Search Results - "Srivastava, Shanti Swaroop"

Interface interactions between βγ‐crystallin domain and Ig‐like domain render Ca2+‐binding site inoperative in abundant perithecial protein of Neurospora crassa by Swaroop Srivastava, Shanti, Raman, Rajeev, Kiran, Uday, Garg, Rupsi, Chadalawada, Swathi, Pawar, Asmita D., Sankaranarayanan, Rajan, Sharma, Yogendra

“…Summary We describe a set of proteins in which a βγ‐crystallin domain pairs with an Ig‐like domain, and which are confined to microbes, like bacteria, slime…”
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Plasmodium vivax and human hexokinases share similar active sites but display distinct quaternary architectures by Srivastava, Shanti Swaroop, Darling, Joseph E, Suryadi, Jimmy, Morris, James C, Drew, Mark E, Subramaniam, Sriram

“…Malaria is a devastating disease caused by a protozoan parasite. It affects over 300 million individuals and results in over 400 000 deaths annually, most of…”
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Cryo-EM research in India by Shukla, Arun K, Banerjee, Manidipa, Singh, Appu K, Penmatsa, Aravind, Dutta, Somnath, Anand, Ruchi, Sirajuddin, Minhajuddin, Srivastava, Shanti Swaroop

“…To celebrate the 50th anniversary of Cell Press and the Cell special issue focusing on structural biology, we want to highlight the rapid progress of cryo-EM…”
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βγ-Crystallination Endows a Novel Bacterial Glycoside Hydrolase 64 with Ca2+-Dependent Activity Modulation by Krishnan, Bal, Srivastava, Shanti Swaroop, Sankeshi, Venu, Garg, Rupsi, Srivastava, Sudhakar, Sankaranarayanan, Rajan, Sharma, Yogendra

“…The prokaryotic βγ-crystallins are a large group of uncharacterized domains with Ca2+-binding motifs. We have observed that a vast number of these domains are…”
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βγ-Crystallination Endows a Novel Bacterial Glycoside Hydrolase 64 with Ca 2+ -Dependent Activity Modulation by Krishnan, Bal, Srivastava, Shanti Swaroop, Sankeshi, Venu, Garg, Rupsi, Srivastava, Sudhakar, Sankaranarayanan, Rajan, Sharma, Yogendra

“…The prokaryotic βγ-crystallins are a large group of uncharacterized domains with Ca -binding motifs. We have observed that a vast number of these domains are…”
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Microbial βγ-crystallins by Mishra, Amita, Krishnan, Bal, Srivastava, Shanti Swaroop, Sharma, Yogendra

“…βγ-Crystallins have emerged as a superfamily of structurally homologous proteins with representatives across the domains of life. A major portion of this…”
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Microbial beta gamma -crystallins by Mishra, Amita, Krishnan, Bal, Srivastava, Shanti Swaroop, Sharma, Yogendra

“…beta gamma -Crystallins have emerged as a superfamily of structurally homologous proteins with representatives across the domains of life. A major portion of…”
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A Transition Metal-Binding, Trimeric beta gamma -Crystallin from Methane-Producing Thermophilic Archaea, Methanosaeta thermophila by Srivastava, Shanti Swaroop, Jamkhindikar, Aditya Anand, Raman, Rajeev, Jobby, Maroor K, Chadalawada, Swathi, Sankaranarayanan, Rajan, Sharma, Yogendra

“…beta gamma -Crystallins are important constituents of the vertebrate eye lens, whereas in microbes, they are prevalent as Ca super(2+)-binding proteins. In…”
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A Transition Metal-Binding, Trimeric βγ-Crystallin from Methane-Producing Thermophilic Archaea, Methanosaeta thermophila by Srivastava, Shanti Swaroop, Jamkhindikar, Aditya Anand, Raman, Rajeev, Jobby, Maroor K, Chadalawada, Swathi, Sankaranarayanan, Rajan, Sharma, Yogendra

“…βγ-Crystallins are important constituents of the vertebrate eye lens, whereas in microbes, they are prevalent as Ca2+-binding proteins. In archaea,…”
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Interface interactions between βγ-crystallin domain and Ig-like domain render Ca 2+ -binding site inoperative in abundant perithecial protein of Neurospora crassa by Swaroop Srivastava, Shanti, Raman, Rajeev, Kiran, Uday, Garg, Rupsi, Chadalawada, Swathi, Pawar, Asmita D, Sankaranarayanan, Rajan, Sharma, Yogendra

“…We describe a set of proteins in which a βγ-crystallin domain pairs with an Ig-like domain, and which are confined to microbes, like bacteria, slime molds and…”
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Ca2+-binding Motif of βγ-Crystallins by Srivastava, Shanti Swaroop, Mishra, Amita, Krishnan, Bal, Sharma, Yogendra

“…βγ-Crystallin-type double clamp (N/D)(N/D)XX(S/T)S motif is an established but sparsely investigated motif for Ca2+ binding. A βγ-crystallin domain is formed…”
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Decoding the molecular design principles underlying Ca(2+) binding to βγ-crystallin motifs by Mishra, Amita, Suman, Shashi Kumar, Srivastava, Shanti Swaroop, Sankaranarayanan, Rajan, Sharma, Yogendra

“…Numerous proteins belonging to the recently expanded βγ-crystallin superfamily bind Ca(2+) at the double-clamp N/D-N/D-X(1)-X(2)-S/T-S motif. However, there…”
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Aggregation-Prone Near-Native Intermediate Formation during Unfolding of a Structurally Similar Nonlenticular βγ-Crystallin Domain by Rajanikanth, V, Srivastava, Shanti Swaroop, Singh, Aditya K, Rajyalakshmi, M, Chandra, Kousik, Aravind, Penmatsa, Sankaranarayanan, Rajan, Sharma, Yogendra

“…The folding and unfolding of structurally similar proteins belonging to a family have long been a focus of investigation of the structure–(un)folding…”
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Decoding the Molecular Design Principles Underlying Ca2+ Binding to βγ-Crystallin Motifs by Mishra, Amita, Suman, Shashi Kumar, Srivastava, Shanti Swaroop, Sankaranarayanan, Rajan, Sharma, Yogendra

“…Numerous proteins belonging to the recently expanded βγ-crystallin superfamily bind Ca2+ at the double-clamp N/D-N/D-X1-X2-S/T-S motif. However, there have…”
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