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J Kallijärvi

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Biochemistry|August 22, 2001
Amphoterin includes a sequence motif which is homologous to the Alzheimer's beta-amyloid peptide (Abeta), forms amyloid fibrils in vitro, and binds avidly to AbetaJ Kallijärvi, M Haltia, M H Baumann
The Biochemical Journal|June 22, 2000
Apolipoprotein E includes a binding site which is recognized by several amyloidogenic polypeptidesM H Baumann, J Kallijärvi, H Lankinen, et al.
Clinical Genetics|November 15, 2006
Wilms' tumor and novel TRIM37 mutations in an Australian patient with mulibrey nanismR H Hämäläinen, D Mowat, M T Gabbett, et al.
Experimental & Molecular Medicine|April 3, 2023
Altered acylcarnitine metabolism and inflexible mitochondrial fuel utilization characterize the loss of neonatal myocardial regeneration capacityE Kankuri, P Finckenberg, J Leinonen, et al.
Pageof 1

Showing results (1-10 of 4) with videos related to

Sort By:
Pageof 1
Biochemistry|August 22, 2001
Amphoterin includes a sequence motif which is homologous to the Alzheimer's beta-amyloid peptide (Abeta), forms amyloid fibrils in vitro, and binds avidly to AbetaJ Kallijärvi, M Haltia, M H Baumann
The Biochemical Journal|June 22, 2000
Apolipoprotein E includes a binding site which is recognized by several amyloidogenic polypeptidesM H Baumann, J Kallijärvi, H Lankinen, et al.
Clinical Genetics|November 15, 2006
Wilms' tumor and novel TRIM37 mutations in an Australian patient with mulibrey nanismR H Hämäläinen, D Mowat, M T Gabbett, et al.
Experimental & Molecular Medicine|April 3, 2023
Altered acylcarnitine metabolism and inflexible mitochondrial fuel utilization characterize the loss of neonatal myocardial regeneration capacityE Kankuri, P Finckenberg, J Leinonen, et al.
Pageof 1