Searched for: person:henrim04
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Carcinoid Heart Disease [Case Report]
Dangol, Raj K; Henricus, Marsiyana M
PMID: 35593702
ISSN: 1533-4406
CID: 5352762
Structural Analysis of Heptameric Alpha-Hemolysin under Extreme Conditions that Facilitate Nucleic Acid Translocation [Meeting Abstract]
Henricus, Marsiyana M.; Japrung, Deanpen; Li, Qiuhong; Maglia, Giovanni; Bayley, Hagan
ISI:000208762006244
ISSN: 0006-3495
CID: 5352802
DNA strands from denatured duplexes are translocated through engineered protein nanopores at alkaline pH
Maglia, Giovanni; Henricus, Marsiyana; Wyss, Romain; Li, Qiuhong; Cheley, Stephen; Bayley, Hagan
Nanopores are under development for the detection of a variety of analytes and the investigation of chemical reactions at the single molecule level. In particular, the analysis of nucleic acid molecules is under intense investigation, including the development of systems for rapid, low-cost DNA sequencing. Here, we show that DNA can be translocated through an engineered alphaHL protein pore at pH 11.7, a value at which dsDNA is denatured. Therefore, the alphaHL pore is sufficiently stable to entertain the possibility of direct nanopore sequencing of genomic dsDNA samples, which are more readily obtained and handled than ssDNA.
PMID: 19645477
ISSN: 1530-6992
CID: 5352732
Endoscopic Management Of Walled Off Pancreatic Necrosis In A Community Hospital Setting
Naqvi, Haider A; Bente, Andreea; Henricus, Marsiyana; Cenac, Kelvin; Yousaf, Muhammad N; Haas, Christopher J; Sankineni, Abhinav
ORIGINAL:0016699
ISSN: 1097-6779
CID: 5456882
Prosthetic Heart Valves
Chapter by: Chan, Christine K; Henricus, Marsiyana M; Ibrahim, George S; Maniya, Omar Z
in: Learning cardiac auscultation : from essentials to expert clinical interpretation by Taylor, Allen J [Ed]
London : Springer, [2015]
pp. 249-261
ISBN: 9781447167372
CID: 5456852
Pulmonic Valve: Pulmonary Arterial Hypertension
Chapter by: Kass, Samantha L; Madison, K Elizabeth; Henricus, Marsiyana M; Chan, Christine K
in: Learning cardiac auscultation : from essentials to expert clinical interpretation by Taylor, Allen J [Ed]
London : Springer, [2015]
pp. 191-203
ISBN: 9781447167372
CID: 5456862
Interactions of amyloid Aβ(1-42) peptide with self-assembled peptide nanospheres
Smoak, Evan M; Dabakis, Melanie P; Henricus, Marsiyana M; Tamayev, Robert; Banerjee, Ipsita A
In this work we have probed the interactions of the amyloid Aβ(1-42) peptide with self-assembled nanospheres. The nanospheres were formed by self-assembly of a newly developed bolaamphiphile bis(N-alpha-amido-methionine)-1,8 octane dicarboxylate under aqueous conditions. It was found that the interactions of the Aβ(1-42) peptide with the nanospheres were concentration as well as pH dependent and the peptide largely adopts a random coil structure upon interacting with the nanospheres. Further, upon incorporation with the nanospheres, we observed a relative diminution in the aggregation of Aβ(1-42) at low concentrations of Aβ(1-42). The interactions between the nanospheres and the Aβ(1-42) peptide were investigated by atomic force microscopy, transmission electron microscopy, circular dichroism, FTIR and fluorescence spectroscopy, and the degree of fibrillation in the presence and absence of nanospheres was monitored by the Thioflavine T assay. We believe that the outcome from this work will help further elucidate the binding properties of Aβ peptide as well as designing nanostructures as templates for further investigating the nucleation and fibrillation process of Aβ-like peptides.
PMID: 20814889
ISSN: 1099-1387
CID: 5352752
Urea facilitates the translocation of single-stranded DNA and RNA through the alpha-hemolysin nanopore
Japrung, Deanpen; Henricus, Marsiyana; Li, Qiuhong; Maglia, Giovanni; Bayley, Hagan
The staphylococcal alpha-hemolysin (alphaHL) protein nanopore is under investigation as a fast, cheap detector for nucleic acid analysis and sequencing. Although discrimination of all four bases of DNA by the alphaHL pore has been demonstrated, analysis of single-stranded DNAs and RNAs containing secondary structure mediated by basepairing is prevented because these nucleic acids cannot be translocated through the pore. Here, we show that a structured 95-nucleotide single-stranded DNA and its RNA equivalent are translocated through the alphaHL pore in the presence of 4 M urea, a concentration that denatures the secondary structure of the polynucleotides. The alphaHL pore is functional even in 7 M urea, and therefore it is easily stable enough for analyses of challenging DNA and RNA species.
PMCID:2862201
PMID: 20441749
ISSN: 1542-0086
CID: 5352742
Urea Facilitates the Translocation of Single-Stranded DNA and RNA Through the alpha-Hemolysin Nanopore [Meeting Abstract]
Japrung, Deanpen; Henricus, Marsiyana; Li, Qiuhong; Maglia, Giovanni; Bayley, Hagan
ISI:000208762000233
ISSN: 0006-3495
CID: 5352792
In Situ Photopolymerization of PEGDA-Protein Hydrogels on Nanotube Surfaces
Smoak, Evan M.; Henricus, Marsiyana M.; Banerjee, Ipsita A.
ISI:000282840900009
ISSN: 0021-8995
CID: 5352862