Zobrazeno 1 - 10
of 10
pro vyhledávání: '"John M. Boettcher"'
Autor:
Kristin M Nuzzio, Eric D Watt, John M Boettcher, Joshua M Gajsiewicz, James H Morrissey, Chad M Rienstra
Publikováno v:
PLoS ONE, Vol 11, Iss 9, p e0163206 (2016)
In normal hemostasis, the blood clotting cascade is initiated when factor VIIa (fVIIa, other clotting factors are named similarly) binds to the integral membrane protein, human tissue factor (TF). The TF/fVIIa complex in turn activates fX and fIX, ev
Externí odkaz:
https://doaj.org/article/7698e29808764ebba12b298f030df4b4
Autor:
Lindsay J. Sperling, John M. Boettcher, Yi Gui Gao, Scott R. Wilson, Heather L. Frericks Schmidt, Chad M. Rienstra, Benjamin J. Wylie
Publikováno v:
The Journal of Physical Chemistry B. 111:14362-14369
The study of micro- or nanocrystalline proteins by magic-angle spinning (MAS) solid-state NMR (SSNMR) gives atomic-resolution insight into structure in cases when single crystals cannot be obtained for diffraction studies. Subtle differences in the l
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::e92e348bb628e1933a4d7d8d305c2dfd
https://doi.org/10.1021/jp075531p
https://doi.org/10.1021/jp075531p
Autor:
James H. Morrissey, John M. Boettcher, Joshua M. Gajsiewicz, Chad M. Rienstra, Eric D. Watt, Kristin M. Nuzzio
Publikováno v:
PLoS ONE
PLoS ONE, Vol 11, Iss 9, p e0163206 (2016)
PLoS ONE, Vol 11, Iss 9, p e0163206 (2016)
In normal hemostasis, the blood clotting cascade is initiated when factor VIIa (fVIIa, other clotting factors are named similarly) binds to the integral membrane protein, human tissue factor (TF). The TF/fVIIa complex in turn activates fX and fIX, ev
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::c53903b145e23ba56719403c10429464
https://pubmed.ncbi.nlm.nih.gov/27657719
https://pubmed.ncbi.nlm.nih.gov/27657719
Publikováno v:
Nature chemical biology
Sublancin is shown to be an S-linked glycopeptide containing a glucose attached to a cysteine residue, establishing a new post-translational modification. The activity of the S-glycosyl transferase was reconstituted in vitro, and the enzyme is shown
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::565f3446dfedc67a869d0bed2e514873
https://doi.org/10.1038/nchembio.509
https://doi.org/10.1038/nchembio.509
Publikováno v:
Biomolecular NMR Assignments. 4:183-185
Backbone (1)H, (13)C and (15)N resonance assignments are presented for the extracellular domain of tissue factor. Tissue factor is the integral membrane protein that initiates blood coagulation through the formation an enzymatic complex with the plas
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::0863229982842942bdc53620f214fff3
https://doi.org/10.1007/s12104-010-9233-x
https://doi.org/10.1007/s12104-010-9233-x
Autor:
John M. Boettcher, Daniel T. Ladror, Jimin George, Chad M. Rienstra, Kevin L. Hartman, Wendy S. Woods, Zhi Qi
Publikováno v:
Biomolecular NMR Assignments. 1:167-169
(13)C, (15)N, and (1)H chemical shift assignments are presented for the cAMP-regulated phosphoprotein endosulfine-alpha in its free and micelle-bound states. Secondary chemical shift analysis demonstrates formation of four helices in the micelle-boun
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::95f35fc72ae41615517496ee77bae011
https://doi.org/10.1007/s12104-007-9063-7
https://doi.org/10.1007/s12104-007-9063-7
Autor:
Wendy S. Woods, Jimin George, Kevin L. Hartman, Daniel T. Ladror, Chad M. Rienstra, Zhi Qi, John M. Boettcher
Publikováno v:
Biochemistry. 47(47)
Endosulfine-alpha (ENSA) is a 121-residue cAMP-regulated phosphoprotein, originally identified as an endogenous regulator of ATP-sensitive potassium channels. ENSA has been implicated in the regulation of insulin secretion, and expression of ENSA is
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::dcc5c907c80ba79a99b6185670a6b7e0
https://pubmed.ncbi.nlm.nih.gov/18973346
https://pubmed.ncbi.nlm.nih.gov/18973346
Autor:
Zhi Qi, Donghua H. Zhou, Wendy S. Woods, John M. Boettcher, Kathryn D. Kloepper, Jimin George, Daniel T. Ladror, Chad M. Rienstra, Kevin L. Hartman
Publikováno v:
The Journal of biological chemistry. 282(47)
Alpha-synuclein (AS) is an intrinsically unstructured protein in aqueous solution but is capable of forming beta-sheet-rich fibrils that accumulate as intracytoplasmic inclusions in Parkinson disease and certain other neurological disorders. However,
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::71fffd0eae5ade29deb8718dae9e15a6
https://pubmed.ncbi.nlm.nih.gov/17893145
https://pubmed.ncbi.nlm.nih.gov/17893145
Autor:
John M. Boettcher, Rebecca L. Davis-Harrison, Narjes Tavoosi, Mary C. Clay, Chad M. Rienstra, James H. Morrissey
Publikováno v:
Blood. 116:1141-1141
Abstract 1141 Most steps in the blood coagulation cascade obligatorily take place on membrane surfaces and are dependent on the exposure of phosphatidylserine (PS). Many coagulation proteins bind to PS-containing membrane bilayers in a calcium-depend
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::a05afba57e38ac07a90e0a54420c1923
https://doi.org/10.1182/blood.v116.21.1141.1141
https://doi.org/10.1182/blood.v116.21.1141.1141
Autor:
Heather L. Frericks Schmidt, Lindsay J. Sperling, Yi Gui Gao, Benjamin J. Wylie, John M. Boettcher, Scott R. Wilson, Chad M. Rienstra
Publikováno v:
Journal of Physical Chemistry B; Dec2007, Vol. 111 Issue 51, p14362-14369, 8p