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The catalytic α subunits cannot bind the NPxYR sequence of ApoER2, but a point mutation that converts the arginine residue adjacent to the NPxY motif to a leucine rescued Pafah1b α subunit binding, demonstrating that this residue is critical for coupling the Pafah1b complex selectively with VLDLR.

Sequencing of these genes from osu1-2 revealed that At1g78230 was identical to the reference sequence, and an A to T mutation in the seventh exon of At1g78240 (Figure 6B) resulting in a missense mutation that converts Asn at 560 to Tyr (N560Y).

However, it has a mutation that converts Phe-29 in the AVR4 protein to leucine.

CCC5 is identical to CCC3 save for a point mutation that converts the methionine (ATG) in the proximal translational start site to an isoleucine.

In a previous report [ 25], we described a new neuroanatomical phenotype in Bbs2 −/−, Bbs4 −/−, Bbs6 −/− and Bbs1 M390R/M390R knockin mutant mice (mice homozygous for the most common human BBS mutation that converts a methionine codon to an arginine codon).

In fact, a single-point mutation that converts the glycine residue into cysteine was sufficient to generate a mutant protein with activity similar to a bona fide DSP [ 7].

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Methylcytosine tends to mutate to thymine (T), thus the gradational accumulation of mutation that convert CpG dinucleotides to TpG dinucleotides lead to AT-rich genomes [ 37– 37].

Therefore, we sequenced the MRH2 genomic DNA and found that there was a G to A mutation that converted a conserved 3' splicing site AG (at the end of the 5th intron) to AA (Figure 2A, upper panel).

This transgenic contained a site-specific mutation that converted the DLNQIP EAR-motif at positions 143-148 to AAAQIA at the same position (as shown in Figure 1A).

We were then able to engineer an in silico mutant channel with three point mutations that converted mVDAC1 into a channel with a preference for cations.

Mutations that convert the normal c-Myb protein into an oncogenic transforming protein also change the spectrum of genes that it regulates [2], [3].

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