. Shiozaki, Srinivasa M. Srinivasula, Yigong Shi, Yang Chao
Publikováno v:
PLoS Biology
PLoS Biology, Vol 3, Iss 6, p e183 (2005)
PLoS Biology, Vol 3, Iss 6, p e183 (2005)
Caspases are responsible for the execution of programmed cell death (apoptosis) and must undergo proteolytic activation, in response to apoptotic stimuli, to function. The mechanism of initiator caspase activation has been generalized by the induced
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::362f7c79030495e471bc3a9225d718b5
https://pubmed.ncbi.nlm.nih.gov/15941357
https://pubmed.ncbi.nlm.nih.gov/15941357
Publikováno v:
Biochemistry. 43(31)
The alpha-lactalbumins and c-type lysozymes have virtually identical structure but exhibit very different folding behavior. All alpha-lactalbumins form a well populated molten globule state, while most of the lysozymes do not. alpha-Lactalbumin consi
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::7bcb241530b538592696aa266719e744
https://pubmed.ncbi.nlm.nih.gov/15287723
https://pubmed.ncbi.nlm.nih.gov/15287723
Publikováno v:
Biochemistry. 43(11)
The villin headpiece subdomain is a cooperatively folded 36-residue, three-alpha-helix protein. The domain is one of the smallest naturally occurring sequences which has been shown to fold. Recent experimental studies have shown that it folds on the
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::d7a02a4109cfb2756e52cb7cf3ebcd0a
https://pubmed.ncbi.nlm.nih.gov/15023077
https://pubmed.ncbi.nlm.nih.gov/15023077