• 대한세포병리학회지
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• 제13권1호
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• pp.38-41
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• 2002

Localized amyloidosis of the ureter is rare and clinically confused with neoplasm. We describe a case of localized amyloidosis of the ureter in which the presence of amyloid was detected in ureteral washing cytology. A 75-year-old female presented with gross hematuria. Abdominal CT and retrograde pyelography revealed hydronephrosis and hydroureter on the left side with abrupt narrowing of the distal ureter. Ureteral washing cytology yielded a hypocellular smear with many irregular clumps of amorphous, extracellar, waxy material. Biopsy sections demonstrated submucosal deposits of eosinophilic amorphous material which gave characteristic apple green birefringence with Congo-red stain under the polarized light. Familarity with the cytologic features of amyloid is helpful for preoperative diagnosis and proper treatment.

• Bulletin of the Korean Chemical Society
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• 제30권12호
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• pp.3006-3010
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• 2009

We have performed long time REMD simulation on 15-19 residues of human calcitonin hormone (DFNKF) which is known to form highly ordered amyloid fibril. The simulation started from randomly oriented multiple DFNKF strand. Using all-atom level simulations with the generalized Born solvation (GB) model (param99MOD3), we observed spontaneous formation of ${\beta}$-sheet for tetramer. Interestingly, the current simulation gives anti-parallel sheet as a major conformation, consistent with experiments. The major interaction stabilizing the anti-parallel sheet seems to be the inter-strand hydrogen bond.

• BMB Reports
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• 제38권3호
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• pp.275-280
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• 2005

For most of proteins to be active, they need well-defined three-dimensional structures alone or in complex. Folding is a process through which newly synthesized proteins get to the native state. Protein folding inside cells is assisted by various chaperones and folding factors, and misfolded proteins are eliminated by the ubiquitin-proteasome degradation system to ensure high fidelity of protein expression. Under certain circumstances, misfolded proteins escape the degradation process, yielding to deposit of protein aggregates such as loop-sheet polymer and amyloid fibril. Diseases characterized by insoluble deposits of proteins have been recognized for long time and are grouped as conformational diseases. Study of protein folding mechanism is required for better understanding of the molecular pathway of such conformational diseases.

• 한국자기공명학회논문지
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• 제8권1호
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• pp.19-27
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• 2004

C-terminal fragments of APP (APP-CTs), that contain complete Abeta sequence, are found in neuritic plaques, neurofibrillary tangles and the cytosol of lymphoblastoid cells obtained from AD patients. CT16, Lys649-Asp664 (KKQYTSIHHGVVEVD) has been known as the most toxic part in the C-terminal fragment of amyloid precursor protein (APP). The solution structure of CT16 was investigated using NMR spectroscopy in various membrane-mimicking environments. According to Circular Dichroim (CD) spectra, CT16 has a random structure in aqueous solution, while conformational change was induced by addition of TFE and SDS micelle. Tertiary structure as determined by NMR spectroscopy shows that CT16 has a ${\beta}$-turn conformation in trifluoroethanol-containing aqueous solution.

• 수면정신생리
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• 제29권1호
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• pp.1-3
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• 2022

Sleep is associated with Alzheimer's dementia. Many previous researches have shown that inadequate sleep is one of the risk factors that predict Alzheimer's dementia. The causal mechanism of this association is not clear. Slow wave sleep and REM sleep are critical stages in memory consolidation, and by sequential hypothesis both stages are important. Deposition of amyloid beta and tau, the main pathology of Alzheimer's dementia, are also associated with sleep. This review provides the association of sleep and Alzheimer's dementia, and future research is necessary to examine the specific mechanism of this association between sleep and Alzheimer's dementia, which may lead to an early intervention in sleep.

• 한국응용약물학회:학술대회논문집
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• 한국응용약물학회 2005년도 춘계학술대회
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• pp.35-40
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• 2005

• 한국자기공명학회:학술대회논문집
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• 한국자기공명학회 2000년도 제17회 학술발표회
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• pp.25-25
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• 2000

• 대한약학회:학술대회논문집
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• 대한약학회 2004년도 Proceedings of the Convention of the Pharmaceutical Society of Korea Vol.2
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• pp.148-149
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• 2004

• 대한세포병리학회:학술대회논문집
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• 대한세포병리학회 1993년도 제7차 춘계학술대회 초록집
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• pp.18.2-19
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• 1993

• Bulletin of the Korean Chemical Society
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• 제27권4호
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• pp.477-478
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• 2006