Zobrazeno 1 - 10
of 58
pro vyhledávání: '"Charles L. Murphy"'
Autor:
Désirée S Jansson, Caroline Bröjer, Aleksija Neimanis, Torsten Mörner, Charles L Murphy, Faruk Otman, Per Westermark
Publikováno v:
PLoS ONE, Vol 13, Iss 3, p e0193265 (2018)
Since the late 1990s, high mortality and declining populations have been reported among sea birds including Herring gulls (Larus argentatus) from the Baltic Sea area in Northern Europe. Repeated BoNT type C/D botulism outbreaks have occurred, but it
Externí odkaz:
https://doaj.org/article/1fa46033368846a79ea7f29c8daae804
Autor:
Alan Solomon, Daniel P. Kestler, Charles L. Murphy, S Wang, Deborah T. Weiss, Fred A. Stevens
Publikováno v:
Amyloid. 16:84-88
AA amyloidosis invariably has been associated with fibrillar deposits of the acute phase high-density lipoprotein serum amyloid A isotypes SAA1 and SAA2. We now report the first case in a patient with no antecedent history of a chronic inflammatory o
Autor:
Marianne Schiffer, Alan Solomon, Manfred Eulitz, Priscilla Wilkins Stevens, Maria Berrios-Hammond, Fred J. Stevens, Florence A. Westholm, Ronald Wetzel, Rosemarie Raffen, Deborah K. Hanson, Charles L. Murphy, Y.-L. Deng
Publikováno v:
Protein Science. 4:421-432
The primary structural features that render human monoclonal light chains amyloidogenic are presently unknown. To gain further insight into the physical and biochemical factors that result in the pathologic deposition of these proteins as amyloid fib
Autor:
Rosalba Sánchez, Alan Solomon, Amy Allen, Ernesto Ortiz, Luis del Pozo Yauner, Charles L. Murphy, Rosana Sánchez-López, D. Alejandro Fernández-Velasco, Jonathan S. Wall, Leopoldo Güereca, Baltazar Becerril
Publikováno v:
Proteins: Structure, Function, and Bioinformatics. 72:684-692
Light chain-associated amyloidosis is a fatal disease characterized by the aggregation and pathologic deposition of monoclonal light chain-related fragments as amyloid fibrils in organs or tissues throughout the body. Notably, it has been observed th
Autor:
Stephen J. Kennel, Shuching Wang, James S. Foster, Alan Solomon, Deborah T. Weiss, Eric R. Carlson, John Hudson, Sallie Macy, Charles L. Murphy, Daniel P. Kestler
Publikováno v:
Amyloid. 15:89-95
We have previously reported that the amyloid found in three patients with calcifying epithelial odontogenic tumors (CEOT) was composed of N-terminal fragments of a putative 153-residue protein specified by a gene designated FLJ20513 now known to repr
Autor:
Christoph Röcken, Per Westermark, Hui Zhou, Reinhold P. Linke, Deborah T. Weiss, Shuching Wang, Ulrich Gross, Reinhild Joswig, Charles L. Murphy, Alan Solomon
Publikováno v:
Journal of Laboratory and Clinical Medicine. 145:187-193
Senile seminal vesicle amyloid (SSVA), one of the most common forms of localized amyloidosis, is associated with the male aging process. Although it had been posited that the amyloidogenic component originated from exocrine cells and that, on the bas
Autor:
Per Westermark, Charles L. Murphy, Alan Solomon, Åsa Gustavsson, Bert Ove Olofsson, Joakim Bergström, Ulf Hellman, Knut Sletten, Deborah T. Weiss
Publikováno v:
The Journal of Pathology. 206:224-232
The pathological fibrillar deposits found in the heart and other organs of patients with senile systemic amyloidosis (SSA) and Swedish familial amyloidotic polyneuropathy (FAP) contain wild-type (wt) and a mutant form of transthyretin (TTR), respecti
Autor:
Deborah T. Weiss, Ulf Hellman, Knut Sletten, Charles L. Murphy, Per Westermark, Alan Solomon, Joakim Bergström
Publikováno v:
Laboratory Investigation. 84:981-988
Certain forms of systemic amyloidosis have been associated with the pathologic deposition as fibrils of three different apolipoprotein-related proteins--apolipoprotein A-I, apolipoprotein A-II, and serum amyloid A. We have previously reported (Bergst
Autor:
Robert L. Donnell, Per Westermark, Knut Sletten, Manfred Eulitz, Rudi Hrncic, Charles L. Murphy, Deborah T. Weiss, Gunilla T. Westermark, Kristal Weaver, Alan Solomon
Publikováno v:
Journal of Laboratory and Clinical Medicine. 142:348-355
Calcifying epithelial odontogenic tumors (CEOTs), also known as Pindborg tumors, are characterized by the presence of squamous-cell proliferation, calcification, and, notably, amyloid deposits. On the basis of immunohistochemical analyses, the amyloi
Publikováno v:
Biochemistry. 40:11757-11767
Although the gross morphology of amyloid fibrils is fairly well understood, very little is known about how the constituent polypeptides fold within the amyloid folding motif. In the experiments reported here, we used trypsin and chymotrypsin to condu