Identification of amyloid fibril-forming segments based on structure and residue-based statistical potential | Zendy

Zhuqing Zhang | Zendy; Hao Chen | Zendy; Luhua Lai | Zendy

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Identification of amyloid fibril-forming segments based on structure and residue-based statistical potential

Author(s) -

Zhuqing Zhang,

Hao Chen,

Luhua Lai

Publication year - 2007

Publication title -

bioinformatics

Language(s) - English

Resource type - Journals

SCImago Journal Rank - 3.599

H-Index - 390

eISSN - 1367-4811

pISSN - 1367-4803

DOI - 10.1093/bioinformatics/btm325

Subject(s) - amyloid fibril , fibril , proteome , computational biology , amyloid disease , amyloid (mycology) , protein folding , residue (chemistry) , identification (biology) , computer science , structural bioinformatics , chemistry , bioinformatics , protein structure , biochemistry , biology , amyloid β , medicine , inorganic chemistry , botany , disease , pathology

Experimental evidence suggests that certain short protein segments have stronger amyloidogenic propensities than others. Identification of the fibril-forming segments of proteins is crucial for understanding diseases associated with protein misfolding and for finding favorable targets for therapeutic strategies.

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