Results 281 to 290 of about 165,231 (306)
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Extension of the Binding Motif of the Sin3 Interacting Domain of the Mad Family Proteins,
Biochemistry, 2003Sin3 forms the scaffold for a multiprotein corepressor complex that silences transcription via the action of histone deacetylases. Sin3 is recruited to the DNA by several DNA binding repressors, such as the helix-loop-helix proteins of the Mad family.
van Ingen H +6 more
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Biochemistry, 2015
Hepatoma-derived growth factor (hHDGF) and HDGF-related proteins (HRPs) contain conserved N-terminal HATH domains with a characteristic structural motif, namely the PWWP motif. The HATH domain has attracted attention because of its ability to bind with heparin/heparan sulfate, DNA, and methylated histone peptide.
Yi-Lin, Hung +6 more
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Hepatoma-derived growth factor (hHDGF) and HDGF-related proteins (HRPs) contain conserved N-terminal HATH domains with a characteristic structural motif, namely the PWWP motif. The HATH domain has attracted attention because of its ability to bind with heparin/heparan sulfate, DNA, and methylated histone peptide.
Yi-Lin, Hung +6 more
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Trends in Biochemical Sciences, 2003
Parkin and other unrelated proteins contain a ubiquitin-like domain (UbLD). This article describes a motif that might be important in the interaction of UbLD-containing proteins (UbLPs) with the proteasome. The proteasome-interacting motif, which is conserved in a subset of UbLPs, such as parkin, Rad23 and several transcription factors, is likely to ...
Sudarshan C, Upadhya, Ashok N, Hegde
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Parkin and other unrelated proteins contain a ubiquitin-like domain (UbLD). This article describes a motif that might be important in the interaction of UbLD-containing proteins (UbLPs) with the proteasome. The proteasome-interacting motif, which is conserved in a subset of UbLPs, such as parkin, Rad23 and several transcription factors, is likely to ...
Sudarshan C, Upadhya, Ashok N, Hegde
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The FASEB Journal, 2000
ABSTRACT A common focus among molecular and cellular biologists is the identification of proteins that interact with each other. Yeast two‐hybrid, cDNA expression library screening, and coimmunoprecipitation experiments are powerful methods for identifying novel proteins that bind to one's favorite protein for the
Brian K. Kay +2 more
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ABSTRACT A common focus among molecular and cellular biologists is the identification of proteins that interact with each other. Yeast two‐hybrid, cDNA expression library screening, and coimmunoprecipitation experiments are powerful methods for identifying novel proteins that bind to one's favorite protein for the
Brian K. Kay +2 more
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Biochimica et Biophysica Acta (BBA) - General Subjects, 2019
Sterols have been reported to modulate conformation and hence the function of several membrane proteins. One such group is the Chloride Intracellular Ion Channel (CLIC) family of proteins. The CLIC protein family consists of six evolutionarily conserved protein members in vertebrates.
Khondker Rufaka, Hossain +7 more
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Sterols have been reported to modulate conformation and hence the function of several membrane proteins. One such group is the Chloride Intracellular Ion Channel (CLIC) family of proteins. The CLIC protein family consists of six evolutionarily conserved protein members in vertebrates.
Khondker Rufaka, Hossain +7 more
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Cell growth & differentiation : the molecular biology journal of the American Association for Cancer Research, 1996
The BTB/POZ domain defines a newly characterized protein-protein interaction interface. It is highly conserved throughout metazoan evolution and generally found at the NH2 terminus of either actin-binding or, more commonly, nuclear DNA-binding proteins. By mediating protein binding in large aggregates, the BTB/POZ domain serves to organize higher order
O, Albagli +4 more
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The BTB/POZ domain defines a newly characterized protein-protein interaction interface. It is highly conserved throughout metazoan evolution and generally found at the NH2 terminus of either actin-binding or, more commonly, nuclear DNA-binding proteins. By mediating protein binding in large aggregates, the BTB/POZ domain serves to organize higher order
O, Albagli +4 more
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2009
Nonribosomal peptide synthetases (NRPS) are modular proteins that catalyze the synthesis of small peptides with antibiotic, immunosuppressant, and anticancer activities, as well as siderophores. NRPS usually contain one module for each amino acid incorporated into the final peptide.
Šprung, Matilda +4 more
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Nonribosomal peptide synthetases (NRPS) are modular proteins that catalyze the synthesis of small peptides with antibiotic, immunosuppressant, and anticancer activities, as well as siderophores. NRPS usually contain one module for each amino acid incorporated into the final peptide.
Šprung, Matilda +4 more
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2009
Uloga očuvanih motiva adenilacijske domene peptid sintetaza te njihov relativni položaj u prostornoj strukturi. Utjecaj istih na prepoznavanje proteinskih partnera tijekom katalize.
Bučević Popović, Viljemka +3 more
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Uloga očuvanih motiva adenilacijske domene peptid sintetaza te njihov relativni položaj u prostornoj strukturi. Utjecaj istih na prepoznavanje proteinskih partnera tijekom katalize.
Bučević Popović, Viljemka +3 more
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Understanding Protein-Protein Interactions: From Domain Level to Motif Level
2007Huan Yu, Minping Qian, Minghua Deng
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