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ATCC caption a7 orf ncbi annotation gene intensity b val val ratio 1504 ncgl0899 similarity
ORFs showing altered relative mRNA levels in response to l -valine in the valine production strain VAL1 a
Caption A7 Orf Ncbi Annotation Gene Intensity B Val Val Ratio 1504 Ncgl0899 Similarity, supplied by ATCC, used in various techniques. Bioz Stars score: 95/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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ATCC genbank
ORFs showing altered relative mRNA levels in response to l -valine in the valine production strain VAL1 a
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ORFs showing altered relative mRNA levels in response to l -valine in the valine production strain VAL1 a
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ORFs showing altered relative mRNA levels in response to l -valine in the valine production strain VAL1 a
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ORFs showing altered relative mRNA levels in response to l -valine in the valine production strain VAL1 a
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Upper panels show In vivo MRI examinations of endothelial function in the femoral artery (A) and thoracic aorta (B) in response to acetylcholine (ACh, 16.6 mg/kg i.p.) administered to female wildtype (WT, open symbols, n = 6 for the femoral artery and n = 4 for the thoracic aorta) and <t>GPR18</t> knockout (KO, green symbols, n = 5 for the femoral artery and n = 44 for the thoracic aorta) mice. The unaltered endothelium‐independent responses to infusion of the NO‐donor to sodium nitroprusside (SNP, 1 mg/kg i.v.; WT: N = 5 for the femoral artery and n = 3 for the thoracic aorta; KO: N = 5 for the femoral artery and n = 4 for the thoracic aorta) are shown as insets. Results are shown as changes in vessel volume. The horizontal line represents the mean. p ‐value from Student's t‐test vs. WT. (C) Ex vivo analysis of endothelium‐dependent relaxations in response to ACh administered to 10 μM PE‐precontracted arterial rings of the femoral artery derived from female mice (WT, n = 7; KO, n = 9) in the presence of 10 μM indomethacin. Inset shows endothelial‐independent relaxations in response to DEANO measured in 10 μM PE‐precontracted arterial rings of the femoral artery (WT, n = 8; KO, n = 8), in the presence of 10 μM indomethacin and 300 μM L‐NAME, to inhibit any possible confounding effects of endogenous NOS or COX activity, respectively. The overall P of significant two‐way ANOVA comparison of KO vs. WT is indicated in each concentration‐response graph. * p < 0.05 (Holm‐Sidak post hoc test vs. WT). (D) Representative images and analysis of immunofluorescent staining for endothelial nitric oxide synthase (eNOS) in femoral arteries derived from female GPR18 KO (green circles, n = 3) compared with female WT mice (open circles, n = 4). The horizontal line represents the mean; P‐value from Student's t‐test vs. WT. The micrographs show representative immunofluorescence stainings. Size bar represents 50 μm. (E) Concentration‐response relaxations to acetylcholine (ACh) in the absence (circles; WT, n = 7; KO, n = 10) and presence (squares; WT, n = 7; KO, n = 9) of 10 μM indomethacin in 10 μM PE‐precontracted isolated femoral arteries derived from female WT (left panel with open symbols) and GPR18 KO (left panel with green symbols). The overall p of two‐way ANOVA comparison of KO vs. WT is indicated in each concentration‐response graph. * p < 0.05 (Holm‐Sidak post hoc test vs. WT).
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Upper panels show In vivo MRI examinations of endothelial function in the femoral artery (A) and thoracic aorta (B) in response to acetylcholine (ACh, 16.6 mg/kg i.p.) administered to female wildtype (WT, open symbols, n = 6 for the femoral artery and n = 4 for the thoracic aorta) and <t>GPR18</t> knockout (KO, green symbols, n = 5 for the femoral artery and n = 44 for the thoracic aorta) mice. The unaltered endothelium‐independent responses to infusion of the NO‐donor to sodium nitroprusside (SNP, 1 mg/kg i.v.; WT: N = 5 for the femoral artery and n = 3 for the thoracic aorta; KO: N = 5 for the femoral artery and n = 4 for the thoracic aorta) are shown as insets. Results are shown as changes in vessel volume. The horizontal line represents the mean. p ‐value from Student's t‐test vs. WT. (C) Ex vivo analysis of endothelium‐dependent relaxations in response to ACh administered to 10 μM PE‐precontracted arterial rings of the femoral artery derived from female mice (WT, n = 7; KO, n = 9) in the presence of 10 μM indomethacin. Inset shows endothelial‐independent relaxations in response to DEANO measured in 10 μM PE‐precontracted arterial rings of the femoral artery (WT, n = 8; KO, n = 8), in the presence of 10 μM indomethacin and 300 μM L‐NAME, to inhibit any possible confounding effects of endogenous NOS or COX activity, respectively. The overall P of significant two‐way ANOVA comparison of KO vs. WT is indicated in each concentration‐response graph. * p < 0.05 (Holm‐Sidak post hoc test vs. WT). (D) Representative images and analysis of immunofluorescent staining for endothelial nitric oxide synthase (eNOS) in femoral arteries derived from female GPR18 KO (green circles, n = 3) compared with female WT mice (open circles, n = 4). The horizontal line represents the mean; P‐value from Student's t‐test vs. WT. The micrographs show representative immunofluorescence stainings. Size bar represents 50 μm. (E) Concentration‐response relaxations to acetylcholine (ACh) in the absence (circles; WT, n = 7; KO, n = 10) and presence (squares; WT, n = 7; KO, n = 9) of 10 μM indomethacin in 10 μM PE‐precontracted isolated femoral arteries derived from female WT (left panel with open symbols) and GPR18 KO (left panel with green symbols). The overall p of two‐way ANOVA comparison of KO vs. WT is indicated in each concentration‐response graph. * p < 0.05 (Holm‐Sidak post hoc test vs. WT).
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Validation of the proteomic results by western blotting and immunohistochemistry. ( A ) Differential expression of selected proteins as detected by mass spectrometry. ( B , C ) Expression of upregulated proteins by western blot (B) and quantification of protein levels normalized to ACTIN content (C). ( D , E ) Expression of downregulated proteins by western blot (D) and quantification of protein levels normalized to ACTIN content (E). ( F , G ) Representative images of human ovarian cortical sections stained with SERPIN G1 (F) and <t>NCBP2</t> (G). ( H , I ) Quantification of the percentage of SERPIN G1-positive area and NCBP2-positive nuclei. ( J ) Negative control for the immunostaining. Data are expressed as mean ± SD or scatter plots ± SD; N = 5 per experimental group. * P < 0.05; ** P < 0.01; *** P < 0.001; ns: not significant. ECM, extracellular matrix.
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Validation of the proteomic results by western blotting and immunohistochemistry. ( A ) Differential expression of selected proteins as detected by mass spectrometry. ( B , C ) Expression of upregulated proteins by western blot (B) and quantification of protein levels normalized to ACTIN content (C). ( D , E ) Expression of downregulated proteins by western blot (D) and quantification of protein levels normalized to ACTIN content (E). ( F , G ) Representative images of human ovarian cortical sections stained with SERPIN G1 (F) and <t>NCBP2</t> (G). ( H , I ) Quantification of the percentage of SERPIN G1-positive area and NCBP2-positive nuclei. ( J ) Negative control for the immunostaining. Data are expressed as mean ± SD or scatter plots ± SD; N = 5 per experimental group. * P < 0.05; ** P < 0.01; *** P < 0.001; ns: not significant. ECM, extracellular matrix.
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Image Search Results


ORFs showing altered relative mRNA levels in response to l -valine in the valine production strain VAL1 a

Journal:

Article Title: Global Expression Profiling and Physiological Characterization of Corynebacterium glutamicum Grown in the Presence of l -Valine

doi: 10.1128/AEM.69.5.2521-2532.2003

Figure Lengend Snippet: ORFs showing altered relative mRNA levels in response to l -valine in the valine production strain VAL1 a

Article Snippet: Proteins showing altered abundances on 2-D gels in response to l -valine in the wild-type C. glutamicum ATCC 13032 table ft1 table-wrap mode="anchored" t5 TABLE 5. caption a7 ORF NCBI Annotation Gene Intensity b −Val +Val Ratio 1504 NCgl0899 Similarity to 2-nitropropane dioxygenase ( Williopsis mrakii ) 0.4 0.2 0.5 3194 NCgl2167 Pyruvate dehydrogenase component E1 aceE ( C. glutamicum ) 0.6 0.2 0.3 990 NCgl0478 Strong similarity to translation elongation factor EF-G fusA ( E. coli ) 0.3 0.6 2.3 1414 NCgl0827 Strong similarity to PurH bifunctional enzyme ( E. coli ) 0.3 1.5 4.3 2793 NCgl1222 Acetolactate synthase large-chain ilvB ( C. glutamicum ) ilvB 1.6 4.9 3.1 2793 NCgl1222 Acetolactate synthase large-chain ilvB ( C. glutamicum ) ilvB 0.8 3.1 3.6 2793 NCgl1222 Acetolactate synthase large-chain ilvB ( C. glutamicum ) ilvB 0.4 1.5 4.1 2793 NCgl1222 Acetolactate synthase large-chain ilvB ( C. glutamicum ) ilvB 0.2 0.7 4.2 2793 NCgl1222 Acetolactate synthase large-chain ilvB ( C. glutamicum ) ilvB 0.5 2.4 5.1 2793 NCgl1222 Acetolactate synthase large-chain ilvB ( C. glutamicum ) ilvB 0.6 3.4 5.3 2793 NCgl1222 Acetolactate synthase large-chain ilvB ( C. glutamicum ) ilvB 0.2 1.0 5.9 2793 NCgl1222 Acetolactate synthase large-chain ilvB ( C. glutamicum ) ilvB 0.2 1.6 7.2 Open in a separate window a Abbreviations, conditions, and statistical analysis are described in footnotes to Table . b +Val, growth under addition of 40 mM l -valine.

Techniques:

Proteins showing altered abundances on 2-D gels in response to l -valine in the valine production strain VAL1 a

Journal:

Article Title: Global Expression Profiling and Physiological Characterization of Corynebacterium glutamicum Grown in the Presence of l -Valine

doi: 10.1128/AEM.69.5.2521-2532.2003

Figure Lengend Snippet: Proteins showing altered abundances on 2-D gels in response to l -valine in the valine production strain VAL1 a

Article Snippet: Proteins showing altered abundances on 2-D gels in response to l -valine in the wild-type C. glutamicum ATCC 13032 table ft1 table-wrap mode="anchored" t5 TABLE 5. caption a7 ORF NCBI Annotation Gene Intensity b −Val +Val Ratio 1504 NCgl0899 Similarity to 2-nitropropane dioxygenase ( Williopsis mrakii ) 0.4 0.2 0.5 3194 NCgl2167 Pyruvate dehydrogenase component E1 aceE ( C. glutamicum ) 0.6 0.2 0.3 990 NCgl0478 Strong similarity to translation elongation factor EF-G fusA ( E. coli ) 0.3 0.6 2.3 1414 NCgl0827 Strong similarity to PurH bifunctional enzyme ( E. coli ) 0.3 1.5 4.3 2793 NCgl1222 Acetolactate synthase large-chain ilvB ( C. glutamicum ) ilvB 1.6 4.9 3.1 2793 NCgl1222 Acetolactate synthase large-chain ilvB ( C. glutamicum ) ilvB 0.8 3.1 3.6 2793 NCgl1222 Acetolactate synthase large-chain ilvB ( C. glutamicum ) ilvB 0.4 1.5 4.1 2793 NCgl1222 Acetolactate synthase large-chain ilvB ( C. glutamicum ) ilvB 0.2 0.7 4.2 2793 NCgl1222 Acetolactate synthase large-chain ilvB ( C. glutamicum ) ilvB 0.5 2.4 5.1 2793 NCgl1222 Acetolactate synthase large-chain ilvB ( C. glutamicum ) ilvB 0.6 3.4 5.3 2793 NCgl1222 Acetolactate synthase large-chain ilvB ( C. glutamicum ) ilvB 0.2 1.0 5.9 2793 NCgl1222 Acetolactate synthase large-chain ilvB ( C. glutamicum ) ilvB 0.2 1.6 7.2 Open in a separate window a Abbreviations, conditions, and statistical analysis are described in footnotes to Table . b +Val, growth under addition of 40 mM l -valine.

Techniques:

Upper panels show In vivo MRI examinations of endothelial function in the femoral artery (A) and thoracic aorta (B) in response to acetylcholine (ACh, 16.6 mg/kg i.p.) administered to female wildtype (WT, open symbols, n = 6 for the femoral artery and n = 4 for the thoracic aorta) and GPR18 knockout (KO, green symbols, n = 5 for the femoral artery and n = 44 for the thoracic aorta) mice. The unaltered endothelium‐independent responses to infusion of the NO‐donor to sodium nitroprusside (SNP, 1 mg/kg i.v.; WT: N = 5 for the femoral artery and n = 3 for the thoracic aorta; KO: N = 5 for the femoral artery and n = 4 for the thoracic aorta) are shown as insets. Results are shown as changes in vessel volume. The horizontal line represents the mean. p ‐value from Student's t‐test vs. WT. (C) Ex vivo analysis of endothelium‐dependent relaxations in response to ACh administered to 10 μM PE‐precontracted arterial rings of the femoral artery derived from female mice (WT, n = 7; KO, n = 9) in the presence of 10 μM indomethacin. Inset shows endothelial‐independent relaxations in response to DEANO measured in 10 μM PE‐precontracted arterial rings of the femoral artery (WT, n = 8; KO, n = 8), in the presence of 10 μM indomethacin and 300 μM L‐NAME, to inhibit any possible confounding effects of endogenous NOS or COX activity, respectively. The overall P of significant two‐way ANOVA comparison of KO vs. WT is indicated in each concentration‐response graph. * p < 0.05 (Holm‐Sidak post hoc test vs. WT). (D) Representative images and analysis of immunofluorescent staining for endothelial nitric oxide synthase (eNOS) in femoral arteries derived from female GPR18 KO (green circles, n = 3) compared with female WT mice (open circles, n = 4). The horizontal line represents the mean; P‐value from Student's t‐test vs. WT. The micrographs show representative immunofluorescence stainings. Size bar represents 50 μm. (E) Concentration‐response relaxations to acetylcholine (ACh) in the absence (circles; WT, n = 7; KO, n = 10) and presence (squares; WT, n = 7; KO, n = 9) of 10 μM indomethacin in 10 μM PE‐precontracted isolated femoral arteries derived from female WT (left panel with open symbols) and GPR18 KO (left panel with green symbols). The overall p of two‐way ANOVA comparison of KO vs. WT is indicated in each concentration‐response graph. * p < 0.05 (Holm‐Sidak post hoc test vs. WT).

Journal: The FASEB Journal

Article Title: Vascular Bed‐Specific Endothelial Dysfunction and Age‐Dependent Circadian Hypertension in Mice Lacking the Resolvin D2 Receptor GPR18

doi: 10.1096/fj.202503386R

Figure Lengend Snippet: Upper panels show In vivo MRI examinations of endothelial function in the femoral artery (A) and thoracic aorta (B) in response to acetylcholine (ACh, 16.6 mg/kg i.p.) administered to female wildtype (WT, open symbols, n = 6 for the femoral artery and n = 4 for the thoracic aorta) and GPR18 knockout (KO, green symbols, n = 5 for the femoral artery and n = 44 for the thoracic aorta) mice. The unaltered endothelium‐independent responses to infusion of the NO‐donor to sodium nitroprusside (SNP, 1 mg/kg i.v.; WT: N = 5 for the femoral artery and n = 3 for the thoracic aorta; KO: N = 5 for the femoral artery and n = 4 for the thoracic aorta) are shown as insets. Results are shown as changes in vessel volume. The horizontal line represents the mean. p ‐value from Student's t‐test vs. WT. (C) Ex vivo analysis of endothelium‐dependent relaxations in response to ACh administered to 10 μM PE‐precontracted arterial rings of the femoral artery derived from female mice (WT, n = 7; KO, n = 9) in the presence of 10 μM indomethacin. Inset shows endothelial‐independent relaxations in response to DEANO measured in 10 μM PE‐precontracted arterial rings of the femoral artery (WT, n = 8; KO, n = 8), in the presence of 10 μM indomethacin and 300 μM L‐NAME, to inhibit any possible confounding effects of endogenous NOS or COX activity, respectively. The overall P of significant two‐way ANOVA comparison of KO vs. WT is indicated in each concentration‐response graph. * p < 0.05 (Holm‐Sidak post hoc test vs. WT). (D) Representative images and analysis of immunofluorescent staining for endothelial nitric oxide synthase (eNOS) in femoral arteries derived from female GPR18 KO (green circles, n = 3) compared with female WT mice (open circles, n = 4). The horizontal line represents the mean; P‐value from Student's t‐test vs. WT. The micrographs show representative immunofluorescence stainings. Size bar represents 50 μm. (E) Concentration‐response relaxations to acetylcholine (ACh) in the absence (circles; WT, n = 7; KO, n = 10) and presence (squares; WT, n = 7; KO, n = 9) of 10 μM indomethacin in 10 μM PE‐precontracted isolated femoral arteries derived from female WT (left panel with open symbols) and GPR18 KO (left panel with green symbols). The overall p of two‐way ANOVA comparison of KO vs. WT is indicated in each concentration‐response graph. * p < 0.05 (Holm‐Sidak post hoc test vs. WT).

Article Snippet: The breeding and experimental protocols in GPR18 KO (MGI:107859; NCBI ID: 110168; C57BL/6J‐Gpr18 em1 cyagen) mice and WT littermates were approved by the local ethics committee and the Ministry of National Education, Higher Education, and Research and Innovation in France (APAFIS#22187‐2 019 093 011 424 973 v5).

Techniques: In Vivo, Knock-Out, Ex Vivo, Derivative Assay, Activity Assay, Comparison, Concentration Assay, Staining, Immunofluorescence, Isolation

Telemetry mean arterial blood pressures (MAP) in young (A–C) and old (D) WT (open symbols) and GPR18 KO (green symbols) mice. Each datapoint represents the MAP recorded during 1 h for all mice of each group during 3 days and nights. (A, B): The comparison between males (WT, n = 3; KO, n = 3) and females (WT, n = 4; KO, n = 3) in sex‐disaggregated analysis did not reveal any significant sex differences in either WT or GPR18 KO young mice. (C): In the sex aggregated analysis, with young KO ( n = 7; n = 3 males [4.64 ± 0.51 months] and n = 4 females [4.13 ± 0.19 months]) did not exhibit any significant differences compared with young WT ( n = 7; n = 3 males [4.49 ± 0.45 months] and n = 4 females [4.13 ± 0.08 months]) during either day or night. (D): Old KO ( n = 4 [3 females and 1 male; 20.7 ± 0.63 months]) exhibited a significantly increased MAP during daytime and a moderate increase during active night‐time compared with old WT mice ( n = 4 [2 females and 2 males; 21.3 ± 0.48 months]).

Journal: The FASEB Journal

Article Title: Vascular Bed‐Specific Endothelial Dysfunction and Age‐Dependent Circadian Hypertension in Mice Lacking the Resolvin D2 Receptor GPR18

doi: 10.1096/fj.202503386R

Figure Lengend Snippet: Telemetry mean arterial blood pressures (MAP) in young (A–C) and old (D) WT (open symbols) and GPR18 KO (green symbols) mice. Each datapoint represents the MAP recorded during 1 h for all mice of each group during 3 days and nights. (A, B): The comparison between males (WT, n = 3; KO, n = 3) and females (WT, n = 4; KO, n = 3) in sex‐disaggregated analysis did not reveal any significant sex differences in either WT or GPR18 KO young mice. (C): In the sex aggregated analysis, with young KO ( n = 7; n = 3 males [4.64 ± 0.51 months] and n = 4 females [4.13 ± 0.19 months]) did not exhibit any significant differences compared with young WT ( n = 7; n = 3 males [4.49 ± 0.45 months] and n = 4 females [4.13 ± 0.08 months]) during either day or night. (D): Old KO ( n = 4 [3 females and 1 male; 20.7 ± 0.63 months]) exhibited a significantly increased MAP during daytime and a moderate increase during active night‐time compared with old WT mice ( n = 4 [2 females and 2 males; 21.3 ± 0.48 months]).

Article Snippet: The breeding and experimental protocols in GPR18 KO (MGI:107859; NCBI ID: 110168; C57BL/6J‐Gpr18 em1 cyagen) mice and WT littermates were approved by the local ethics committee and the Ministry of National Education, Higher Education, and Research and Innovation in France (APAFIS#22187‐2 019 093 011 424 973 v5).

Techniques: Comparison

Validation of the proteomic results by western blotting and immunohistochemistry. ( A ) Differential expression of selected proteins as detected by mass spectrometry. ( B , C ) Expression of upregulated proteins by western blot (B) and quantification of protein levels normalized to ACTIN content (C). ( D , E ) Expression of downregulated proteins by western blot (D) and quantification of protein levels normalized to ACTIN content (E). ( F , G ) Representative images of human ovarian cortical sections stained with SERPIN G1 (F) and NCBP2 (G). ( H , I ) Quantification of the percentage of SERPIN G1-positive area and NCBP2-positive nuclei. ( J ) Negative control for the immunostaining. Data are expressed as mean ± SD or scatter plots ± SD; N = 5 per experimental group. * P < 0.05; ** P < 0.01; *** P < 0.001; ns: not significant. ECM, extracellular matrix.

Journal: Human Reproduction (Oxford, England)

Article Title: Proteomic profiling reveals the molecular signatures of chemotherapy-induced human ovarian damage

doi: 10.1093/humrep/deaf203

Figure Lengend Snippet: Validation of the proteomic results by western blotting and immunohistochemistry. ( A ) Differential expression of selected proteins as detected by mass spectrometry. ( B , C ) Expression of upregulated proteins by western blot (B) and quantification of protein levels normalized to ACTIN content (C). ( D , E ) Expression of downregulated proteins by western blot (D) and quantification of protein levels normalized to ACTIN content (E). ( F , G ) Representative images of human ovarian cortical sections stained with SERPIN G1 (F) and NCBP2 (G). ( H , I ) Quantification of the percentage of SERPIN G1-positive area and NCBP2-positive nuclei. ( J ) Negative control for the immunostaining. Data are expressed as mean ± SD or scatter plots ± SD; N = 5 per experimental group. * P < 0.05; ** P < 0.01; *** P < 0.001; ns: not significant. ECM, extracellular matrix.

Article Snippet: Non-specific binding sites were blocked using 5% v/v normal goat serum then the slides were incubated with SERPIN G1 (12259-1-AP, Proteintech, 1:1000), NCBP2 (11950-1-AP, Proteintech, 1:3000), 8-OHdG (SAB5200010, Merck, 1:500), Ki67 (556003, BD Biosciences, 1:400) or γH2Ax (05-636, Merck, 1:100) antibodies overnight at 4 °C.

Techniques: Biomarker Discovery, Western Blot, Immunohistochemistry, Quantitative Proteomics, Mass Spectrometry, Expressing, Staining, Negative Control, Immunostaining