Zobrazeno 1 - 10
of 14
pro vyhledávání: '"James R. Arndt"'
Autor:
Ahmad Kiani Karanji, James R. Arndt, Mahdiar Khakinejad, Maxmore Chaibva, Maryssa Beasley, Samaneh Ghassabi Kondalaji, Stephen J. Valentine, Justin Legleiter, Olivia Sarver
Publikováno v:
Biochemistry
Huntington’s disease (HD) is a genetic neurodegenerative disorder characterized by the formation of amyloid fibrils of the huntingtin protein (htt). The seventeen-residue N-terminal region of htt (Nt(17)) has been implicated in formation of early-p
Autor:
Sudi Jawahery, Stephen J. Valentine, Albert W. Pilkington, Silvina Matysiak, James R. Arndt, Maxmore Chaibva, Justin Legleiter, Olivia Sarver
Publikováno v:
Biophysical Journal. 111:349-362
Huntington's disease (HD) is a genetic neurodegenerative disorder caused by an expanded polyglutamine (polyQ) domain near the N-terminus of the huntingtin (htt) protein. Expanded polyQ leads to htt aggregation. The first 17 amino acids (Nt(17)) in ht
Autor:
Megan M. Maurer, Samaneh Ghassabi Kondalaji, Arlo Parker, Stephen J. Valentine, Justin Legleiter, James R. Arndt
Publikováno v:
Biochemistry. 54:4285-4296
Early-stage oligomer formation of the huntingtin protein may be driven by self-association of the seventeen-residue amphipathic α-helix at the protein’s N-terminus (Nt17). Oligomeric structures have been implicated in neuronal toxicity and may rep
Publikováno v:
Analytical Chemistry. 87:5247-5254
Online deuterium hydrogen exchange (DHX) and pepsin digestion (PD) is demonstrated using drift tube ion mobility spectrometry (DTIMS) coupled with linear ion trap (LTQ) mass spectrometry (MS) with electron transfer dissociation (ETD) capabilities. DH
Publikováno v:
Journal of Mass Spectrometry. 50:117-126
Huntington's disease is a genetic neurodegenerative disorder caused by an expansion in a polyglutamine domain near the N-terminus of the huntingtin (htt) protein that results in the formation of protein aggregates. Here, htt aggregate structure has b
Autor:
James R. Arndt, Hossein Maleki, Mahdiar Khakinejad, Samaneh Ghassabi Kondalaji, Gregory C. Donohoe, Stephen J. Valentine
Publikováno v:
Journal of the American Society for Mass Spectrometry. 25:2103-2115
The gas-phase conformations of electrosprayed ions of the model peptide KKDDDDIIKIIK have been examined by ion mobility spectrometry (IMS) and hydrogen deuterium exchange (HDX)-tandem mass spectrometry (MS/MS) techniques. [M+4H](4+) ions exhibit two
Autor:
Hossein Maleki, Carroll R. McBride, James R. Arndt, Mahdiar Khakinejad, Gregory C. Donohoe, Stephen J. Valentine, Jinghai Yi, Timothy R. Nurkiewicz
Publikováno v:
Analytical Chemistry. 86:8121-8128
A new instrument that couples a low-pressure drift tube with a linear ion trap mass spectrometer is demonstrated for complex mixture analysis. The combination of the low-pressure separation with the ion trapping capabilities provides several benefits
Publikováno v:
Nano Research. 5:213-221
Approximately 15 nm thick nitrogen-doped lanthanum titanate (La2Ti2O7) nanosheets with a single-crystalline perovskite structure have been prepared by hydrothermal processing and subsequent heat treatment in NH3 at 600 °C. Doping nitrogen into the L
Publikováno v:
Biomolecular Concepts, Vol 6, Iss 1, Pp 33-46 (2015)
Huntington’s disease (HD) is caused by a polyglutamine (polyQ) domain that is expanded beyond a critical threshold near the N-terminus of the huntingtin (htt) protein, directly leading to htt aggregation. While full-length htt is a large (on the or
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::05b1c56ff5335aa630304b7b833624cb
https://europepmc.org/articles/PMC4590289/
https://europepmc.org/articles/PMC4590289/
Autor:
Pranav Jain, Maxmore Chaibva, Xiang Gao, Olivia Sarver, Justin Legleiter, Stephen J. Valentine, James R. Arndt
Publikováno v:
Biophysical Journal. 110(3):358a-359a
Huntington disease (HD) is a genetic neurodegenerative disease caused by an expanded polyglutamine (polyQ) domain in the first exon of the huntingtin (Htt) protein. This polyQ expansions leads directly to the formation of proteinaceous aggregates inc