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EMS mutagens for example(passive) caused byPoint mutations
iii ) diseasecausingpoint mutations
The most common diseasecausingpoint mutation in mtDNA
reguards to these diseasecausingpoint mutations
known diseasecausingDNAI1 mutation
errors in the DNA replication and by mutagens(passive) are caused byPoint mutations
using the QuikChange ® site - directed mutagenesis kit ( Stratagene , La Jolla , CA , U.S.A.(passive) were createdPoint mutations
using a QuikChange site - directed mutagenesis kit ( Stratagene ) according to the manufacturer 's instructions(passive) were createdPoint mutations
using the QuickChange site - directed mutagenesis kit ( Stratagene , La Jolla , CA(passive) were createdPoint mutations
chemicals or malfunction of DNA replication(passive) often caused byPoint mutations
a gene mutated by chemical mutagenscreatepoint mutations
Ultraviolet ( UV ) radiationcausespoint mutations
using the QuikChange site - directed mutagenesis kit ( Stratagene , La Jolla , CA ) according to the manufacturer 's instructions , using full - length(passive) was created byS1928A ) mutation
using the QuikChange kit ( Stratagene(passive) were createdPoint mutations
Methods for detecting methylated nucleotidesUS7368239Aug 26 , 2004May 6 , 2008Applera CorporationReacting DNA with magnesium bisulfite ; kitsUS7371526Aug 26 , 2004May 13 , 2008Applera CorporationReacting nucleic acids with magnesium / sodium bisulfite in presence of polyamine catalyst ( guanidineto createpoint mutations
ArticlePubMedGoogle Scholar Stokowski RP , Cox DR : Functional analysis of the neurofibromatosis type 2 protein by means of diseasecausingpoint mutations
miscopying of just one or a small number of nucleotides(passive) is caused byPoint mutation
Site - directed mutagenesis was usedto createpoint mutations
that changed codon 65 from arginine ( CGT ) to histidine ( CAT ) in one allele.more(passive) was discoveredA point mutation
mutagens , things like chemicals or radiation that damage DNA(passive) can also be caused byPoint mutations
using QuikChange II site - directed mutagenesis ( Agilent(passive) were createdpoint mutations
misincorporation during repair DNA synthesis or novel junctions made by nonhomologous end joining ( NHEJ(passive) caused bypoint mutations
PubMed Abstract | Publisher Full Text Stokowski RP , Cox DR : Functional analysis of the neurofibromatosis type 2 protein by means of diseasecausingpoint mutations
at position 4 of the leader sequence of the RSV genome clone ( C residue to G(passive) was createdA point mutation
when exchanging a single nucleotide for another ( Freese , 1959a ) , in respect to the CRS ( or other reference sequence(passive) are causedPoint mutations
substitution of serine for asparagine at position 17 ( Rap1N17(passive) created bya point mutation
B. A largebody of research ... chemi - calscausepoint mutations
genome editing techniques(passive) created bypoint mutations
in full - length pLgateway_SAMHD1IRESYFP(passive) were createdPoint mutations
a single nucleotide substitution in a normal DNA sequence(passive) caused bypoint mutations
with the GeneTailor Site - Directed Mutagenesis Kit ( Invitrogen(passive) were createdPoint mutations
the substitution of one nucleotide for another(passive) caused byPoint MutationA mutation
in box D , which in U14 is known to lead to underaccumulation of snoRNA ( 23(passive) was createdA point mutation
using the QuickChange mutagenesis kit ( Stratagene , USA(passive) were createdPoint mutations
errors in chromosome replication that are not corrected in proofreading or by environmental mutagens such as chemicals and radiation(passive) can be caused byPoint mutations
QuickChange II Site - Directed Mutagenesis Kit ( Agilent(passive) were created byPoint mutations
A site - directed mutagenesis kit ( QuikChangeII ; Stratagene ) was usedto createpoint mutations
Ultraviolet light Thymine dimerHow to createpoint mutations
DNA dimerscausepoint mutations
DNA lesionscreatepoint mutations
in single amino acid substitutions at critical positionsresultingin single amino acid substitutions at critical positions
to single amino acid substitutions to large truncationsleadingto single amino acid substitutions to large truncations
to single amino acid substitutions in SQLE proteinsleadingto single amino acid substitutions in SQLE proteins
amino acid substitutions in proteinscausingamino acid substitutions in proteins
amino acid substitutions in the � a � determinantcausingamino acid substitutions in the � a � determinant
to amino acid substitutions or truncationsleadingto amino acid substitutions or truncations
to the corresponding amino acid substitutionsleadingto the corresponding amino acid substitutions
to amino acid substitutions in both VP2 and VP3leadto amino acid substitutions in both VP2 and VP3
to amino acid substitutions in Fm - PEPleadingto amino acid substitutions in Fm - PEP
in amino acid substitutions in HBsAg proteinmay resultin amino acid substitutions in HBsAg protein
in amino acid substitutions in the reverse transcriptaseresultingin amino acid substitutions in the reverse transcriptase
in amino acid substitutions ... black arrowsresultedin amino acid substitutions ... black arrows
to amino acid substitutions and a gain of toxic functionleadto amino acid substitutions and a gain of toxic function
in amino acid substitutions in the respective protein domainsresultingin amino acid substitutions in the respective protein domains
in amino acid substitutions near the C terminus ofwould resultin amino acid substitutions near the C terminus of
amino acid substitutions A353V and G402E into the mousecausingamino acid substitutions A353V and G402E into the mouse
amino acid substitutions ... D1595H in DC-30causedamino acid substitutions ... D1595H in DC-30
in two amino acid substitutions in the F generesultingin two amino acid substitutions in the F gene
the amino acid substitutions R86H , Y107C , and A134 Tcausingthe amino acid substitutions R86H , Y107C , and A134 T
in stop codons , frameshift mutations or amino acid substitutions".16may resultin stop codons , frameshift mutations or amino acid substitutions".16
to amino acid substitutions in either extracellular or cytoplasmic domainsleadingto amino acid substitutions in either extracellular or cytoplasmic domains
to amino acid substitutions within the keratin rod domainleadingto amino acid substitutions within the keratin rod domain
in amino acid substitutions L10F , M46I , I47V , and I50V.resultingin amino acid substitutions L10F , M46I , I47V , and I50V.
in amino acid substitutions in a wide variety of human cancersresultingin amino acid substitutions in a wide variety of human cancers
single amino acid substitutions in or adjacent to predicted functional domains of RpoN and AlgT , respectively ( Fig . S1causingsingle amino acid substitutions in or adjacent to predicted functional domains of RpoN and AlgT , respectively ( Fig . S1
premature stop codons or abnormal splicingcausingpremature stop codons or abnormal splicing
in amino acid substitutions , termination , exon skipping , or splicing defectsresultingin amino acid substitutions , termination , exon skipping , or splicing defects
to amino acid substitutions ( 5 ) and direct repeat insertions ( 3leadingto amino acid substitutions ( 5 ) and direct repeat insertions ( 3
to amino acid substitutions at one of four amino acid positionsleadingto amino acid substitutions at one of four amino acid positions
to amino acid substitutions in the CYP51A protein ( TR46 / Y121 / T289leadingto amino acid substitutions in the CYP51A protein ( TR46 / Y121 / T289
to premature stop codons and disrupted synthesis of the dystrophin protein ( 1leadingto premature stop codons and disrupted synthesis of the dystrophin protein ( 1
in premature termination codons or amino acid substitutions in the hormone- or DNA - binding domains of the receptorresultin premature termination codons or amino acid substitutions in the hormone- or DNA - binding domains of the receptor
premature stop codons ( small deletions and nonsense changescausingpremature stop codons ( small deletions and nonsense changes
in amino acid substitutions in antigenic sites on the surface of the HA ( 1 , 25resultingin amino acid substitutions in antigenic sites on the surface of the HA ( 1 , 25
to premature stop codons ( eg , AR - Q640Xleadingto premature stop codons ( eg , AR - Q640X
to frame shifts and premature stop codons in coding regionsleadingto frame shifts and premature stop codons in coding regions
two amino acid substitutions in the open reading frame ( E430V T550Acausetwo amino acid substitutions in the open reading frame ( E430V T550A
to specific amino acid substitutions that produce a dysfunc- tional antithrombin proteinleadingto specific amino acid substitutions that produce a dysfunc- tional antithrombin protein
to amino acid substitutions or early stop codons , confirming PsMAX2 is RMS4 ( Fig . 1leadingto amino acid substitutions or early stop codons , confirming PsMAX2 is RMS4 ( Fig . 1
to single amino acid substitutions mutations leading to premature termination of protein translation deletions insertions splicing mutations along with other more technical substitutions or rearrangementsleadingto single amino acid substitutions mutations leading to premature termination of protein translation deletions insertions splicing mutations along with other more technical substitutions or rearrangements