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Biochemistry|January 31, 1984
1H NMR (500 MHz) of gene 32 protein--oligonucleotide complexesR V Prigodich, J Casas-Finet, K R Williams, et al.Human Movement Science|November 2, 2018
Qualitative and quantitative change in the kinematics of learning a non-dominant overarm throwHannah A Palmer, Karl M Newell, Dan Gordon, et al.Biochemistry|December 26, 1989
p10 single-stranded nucleic acid binding protein from murine leukemia virus binds metal ions via the peptide sequence Cys26-X2-Cys29-X4-His34-X4-Cys39W J Roberts, T Pan, J I Elliott, et al.Neurobiology of Disease|January 1, 1997
Apolipoprotein E uptake and low-density lipoprotein receptor-related protein expression by the NTera2/D1 cell line: a cell culture model of relevance for late-onset Alzheimer's diseaseK R Williams, V Pye, A M Saunders, et al.Biochemistry|July 12, 1994
Purification and nucleic acid binding properties of a fragment of type C1/C2 heterogeneous nuclear ribonucleoprotein from thymic nuclear extractsS B Amrute, Z Abdul-Manan, V Pandey, et al.The Journal of Biological Chemistry|June 25, 1985
A monoclonal antibody that recognizes the functional domain of Escherichia coli single-stranded DNA binding protein that includes the ssb-113 mutationJ W Chase, J Flory, N H Ruddle, et al.Scientific Reports|January 12, 2021
Bidirectional causal control in the dynamics of handstand balanceHannah E Wyatt, Domenico Vicinanza, Karl M Newell, et al.The Journal of Biological Chemistry|December 25, 1989
Phosphorylation of DARPP-32, a dopamine- and cAMP-regulated phosphoprotein, by casein kinase IIJ A Girault, H C Hemmings, K R Williams, et al.The Journal of Biological Chemistry|May 5, 1989
ARPP-21, a cyclic AMP-regulated phosphoprotein (Mr = 21,000) enriched in dopamine-innervated brain regions. Amino acid sequence of the site phosphorylated by cyclic AMP in intact cells and kinetic studies of its phosphorylation in vitroH C Hemmings, J A Girault, K R Williams, et al.The Journal of Biological Chemistry|March 5, 1988
Phenylalanines that are conserved among several RNA-binding proteins form part of a nucleic acid-binding pocket in the A1 heterogeneous nuclear ribonucleoproteinB M Merrill, K L Stone, F Cobianchi, et al.Pageof 25