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Medicago c2h2 type zinc finger protein
C2h2 Type Zinc Finger Protein, supplied by Medicago, 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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C2h2 Zinc Finger Transcription Factors, supplied by InterPro 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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C2h2 Zinc Finger Transcription Factor Palm1, supplied by Medicago, 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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C2h2 Type Zinc Finger Domain, supplied by InterPro 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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C2h2 Zinc Finger Domain Ipr013087, supplied by InterPro 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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Medicago c2h2 zinc finger gene family
Fig. 1. Three-dimensional structure of a typical <t>C2H2-type</t> zinc finger protein. (A) Protein sequence alignment of the 3-D structure composed of H1–H6 helix strands and beta sheets. (B) Normal representation of the 3-D structure showing five Zn metal ions. (C) Example of C2H2-type zinc finger proteins interacting with Zn metal ions. The amino acids on (C) are the catalytic sites (two HIS507, HIS511 and CYS491, CYS4940) of the protein.
C2h2 Zinc Finger Gene Family, supplied by Medicago, 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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InterPro Inc c2h2 zinc finger domains
Predicted protein consequence of germline and somatic ZFX missense variants in the present work and related studies, and regional missense constraint analysis. A, Schematic of protein domain structure of ZFX transcription factor (Uniprot P17010) (not to scale). N-terminal Zfx/Zfy transcriptional activator domain (InterPro <t>IPR006794)</t> encompasses residues 70 to 410, shown in blue (not to scale). Individual <t>C2H2</t> zinc finger domains (InterPro IPR006794), 13 in total, shown in yellow. ZFX residues 747 to 775 comprise zinc finger 12, and residues 776 to 803 comprise zinc finger 13. Individual residues shown in red font altered by germline and/or somatic ZFX missense variants indicated below by black arrows (3, 4) (see also Table 2). B, GnomAD v2.1.1 regional missense constraint analysis with legend indicating color coding of missense observed/expected (o/e) ratio from 0.0 to 1.0+ (from gnomAD browser [Broad Institute]). Gray (ZFX residues Met1 to Val161), o/e ratio 0.9261, P value = not significant; orange (ZFX residues Val161 to Ser 646), o/e ratio 0.4850, P value = 1.000e-12; dark red (ZFX residues Ser646 to Pro805 includes the C-terminal portion of zinc finger 8 (residues 633-661) through the C-terminus of ZFX), o/e ratio 0.1561, P value = 1.435e-11.
C2h2 Zinc Finger Domains, supplied by InterPro 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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Garton Inc c2h2 zinc finger proteins
Predicted protein consequence of germline and somatic ZFX missense variants in the present work and related studies, and regional missense constraint analysis. A, Schematic of protein domain structure of ZFX transcription factor (Uniprot P17010) (not to scale). N-terminal Zfx/Zfy transcriptional activator domain (InterPro <t>IPR006794)</t> encompasses residues 70 to 410, shown in blue (not to scale). Individual <t>C2H2</t> zinc finger domains (InterPro IPR006794), 13 in total, shown in yellow. ZFX residues 747 to 775 comprise zinc finger 12, and residues 776 to 803 comprise zinc finger 13. Individual residues shown in red font altered by germline and/or somatic ZFX missense variants indicated below by black arrows (3, 4) (see also Table 2). B, GnomAD v2.1.1 regional missense constraint analysis with legend indicating color coding of missense observed/expected (o/e) ratio from 0.0 to 1.0+ (from gnomAD browser [Broad Institute]). Gray (ZFX residues Met1 to Val161), o/e ratio 0.9261, P value = not significant; orange (ZFX residues Val161 to Ser 646), o/e ratio 0.4850, P value = 1.000e-12; dark red (ZFX residues Ser646 to Pro805 includes the C-terminal portion of zinc finger 8 (residues 633-661) through the C-terminus of ZFX), o/e ratio 0.1561, P value = 1.435e-11.
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InterPro Inc c2h2-type zinc finger dna-binding domain ipr007087
Predicted protein consequence of germline and somatic ZFX missense variants in the present work and related studies, and regional missense constraint analysis. A, Schematic of protein domain structure of ZFX transcription factor (Uniprot P17010) (not to scale). N-terminal Zfx/Zfy transcriptional activator domain (InterPro <t>IPR006794)</t> encompasses residues 70 to 410, shown in blue (not to scale). Individual <t>C2H2</t> zinc finger domains (InterPro IPR006794), 13 in total, shown in yellow. ZFX residues 747 to 775 comprise zinc finger 12, and residues 776 to 803 comprise zinc finger 13. Individual residues shown in red font altered by germline and/or somatic ZFX missense variants indicated below by black arrows (3, 4) (see also Table 2). B, GnomAD v2.1.1 regional missense constraint analysis with legend indicating color coding of missense observed/expected (o/e) ratio from 0.0 to 1.0+ (from gnomAD browser [Broad Institute]). Gray (ZFX residues Met1 to Val161), o/e ratio 0.9261, P value = not significant; orange (ZFX residues Val161 to Ser 646), o/e ratio 0.4850, P value = 1.000e-12; dark red (ZFX residues Ser646 to Pro805 includes the C-terminal portion of zinc finger 8 (residues 633-661) through the C-terminus of ZFX), o/e ratio 0.1561, P value = 1.435e-11.
C2h2 Type Zinc Finger Dna Binding Domain Ipr007087, supplied by InterPro 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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Fig. 1. Three-dimensional structure of a typical C2H2-type zinc finger protein. (A) Protein sequence alignment of the 3-D structure composed of H1–H6 helix strands and beta sheets. (B) Normal representation of the 3-D structure showing five Zn metal ions. (C) Example of C2H2-type zinc finger proteins interacting with Zn metal ions. The amino acids on (C) are the catalytic sites (two HIS507, HIS511 and CYS491, CYS4940) of the protein.

Journal: Journal of experimental botany

Article Title: Recent advances in the multifaceted functions of Cys2/His2-type zinc finger proteins in plant growth, development, and stress responses.

doi: 10.1093/jxb/erae278

Figure Lengend Snippet: Fig. 1. Three-dimensional structure of a typical C2H2-type zinc finger protein. (A) Protein sequence alignment of the 3-D structure composed of H1–H6 helix strands and beta sheets. (B) Normal representation of the 3-D structure showing five Zn metal ions. (C) Example of C2H2-type zinc finger proteins interacting with Zn metal ions. The amino acids on (C) are the catalytic sites (two HIS507, HIS511 and CYS491, CYS4940) of the protein.

Article Snippet: Genome-wide study of C2H2 zinc finger gene family in Medicago truncatula.

Techniques: Sequencing

Fig. 2. Classification of C2H2-type zinc finger proteins into subgroups in Arabidopsis. The image was created using Figdraw (https://www.figdraw. com).

Journal: Journal of experimental botany

Article Title: Recent advances in the multifaceted functions of Cys2/His2-type zinc finger proteins in plant growth, development, and stress responses.

doi: 10.1093/jxb/erae278

Figure Lengend Snippet: Fig. 2. Classification of C2H2-type zinc finger proteins into subgroups in Arabidopsis. The image was created using Figdraw (https://www.figdraw. com).

Article Snippet: Genome-wide study of C2H2 zinc finger gene family in Medicago truncatula.

Techniques:

Fig. 3. The regulatory network of C2H2-type zinc finger proteins in responses to abiotic stresses. ABA, abscisic acid; APX, ascorbate peroxidase; AsA, ascorbic acid; CAT, catalase; GA, gibberellin; JA, jasmonic acid; MAPK, mitogen-activated protein kinase; MDA, malondialdehyde; POD, peroxidase; ROS, reactive oxygen species; SA, salicylic acid; SOD, superoxide dismutase.

Journal: Journal of experimental botany

Article Title: Recent advances in the multifaceted functions of Cys2/His2-type zinc finger proteins in plant growth, development, and stress responses.

doi: 10.1093/jxb/erae278

Figure Lengend Snippet: Fig. 3. The regulatory network of C2H2-type zinc finger proteins in responses to abiotic stresses. ABA, abscisic acid; APX, ascorbate peroxidase; AsA, ascorbic acid; CAT, catalase; GA, gibberellin; JA, jasmonic acid; MAPK, mitogen-activated protein kinase; MDA, malondialdehyde; POD, peroxidase; ROS, reactive oxygen species; SA, salicylic acid; SOD, superoxide dismutase.

Article Snippet: Genome-wide study of C2H2 zinc finger gene family in Medicago truncatula.

Techniques:

Fig. 4. The regulatory network of C2H2 zinc finger proteins in response to biotic stress. ABA, abscisic acid; ETI, effector-triggered immunity; H2O2, hydrogen peroxide; HR, hypersensitive response; JA, jasmonic acid; PTI, (pathogen-associated molecular pattern-triggered immunity; SA, salicylic acid.

Journal: Journal of experimental botany

Article Title: Recent advances in the multifaceted functions of Cys2/His2-type zinc finger proteins in plant growth, development, and stress responses.

doi: 10.1093/jxb/erae278

Figure Lengend Snippet: Fig. 4. The regulatory network of C2H2 zinc finger proteins in response to biotic stress. ABA, abscisic acid; ETI, effector-triggered immunity; H2O2, hydrogen peroxide; HR, hypersensitive response; JA, jasmonic acid; PTI, (pathogen-associated molecular pattern-triggered immunity; SA, salicylic acid.

Article Snippet: Genome-wide study of C2H2 zinc finger gene family in Medicago truncatula.

Techniques:

Fig. 5. The regulatory network of C2H2 zinc finger proteins in response to plant growth and development. ABA, abscisic acid; CK, cytokinin; GA, gibberellin; JA, jasmonic acid.

Journal: Journal of experimental botany

Article Title: Recent advances in the multifaceted functions of Cys2/His2-type zinc finger proteins in plant growth, development, and stress responses.

doi: 10.1093/jxb/erae278

Figure Lengend Snippet: Fig. 5. The regulatory network of C2H2 zinc finger proteins in response to plant growth and development. ABA, abscisic acid; CK, cytokinin; GA, gibberellin; JA, jasmonic acid.

Article Snippet: Genome-wide study of C2H2 zinc finger gene family in Medicago truncatula.

Techniques:

Predicted protein consequence of germline and somatic ZFX missense variants in the present work and related studies, and regional missense constraint analysis. A, Schematic of protein domain structure of ZFX transcription factor (Uniprot P17010) (not to scale). N-terminal Zfx/Zfy transcriptional activator domain (InterPro IPR006794) encompasses residues 70 to 410, shown in blue (not to scale). Individual C2H2 zinc finger domains (InterPro IPR006794), 13 in total, shown in yellow. ZFX residues 747 to 775 comprise zinc finger 12, and residues 776 to 803 comprise zinc finger 13. Individual residues shown in red font altered by germline and/or somatic ZFX missense variants indicated below by black arrows (3, 4) (see also Table 2). B, GnomAD v2.1.1 regional missense constraint analysis with legend indicating color coding of missense observed/expected (o/e) ratio from 0.0 to 1.0+ (from gnomAD browser [Broad Institute]). Gray (ZFX residues Met1 to Val161), o/e ratio 0.9261, P value = not significant; orange (ZFX residues Val161 to Ser 646), o/e ratio 0.4850, P value = 1.000e-12; dark red (ZFX residues Ser646 to Pro805 includes the C-terminal portion of zinc finger 8 (residues 633-661) through the C-terminus of ZFX), o/e ratio 0.1561, P value = 1.435e-11.

Journal: JCEM Case Reports

Article Title: A Germline ZFX Missense Variant in a Patient With Primary Hyperparathyroidism

doi: 10.1210/jcemcr/luae115

Figure Lengend Snippet: Predicted protein consequence of germline and somatic ZFX missense variants in the present work and related studies, and regional missense constraint analysis. A, Schematic of protein domain structure of ZFX transcription factor (Uniprot P17010) (not to scale). N-terminal Zfx/Zfy transcriptional activator domain (InterPro IPR006794) encompasses residues 70 to 410, shown in blue (not to scale). Individual C2H2 zinc finger domains (InterPro IPR006794), 13 in total, shown in yellow. ZFX residues 747 to 775 comprise zinc finger 12, and residues 776 to 803 comprise zinc finger 13. Individual residues shown in red font altered by germline and/or somatic ZFX missense variants indicated below by black arrows (3, 4) (see also Table 2). B, GnomAD v2.1.1 regional missense constraint analysis with legend indicating color coding of missense observed/expected (o/e) ratio from 0.0 to 1.0+ (from gnomAD browser [Broad Institute]). Gray (ZFX residues Met1 to Val161), o/e ratio 0.9261, P value = not significant; orange (ZFX residues Val161 to Ser 646), o/e ratio 0.4850, P value = 1.000e-12; dark red (ZFX residues Ser646 to Pro805 includes the C-terminal portion of zinc finger 8 (residues 633-661) through the C-terminus of ZFX), o/e ratio 0.1561, P value = 1.435e-11.

Article Snippet: Individual C2H2 zinc finger domains (InterPro IPR006794), 13 in total, shown in yellow.

Techniques: