hcmv drug resistance mutations search tool Search Results


hcm mutations  (ALFARES Pharmaceuticals)
90
ALFARES Pharmaceuticals hcm mutations
Locations of 17 hypertrophic cardiomyopathy mutations in the myosin catalytic domain. (A) Cartoon showing two groups of <t>HCM</t> <t>mutations.</t> Four mutations are in the converter domain (dark green), and 13 are on or very near the myosin mesa (bright green). Sixteen of the HCM mutations were chosen because they have been documented to be the cause of HCM in families carrying these mutations (Alfares et al., 2015). The 17th is M531R, which, while only documented in one family, is a left ventricular non-compaction mutant myosin that appears to be hypercontractile in our studies. (B) The top view of the mesa showing 13 mutations on or near the mesa surface. The residues labeled in blue denote the positively charged amino acids. (C) The same view as in B except the surface charge distribution is shown. I263T, N444S, and M531R are slightly below the surface in acidic pockets, while the remainder of the mutations are on or very near the surface and most are arginine residues, seven of which form a particularly large domain of positive charge on the right half of the mesa as viewed.
Hcm Mutations, supplied by ALFARES Pharmaceuticals, used in various techniques. Bioz Stars score: 90/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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35s]methionine labeled, in vitro-transcribed and -translated eid-1 or mutations (promega)  (Promega)
90
Promega 35s]methionine labeled, in vitro-transcribed and -translated eid-1 or mutations (promega)
Locations of 17 hypertrophic cardiomyopathy mutations in the myosin catalytic domain. (A) Cartoon showing two groups of <t>HCM</t> <t>mutations.</t> Four mutations are in the converter domain (dark green), and 13 are on or very near the myosin mesa (bright green). Sixteen of the HCM mutations were chosen because they have been documented to be the cause of HCM in families carrying these mutations (Alfares et al., 2015). The 17th is M531R, which, while only documented in one family, is a left ventricular non-compaction mutant myosin that appears to be hypercontractile in our studies. (B) The top view of the mesa showing 13 mutations on or near the mesa surface. The residues labeled in blue denote the positively charged amino acids. (C) The same view as in B except the surface charge distribution is shown. I263T, N444S, and M531R are slightly below the surface in acidic pockets, while the remainder of the mutations are on or very near the surface and most are arginine residues, seven of which form a particularly large domain of positive charge on the right half of the mesa as viewed.
35s]Methionine Labeled, In Vitro Transcribed And Translated Eid 1 Or Mutations (Promega), supplied by Promega, used in various techniques. Bioz Stars score: 90/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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35s]methionine labeled, in vitro-transcribed and -translated eid-1 or mutations (promega) - by Bioz Stars, 2026-09
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go taq flexi dna polymerase  (Promega)
90
Promega go taq flexi dna polymerase
Locations of 17 hypertrophic cardiomyopathy mutations in the myosin catalytic domain. (A) Cartoon showing two groups of <t>HCM</t> <t>mutations.</t> Four mutations are in the converter domain (dark green), and 13 are on or very near the myosin mesa (bright green). Sixteen of the HCM mutations were chosen because they have been documented to be the cause of HCM in families carrying these mutations (Alfares et al., 2015). The 17th is M531R, which, while only documented in one family, is a left ventricular non-compaction mutant myosin that appears to be hypercontractile in our studies. (B) The top view of the mesa showing 13 mutations on or near the mesa surface. The residues labeled in blue denote the positively charged amino acids. (C) The same view as in B except the surface charge distribution is shown. I263T, N444S, and M531R are slightly below the surface in acidic pockets, while the remainder of the mutations are on or very near the surface and most are arginine residues, seven of which form a particularly large domain of positive charge on the right half of the mesa as viewed.
Go Taq Flexi Dna Polymerase, supplied by Promega, used in various techniques. Bioz Stars score: 90/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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mutation  (Azenta)
86
Azenta mutation
Locations of 17 hypertrophic cardiomyopathy mutations in the myosin catalytic domain. (A) Cartoon showing two groups of <t>HCM</t> <t>mutations.</t> Four mutations are in the converter domain (dark green), and 13 are on or very near the myosin mesa (bright green). Sixteen of the HCM mutations were chosen because they have been documented to be the cause of HCM in families carrying these mutations (Alfares et al., 2015). The 17th is M531R, which, while only documented in one family, is a left ventricular non-compaction mutant myosin that appears to be hypercontractile in our studies. (B) The top view of the mesa showing 13 mutations on or near the mesa surface. The residues labeled in blue denote the positively charged amino acids. (C) The same view as in B except the surface charge distribution is shown. I263T, N444S, and M531R are slightly below the surface in acidic pockets, while the remainder of the mutations are on or very near the surface and most are arginine residues, seven of which form a particularly large domain of positive charge on the right half of the mesa as viewed.
Mutation, supplied by Azenta, used in various techniques. Bioz Stars score: 86/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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software rstudio  (RStudio)
90
RStudio software rstudio
Locations of 17 hypertrophic cardiomyopathy mutations in the myosin catalytic domain. (A) Cartoon showing two groups of <t>HCM</t> <t>mutations.</t> Four mutations are in the converter domain (dark green), and 13 are on or very near the myosin mesa (bright green). Sixteen of the HCM mutations were chosen because they have been documented to be the cause of HCM in families carrying these mutations (Alfares et al., 2015). The 17th is M531R, which, while only documented in one family, is a left ventricular non-compaction mutant myosin that appears to be hypercontractile in our studies. (B) The top view of the mesa showing 13 mutations on or near the mesa surface. The residues labeled in blue denote the positively charged amino acids. (C) The same view as in B except the surface charge distribution is shown. I263T, N444S, and M531R are slightly below the surface in acidic pockets, while the remainder of the mutations are on or very near the surface and most are arginine residues, seven of which form a particularly large domain of positive charge on the right half of the mesa as viewed.
Software Rstudio, supplied by RStudio, used in various techniques. Bioz Stars score: 90/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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missense mutation-positive mutation  (CH Instruments)
90
CH Instruments missense mutation-positive mutation
Locations of 17 hypertrophic cardiomyopathy mutations in the myosin catalytic domain. (A) Cartoon showing two groups of <t>HCM</t> <t>mutations.</t> Four mutations are in the converter domain (dark green), and 13 are on or very near the myosin mesa (bright green). Sixteen of the HCM mutations were chosen because they have been documented to be the cause of HCM in families carrying these mutations (Alfares et al., 2015). The 17th is M531R, which, while only documented in one family, is a left ventricular non-compaction mutant myosin that appears to be hypercontractile in our studies. (B) The top view of the mesa showing 13 mutations on or near the mesa surface. The residues labeled in blue denote the positively charged amino acids. (C) The same view as in B except the surface charge distribution is shown. I263T, N444S, and M531R are slightly below the surface in acidic pockets, while the remainder of the mutations are on or very near the surface and most are arginine residues, seven of which form a particularly large domain of positive charge on the right half of the mesa as viewed.
Missense Mutation Positive Mutation, supplied by CH Instruments, used in various techniques. Bioz Stars score: 90/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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noninherited mutation  (NantOmics LLC)
90
NantOmics LLC noninherited mutation
Locations of 17 hypertrophic cardiomyopathy mutations in the myosin catalytic domain. (A) Cartoon showing two groups of <t>HCM</t> <t>mutations.</t> Four mutations are in the converter domain (dark green), and 13 are on or very near the myosin mesa (bright green). Sixteen of the HCM mutations were chosen because they have been documented to be the cause of HCM in families carrying these mutations (Alfares et al., 2015). The 17th is M531R, which, while only documented in one family, is a left ventricular non-compaction mutant myosin that appears to be hypercontractile in our studies. (B) The top view of the mesa showing 13 mutations on or near the mesa surface. The residues labeled in blue denote the positively charged amino acids. (C) The same view as in B except the surface charge distribution is shown. I263T, N444S, and M531R are slightly below the surface in acidic pockets, while the remainder of the mutations are on or very near the surface and most are arginine residues, seven of which form a particularly large domain of positive charge on the right half of the mesa as viewed.
Noninherited Mutation, supplied by NantOmics LLC, used in various techniques. Bioz Stars score: 90/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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mutation-specific forward primer  (PrimerDesign Inc)
90
PrimerDesign Inc mutation-specific forward primer
Locations of 17 hypertrophic cardiomyopathy mutations in the myosin catalytic domain. (A) Cartoon showing two groups of <t>HCM</t> <t>mutations.</t> Four mutations are in the converter domain (dark green), and 13 are on or very near the myosin mesa (bright green). Sixteen of the HCM mutations were chosen because they have been documented to be the cause of HCM in families carrying these mutations (Alfares et al., 2015). The 17th is M531R, which, while only documented in one family, is a left ventricular non-compaction mutant myosin that appears to be hypercontractile in our studies. (B) The top view of the mesa showing 13 mutations on or near the mesa surface. The residues labeled in blue denote the positively charged amino acids. (C) The same view as in B except the surface charge distribution is shown. I263T, N444S, and M531R are slightly below the surface in acidic pockets, while the remainder of the mutations are on or very near the surface and most are arginine residues, seven of which form a particularly large domain of positive charge on the right half of the mesa as viewed.
Mutation Specific Forward Primer, supplied by PrimerDesign Inc, used in various techniques. Bioz Stars score: 90/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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transgenic mice carrying a caspase-3 null mutation  (Merck KGaA)
90
Merck KGaA transgenic mice carrying a caspase-3 null mutation
Locations of 17 hypertrophic cardiomyopathy mutations in the myosin catalytic domain. (A) Cartoon showing two groups of <t>HCM</t> <t>mutations.</t> Four mutations are in the converter domain (dark green), and 13 are on or very near the myosin mesa (bright green). Sixteen of the HCM mutations were chosen because they have been documented to be the cause of HCM in families carrying these mutations (Alfares et al., 2015). The 17th is M531R, which, while only documented in one family, is a left ventricular non-compaction mutant myosin that appears to be hypercontractile in our studies. (B) The top view of the mesa showing 13 mutations on or near the mesa surface. The residues labeled in blue denote the positively charged amino acids. (C) The same view as in B except the surface charge distribution is shown. I263T, N444S, and M531R are slightly below the surface in acidic pockets, while the remainder of the mutations are on or very near the surface and most are arginine residues, seven of which form a particularly large domain of positive charge on the right half of the mesa as viewed.
Transgenic Mice Carrying A Caspase 3 Null Mutation, supplied by Merck KGaA, used in various techniques. Bioz Stars score: 90/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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virsnip assays tib molbiol  (TIB MOLBIOL)
90
TIB MOLBIOL virsnip assays tib molbiol
Locations of 17 hypertrophic cardiomyopathy mutations in the myosin catalytic domain. (A) Cartoon showing two groups of <t>HCM</t> <t>mutations.</t> Four mutations are in the converter domain (dark green), and 13 are on or very near the myosin mesa (bright green). Sixteen of the HCM mutations were chosen because they have been documented to be the cause of HCM in families carrying these mutations (Alfares et al., 2015). The 17th is M531R, which, while only documented in one family, is a left ventricular non-compaction mutant myosin that appears to be hypercontractile in our studies. (B) The top view of the mesa showing 13 mutations on or near the mesa surface. The residues labeled in blue denote the positively charged amino acids. (C) The same view as in B except the surface charge distribution is shown. I263T, N444S, and M531R are slightly below the surface in acidic pockets, while the remainder of the mutations are on or very near the surface and most are arginine residues, seven of which form a particularly large domain of positive charge on the right half of the mesa as viewed.
Virsnip Assays Tib Molbiol, supplied by TIB MOLBIOL, used in various techniques. Bioz Stars score: 90/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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p/q calcium channel gene  (Wieser GmbH)
90
Wieser GmbH p/q calcium channel gene
Locations of 17 hypertrophic cardiomyopathy mutations in the myosin catalytic domain. (A) Cartoon showing two groups of <t>HCM</t> <t>mutations.</t> Four mutations are in the converter domain (dark green), and 13 are on or very near the myosin mesa (bright green). Sixteen of the HCM mutations were chosen because they have been documented to be the cause of HCM in families carrying these mutations (Alfares et al., 2015). The 17th is M531R, which, while only documented in one family, is a left ventricular non-compaction mutant myosin that appears to be hypercontractile in our studies. (B) The top view of the mesa showing 13 mutations on or near the mesa surface. The residues labeled in blue denote the positively charged amino acids. (C) The same view as in B except the surface charge distribution is shown. I263T, N444S, and M531R are slightly below the surface in acidic pockets, while the remainder of the mutations are on or very near the surface and most are arginine residues, seven of which form a particularly large domain of positive charge on the right half of the mesa as viewed.
P/Q Calcium Channel Gene, supplied by Wieser GmbH, used in various techniques. Bioz Stars score: 90/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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connexin40 mutation  (SCHOTT)
90
SCHOTT connexin40 mutation
Locations of 17 hypertrophic cardiomyopathy mutations in the myosin catalytic domain. (A) Cartoon showing two groups of <t>HCM</t> <t>mutations.</t> Four mutations are in the converter domain (dark green), and 13 are on or very near the myosin mesa (bright green). Sixteen of the HCM mutations were chosen because they have been documented to be the cause of HCM in families carrying these mutations (Alfares et al., 2015). The 17th is M531R, which, while only documented in one family, is a left ventricular non-compaction mutant myosin that appears to be hypercontractile in our studies. (B) The top view of the mesa showing 13 mutations on or near the mesa surface. The residues labeled in blue denote the positively charged amino acids. (C) The same view as in B except the surface charge distribution is shown. I263T, N444S, and M531R are slightly below the surface in acidic pockets, while the remainder of the mutations are on or very near the surface and most are arginine residues, seven of which form a particularly large domain of positive charge on the right half of the mesa as viewed.
Connexin40 Mutation, supplied by SCHOTT, used in various techniques. Bioz Stars score: 90/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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Image Search Results


Locations of 17 hypertrophic cardiomyopathy mutations in the myosin catalytic domain. (A) Cartoon showing two groups of HCM mutations. Four mutations are in the converter domain (dark green), and 13 are on or very near the myosin mesa (bright green). Sixteen of the HCM mutations were chosen because they have been documented to be the cause of HCM in families carrying these mutations (Alfares et al., 2015). The 17th is M531R, which, while only documented in one family, is a left ventricular non-compaction mutant myosin that appears to be hypercontractile in our studies. (B) The top view of the mesa showing 13 mutations on or near the mesa surface. The residues labeled in blue denote the positively charged amino acids. (C) The same view as in B except the surface charge distribution is shown. I263T, N444S, and M531R are slightly below the surface in acidic pockets, while the remainder of the mutations are on or very near the surface and most are arginine residues, seven of which form a particularly large domain of positive charge on the right half of the mesa as viewed.

Journal: The Journal of Experimental Biology

Article Title: Effects of hypertrophic and dilated cardiomyopathy mutations on power output by human β-cardiac myosin

doi: 10.1242/jeb.125930

Figure Lengend Snippet: Locations of 17 hypertrophic cardiomyopathy mutations in the myosin catalytic domain. (A) Cartoon showing two groups of HCM mutations. Four mutations are in the converter domain (dark green), and 13 are on or very near the myosin mesa (bright green). Sixteen of the HCM mutations were chosen because they have been documented to be the cause of HCM in families carrying these mutations (Alfares et al., 2015). The 17th is M531R, which, while only documented in one family, is a left ventricular non-compaction mutant myosin that appears to be hypercontractile in our studies. (B) The top view of the mesa showing 13 mutations on or near the mesa surface. The residues labeled in blue denote the positively charged amino acids. (C) The same view as in B except the surface charge distribution is shown. I263T, N444S, and M531R are slightly below the surface in acidic pockets, while the remainder of the mutations are on or very near the surface and most are arginine residues, seven of which form a particularly large domain of positive charge on the right half of the mesa as viewed.

Article Snippet: Sixteen of the HCM mutations were chosen because they have been documented to be the cause of HCM in families carrying these mutations ( Alfares et al., 2015 ).

Techniques: Mutagenesis, Labeling