A L Fink

Natively unfolded human prothymosin alpha adopts partially folded collapsed conformation at acidic pH.

S Doniach, V. Uversky, A. Fink, 1999, Biochemistry.

Mechanism of acid-induced folding of proteins.

A. Fink, N. Takahashi, Y. Goto, 1990, Biochemistry.

Association-induced folding of globular proteins.

S Doniach, V. Uversky, A. Fink, 1998, Proceedings of the National Academy of Sciences of the United States of America.

Discrete intermediates versus molten globule models for protein folding: characterization of partially folded intermediates of apomyoglobin.

A. Fink, K. Oberg, A L Fink, 1998, Folding & design.

Zn(2+)-mediated structure formation and compaction of the "natively unfolded" human prothymosin alpha.

S Doniach, V. Uversky, A. Fink, 2000, Biochemical and biophysical research communications.

Intermediate conformational states of apocytochrome c.

A L Fink, M Kataoka, Y Goto, 1993, Biochemistry.

Lysine-73 is involved in the acylation and deacylation of beta-lactamase.

A. Fink, A L Fink, E J Lietz, 2000, Biochemistry.

Conformational states of beta-lactamase: molten-globule states at acidic and alkaline pH with high salt.

A. Fink, Y. Goto, A L Fink, 1989, Biochemistry.

Pesticides directly accelerate the rate of α‐synuclein fibril formation: a possible factor in Parkinson's disease

V. Uversky, Jie Li, A. Fink, 2001, FEBS letters.

Metal-triggered structural transformations, aggregation, and fibrillation of human alpha-synuclein. A possible molecular NK between Parkinson's disease and heavy metal exposure.

V. Uversky, Jie Li, A. Fink, 2001, The Journal of biological chemistry.