Zobrazeno 1 - 10
of 10
pro vyhledávání: '"Kristi Lazar Cantrell"'
Autor:
Joan-Emma Shea, Grace E. Schonfeld, Sarah L. Claud, Shruti Arya, Pritam Ganguly, Andrea Arsiccio, Xikun Liu, Kristi Lazar Cantrell, Benjamin Trapp, Michael T. Bowers
Publikováno v:
The Journal of Physical Chemistry B. 124:8772-8783
Aberrant protein folding leading to the formation of characteristic cross-β-sheet-rich amyloid structures is well known for its association with a variety of debilitating human diseases. Often, depending upon amino acid composition, only a small seg
Autor:
Kristi Lazar Cantrell, Thanh D. Do, Grace E. Schonfeld, Aleksandra Antevska, Damilola S. Oluwatoba, Amber L. H. Gray
Publikováno v:
Analytical Chemistry. 92:11802-11808
Our knowledge of amyloid formation and cytotoxicity originating from self-assembly of α-helical peptides is incomplete. PSMα3 is the only system where high-resolution X-ray crystallography and toxi...
Autor:
Nicole M. Marsh, Dezmond Bishop, Michael T. Bowers, Kristi Lazar Cantrell, Veronica Laos, Christian A. Lang, Steven K. Buratto, Ambuj K. Singh
Publikováno v:
Biochemistry. 59:499-508
TDP-43 aggregates are a salient feature of amyotrophic lateral sclerosis (ALS), frontotemporal dementia (FTD), and a variety of other neurodegenerative diseases, including Alzheimer's disease (AD). With an anticipated growth in the most susceptible d
Autor:
Veronica Laos, Steven K. Buratto, Dezmond Bishop, Thanh D. Do, Kristi Lazar Cantrell, Megan Fetters, Michael T. Bowers, Yingying Jin, Nicole M. Marsh, Brady Quon
Publikováno v:
ACS Chemical Neuroscience. 10:4112-4123
Aggregation of TAR DNA-binding protein of 43 kDa (TDP-43) is a salient feature of amyotrophic lateral sclerosis (ALS), a debilitating neurodegenerative disorder affecting over 200 000 people worldwide. The protein undergoes both functional and pathog
Autor:
Veronica, Laos, Dezmond, Bishop, Christian A, Lang, Nicole M, Marsh, Kristi Lazar, Cantrell, Steven K, Buratto, Ambuj K, Singh, Michael T, Bowers
Publikováno v:
Biochemistry. 59(4)
TDP-43 aggregates are a salient feature of amyotrophic lateral sclerosis (ALS), frontotemporal dementia (FTD), and a variety of other neurodegenerative diseases, including Alzheimer's disease (AD). With an anticipated growth in the most susceptible d
Autor:
Steven K. Buratto, Chun Wu, Kristi Lazar Cantrell, Alexandre I. Ilitchev, Michael T. Bowers, Carina Olivas, Maxwell J. Giammona, Sarah L. Claud
Publikováno v:
Journal of the American Chemical Society. 140:9685-9695
Protein aggregation is typically attributed to the association of homologous amino acid sequences between monomers of the same protein. Coaggregation of heterogeneous peptide species can occur, however, and is implicated in the proliferation of seemi
Publikováno v:
ACS chemical neuroscience. 10(11)
The aberrant association of proteins/peptides is implicated in the etiology and pathogenesis of a variety of human diseases. In general, the primary protein component responsible for the formation of aggregates is different in each case and is specif
Autor:
Veronica, Laos, Thanh D, Do, Dezmond, Bishop, Yingying, Jin, Nicole M, Marsh, Brady, Quon, Megan, Fetters, Kristi Lazar, Cantrell, Steven K, Buratto, Michael T, Bowers
Publikováno v:
ACS chemical neuroscience. 10(9)
Aggregation of TAR DNA-binding protein of 43 kDa (TDP-43) is a salient feature of amyotrophic lateral sclerosis (ALS), a debilitating neurodegenerative disorder affecting over 200 000 people worldwide. The protein undergoes both functional and pathog
Autor:
Joan-Emma Shea, Michael T. Bowers, Pritam Ganguly, Kristi Lazar Cantrell, Sarah L. Claud, Shruti Arya, Andrea Arsiccio
Publikováno v:
Biophysical Journal. 116:492a
Autor:
Stuart C. Feinstein, Sarah J. Benbow, Nichole E. LaPointe, Nicolette Dressler, Srinivasan Ramachandran, Thanh D. Do, Noelle E. Huskey, Megan Korff, Ratnesh Lal, Michelle R. Gaylord, H. Eric Feinstein, Michael T. Bowers, Kristi Lazar Cantrell, Nirav Patel, Brady Quon
Publikováno v:
Journal of neurochemistry. 137(6)
Despite extensive structure-function analyses, the molecular mechanisms of normal and pathological tau action remain poorly understood. How does the C-terminal microtubule-binding region regulate microtubule dynamics and bundling? In what biophysical