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Author Details
Full Name
Hector Viadiu
Affiliation
All India Institute of Medical Sciences
ORCID
Career Start Year
1995
Papers
24
H Index
15
Expertise
CM4AI Collaborator
PMID
Paper Title
Journal Title
Published Year
35217090
Deciphering the mechanism of p73 recognition of p53 response elements using the crystal structure of p73-DNA complexes and computational studies.
Int J Biol Macromol
2022
35217090
Deciphering the mechanism of p73 recognition of p53 response elements using the crystal structure of p73-DNA complexes and computational studies.
Int J Biol Macromol
2022
30023688
Spiked Genes: A Method to Introduce Random Point Nucleotide Mutations Evenly throughout an Entire Gene Using a Complete Set of Spiked Oligonucleotides for the Assembly.
ACS Omega
2017
30023688
Spiked Genes: A Method to Introduce Random Point Nucleotide Mutations Evenly throughout an Entire Gene Using a Complete Set of Spiked Oligonucleotides for the Assembly.
ACS Omega
2017
27132513
TNF-α modulates genome-wide redistribution of οNp63α/TAp73 and NF-κB cREL interactive binding on TP53 and AP-1 motifs to promote an oncogenic gene program in squamous cancer.
Oncogene
2016
27132513
TNF-α modulates genome-wide redistribution of οNp63α/TAp73 and NF-κB cREL interactive binding on TP53 and AP-1 motifs to promote an oncogenic gene program in squamous cancer.
Oncogene
2016
26529454
Sequence Variation in the Response Element Determines Binding by the Transcription Factor p73.
Biochemistry
2015
26529454
Sequence Variation in the Response Element Determines Binding by the Transcription Factor p73.
Biochemistry
2015
25201192
Structural studies on mechanisms to activate mutant p53.
Subcell Biochem
2014
25201192
Structural studies on mechanisms to activate mutant p53.
Subcell Biochem
2014
23243311
Crystal structures of the DNA-binding domain tetramer of the p53 tumor suppressor family member p73 bound to different full-site response elements.
J Biol Chem
2013
23892287
Transactivation specificity is conserved among p53 family proteins and depends on a response element sequence code.
Nucleic Acids Res
2013
23463580
EEC- and ADULT-associated TP63 mutations exhibit functional heterogeneity toward P63 responsive sequences.
Hum Mutat
2013
23243311
Crystal structures of the DNA-binding domain tetramer of the p53 tumor suppressor family member p73 bound to different full-site response elements.
J Biol Chem
2013
23892287
Transactivation specificity is conserved among p53 family proteins and depends on a response element sequence code.
Nucleic Acids Res
2013
23463580
EEC- and ADULT-associated TP63 mutations exhibit functional heterogeneity toward P63 responsive sequences.
Hum Mutat
2013
22474346
Structure of p73 DNA-binding domain tetramer modulates p73 transactivation.
Proc Natl Acad Sci U S A
2012
22474346
Structure of p73 DNA-binding domain tetramer modulates p73 transactivation.
Proc Natl Acad Sci U S A
2012
23025236
The tetramer of p53 in the absence of DNA forms a relaxed quaternary state.
Biochemistry
2012
23025236
The tetramer of p53 in the absence of DNA forms a relaxed quaternary state.
Biochemistry
2012
20833632
Asymmetric DNA recognition by the OkrAI endonuclease, an isoschizomer of BamHI.
Nucleic Acids Res
2011
20833632
Asymmetric DNA recognition by the OkrAI endonuclease, an isoschizomer of BamHI.
Nucleic Acids Res
2011
21936505
Nanodiscs versus macrodiscs for NMR of membrane proteins.
Biochemistry
2011
21936505
Nanodiscs versus macrodiscs for NMR of membrane proteins.
Biochemistry
2011
18991721
Molecular architecture of tumor suppressor p53.
Curr Top Med Chem
2008
18991721
Molecular architecture of tumor suppressor p53.
Curr Top Med Chem
2008
17239399
Projection map of aquaporin-9 at 7 A resolution.
J Mol Biol
2007
17239399
Projection map of aquaporin-9 at 7 A resolution.
J Mol Biol
2007
15880121
Domain structure of separase and its binding to securin as determined by EM.
Nat Struct Mol Biol
2005
15880121
Domain structure of separase and its binding to securin as determined by EM.
Nat Struct Mol Biol
2005
16308566
A view of consecutive binding events from structures of tetrameric endonuclease SfiI bound to DNA.
EMBO J
2005
16308566
A view of consecutive binding events from structures of tetrameric endonuclease SfiI bound to DNA.
EMBO J
2005
12719261
Energetic and structural considerations for the mechanism of protein sliding along DNA in the nonspecific BamHI-DNA complex.
Biophys J
2003
12719261
Energetic and structural considerations for the mechanism of protein sliding along DNA in the nonspecific BamHI-DNA complex.
Biophys J
2003
12876363
Crystallization of restriction endonuclease SfiI in complex with DNA.
Acta Crystallogr D Biol Crystallogr
2003
12876363
Crystallization of restriction endonuclease SfiI in complex with DNA.
Acta Crystallogr D Biol Crystallogr
2003
10806094
Crystallization of restriction endonuclease BamHI with nonspecific DNA.
J Struct Biol
2000
10882125
Structure of BamHI bound to nonspecific DNA: a model for DNA sliding.
Mol Cell
2000
11073444
Allosteric effects of Pit-1 DNA sites on long-term repression in cell type specification.
Science
2000
10806094
Crystallization of restriction endonuclease BamHI with nonspecific DNA.
J Struct Biol
2000
10882125
Structure of BamHI bound to nonspecific DNA: a model for DNA sliding.
Mol Cell
2000
11073444
Allosteric effects of Pit-1 DNA sites on long-term repression in cell type specification.
Science
2000
9783752
The role of metals in catalysis by the restriction endonuclease BamHI.
Nat Struct Biol
1998
9783752
The role of metals in catalysis by the restriction endonuclease BamHI.
Nat Struct Biol
1998
7822310
Substitution of Asp for Asn at position 132 in the active site of TEM beta-lactamase. Activity toward different substrates and effects of neighboring residues.
J Biol Chem
1995
7822311
A new TEM beta-lactamase double mutant with broadened specificity reveals substrate-dependent functional interactions.
J Biol Chem
1995
7822310
Substitution of Asp for Asn at position 132 in the active site of TEM beta-lactamase. Activity toward different substrates and effects of neighboring residues.
J Biol Chem
1995
7822311
A new TEM beta-lactamase double mutant with broadened specificity reveals substrate-dependent functional interactions.
J Biol Chem
1995
1 - 48 of 48
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Center for Cancer Research, National Cancer Institute
Co-authored papers
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University of California San Francisco
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National Institute on Deafness and Other Communication Disorders
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The Fifth Affiliated Hospital, Sun Yat-sen University
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0 SW US Veterans Hospital Road
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State University of New York at Buffalo
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Center for Cancer Research, National Cancer Institute, National Institutes of Health
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University of Illinois at Urbana-Champaign
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University of California at Santa Cruz
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Human Phenome Institute and Shanghai Cancer Center, Fudan University
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Clinical Immunology Section, National Eye Institute
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University of California San Diego
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