Ngā hua rapu kaituhi

1

Conserved F84 and P86 residues in αB-crystallin are essential to effectively prevent the aggregation of substrate proteins mā Santhoshkumar, Puttur, Sharma, K. Krishna

I whakaputaina 2006

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2

Lens Aging: Effects of Crystallins mā Sharma, K. Krishna, Santhoshkumar, Puttur

I whakaputaina 2009

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3

Substrate Protein Interactions and Methylglyoxal Modifications Reduce the Aggregation Propensity of Human Alpha-A-Crystallin G98R Mutant mā Santhoshkumar, Puttur, Sharma, Krishna K.

I whakaputaina 2022

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4

Anti-chaperone βA3/A1(102-117) peptide interacting sites in human αB-crystallin mā Rao, Guruprasad, Santhoshkumar, Puttur, Sharma, K. Krishna

I whakaputaina 2008

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5

Role of αBI5 and αBT162 residues in subunit interaction during oligomerization of αB-crystallin mā Murugesan, Raju, Santhoshkumar, Puttur, Sharma, K. Krishna

I whakaputaina 2008

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6

Cataract-causing αAG98R-crystallin mutant dissociates into monomers having chaperone activity mā Raju, Murugesan, Santhoshkumar, Puttur, Sharma, K. Krishna

I whakaputaina 2011

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7

αA-Crystallin Peptide (66) SDRDKFVIFLDVKHF (80) Accumulating in Aging Lens Impairs the Function of α-Crystallin and Induces Lens Protein Aggregation mā Santhoshkumar, Puttur, Raju, Murugesan, Sharma, K. Krishna

I whakaputaina 2011

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8

αA-Crystallin–Derived Mini-Chaperone Modulates Stability and Function of Cataract Causing αAG98R-Crystallin mā Raju, Murugesan, Santhoshkumar, Puttur, Sharma, K. Krishna

I whakaputaina 2012

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9

Profiling of lens protease involved in generation of αA-66-80 crystallin peptide using an internally quenched protease substrate mā Hariharapura, Raghu, Santhoshkumar, Puttur, Sharma, K. Krishna

I whakaputaina 2013

Whiwhi kuputuhi katoa Whiwhi kuputuhi katoa Whiwhi kuputuhi katoa
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10

Deletion of (54)FLRAPSWF(61) Residues Decreases the Oligomeric Size and Enhances the Chaperone Function of αB-Crystallin() mā Santhoshkumar, Puttur, Murugesan, Raju, Krishna Sharma, K.

I whakaputaina 2009

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11

Structural and Functional Consequences of Chaperone Site Deletion in αA-Crystallin mā Santhoshkumar, Puttur, Karmakar, Srabani, Sharma, Krishna K.

I whakaputaina 2016

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12

Lens Endogenous Peptide αA66-80 Generates Hydrogen Peroxide and Induces Cell Apoptosis mā Raju, Murugesan, Santhoshkumar, Puttur, Sharma, K. Krishna

I whakaputaina 2017

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13

αA-crystallin-derived minichaperone stabilizes αAG98R-crystallin by affecting its zeta potential mā Phadte, Ashutosh S., Santhoshkumar, Puttur, Sharma, K. Krishna

I whakaputaina 2018

Whiwhi kuputuhi katoa Whiwhi kuputuhi katoa
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14

Characterization of an N-terminal mutant of αA-crystallin αA–R21Q associated with congenital cataract mā Phadte, Ashutosh S., Santhoshkumar, Puttur, Sharma, K. Krishna

I whakaputaina 2018

Whiwhi kuputuhi katoa Whiwhi kuputuhi katoa Whiwhi kuputuhi katoa
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15

Cell-penetrating Chaperone Peptide Prevents Protein Aggregation And Protects Against Cell Apoptosis mā Raju, Murugesan, Santhoshkumar, Puttur, Sharma, K. Krishna

I whakaputaina 2017

Whiwhi kuputuhi katoa Whiwhi kuputuhi katoa Whiwhi kuputuhi katoa
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16

Significance of Interactions of Low Molecular Weight Crystallin Fragments in Lens Aging and Cataract Formation mā Santhoshkumar, Puttur, Udupa, Padmanabha, Murugesan, Raju, Sharma, K. Krishna

I whakaputaina 2008

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17

Identification and characterization of a copper binding site in αA-crystallin mā Raju, Murugesan, Santhoshkumar, Puttur, Henzl, T. Michael, Sharma, K. Krishna

I whakaputaina 2011

Whiwhi kuputuhi katoa Whiwhi kuputuhi katoa Whiwhi kuputuhi katoa
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18

Addition of αA-Crystallin Sequence 164–173 to a Mini-Chaperone DFVIFLDVKHFSPEDLT Alters the Conformation but Not the Chaperone-like Activity mā Raju, Murugesan, Santhoshkumar, Puttur, Xie, Leike, Sharma, K. Krishna

I whakaputaina 2014

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19

Correction to Addition of αA-Crystallin Sequence 164–173 to a Mini-Chaperone DFVIFLDVKHFSPEDLT Alters the Conformation but Not the Chaperone-like Activity mā Raju, Murugesan, Santhoshkumar, Puttur, Xie, Leike, Sharma, K. Krishna

I whakaputaina 2014

Whiwhi kuputuhi katoa Whiwhi kuputuhi katoa
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20

Functional rescue of cataract-causing αA-G98R-crystallin by targeted compensatory suppressor mutations in human αA-crystallin mā Phadte, Ashutosh S., Mahalingam, Sundararajan, Santhoshkumar, Puttur, Sharma, Krishna K.

I whakaputaina 2019

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Ngā hua rapu - Santhoshkumar, Puttur

Conserved F84 and P86 residues in αB-crystallin are essential to effectively prevent the aggregation of substrate proteins mā Santhoshkumar, Puttur, Sharma, K. Krishna

Lens Aging: Effects of Crystallins mā Sharma, K. Krishna, Santhoshkumar, Puttur

Substrate Protein Interactions and Methylglyoxal Modifications Reduce the Aggregation Propensity of Human Alpha-A-Crystallin G98R Mutant mā Santhoshkumar, Puttur, Sharma, Krishna K.

Anti-chaperone βA3/A1(102-117) peptide interacting sites in human αB-crystallin mā Rao, Guruprasad, Santhoshkumar, Puttur, Sharma, K. Krishna

Role of αBI5 and αBT162 residues in subunit interaction during oligomerization of αB-crystallin mā Murugesan, Raju, Santhoshkumar, Puttur, Sharma, K. Krishna

Cataract-causing αAG98R-crystallin mutant dissociates into monomers having chaperone activity mā Raju, Murugesan, Santhoshkumar, Puttur, Sharma, K. Krishna

αA-Crystallin Peptide (66) SDRDKFVIFLDVKHF (80) Accumulating in Aging Lens Impairs the Function of α-Crystallin and Induces Lens Protein Aggregation mā Santhoshkumar, Puttur, Raju, Murugesan, Sharma, K. Krishna

αA-Crystallin–Derived Mini-Chaperone Modulates Stability and Function of Cataract Causing αAG98R-Crystallin mā Raju, Murugesan, Santhoshkumar, Puttur, Sharma, K. Krishna

Profiling of lens protease involved in generation of αA-66-80 crystallin peptide using an internally quenched protease substrate mā Hariharapura, Raghu, Santhoshkumar, Puttur, Sharma, K. Krishna

Deletion of (54)FLRAPSWF(61) Residues Decreases the Oligomeric Size and Enhances the Chaperone Function of αB-Crystallin() mā Santhoshkumar, Puttur, Murugesan, Raju, Krishna Sharma, K.

Structural and Functional Consequences of Chaperone Site Deletion in αA-Crystallin mā Santhoshkumar, Puttur, Karmakar, Srabani, Sharma, Krishna K.

Lens Endogenous Peptide αA66-80 Generates Hydrogen Peroxide and Induces Cell Apoptosis mā Raju, Murugesan, Santhoshkumar, Puttur, Sharma, K. Krishna

αA-crystallin-derived minichaperone stabilizes αAG98R-crystallin by affecting its zeta potential mā Phadte, Ashutosh S., Santhoshkumar, Puttur, Sharma, K. Krishna

Characterization of an N-terminal mutant of αA-crystallin αA–R21Q associated with congenital cataract mā Phadte, Ashutosh S., Santhoshkumar, Puttur, Sharma, K. Krishna

Cell-penetrating Chaperone Peptide Prevents Protein Aggregation And Protects Against Cell Apoptosis mā Raju, Murugesan, Santhoshkumar, Puttur, Sharma, K. Krishna

Significance of Interactions of Low Molecular Weight Crystallin Fragments in Lens Aging and Cataract Formation mā Santhoshkumar, Puttur, Udupa, Padmanabha, Murugesan, Raju, Sharma, K. Krishna

Identification and characterization of a copper binding site in αA-crystallin mā Raju, Murugesan, Santhoshkumar, Puttur, Henzl, T. Michael, Sharma, K. Krishna

Addition of αA-Crystallin Sequence 164–173 to a Mini-Chaperone DFVIFLDVKHFSPEDLT Alters the Conformation but Not the Chaperone-like Activity mā Raju, Murugesan, Santhoshkumar, Puttur, Xie, Leike, Sharma, K. Krishna

Correction to Addition of αA-Crystallin Sequence 164–173 to a Mini-Chaperone DFVIFLDVKHFSPEDLT Alters the Conformation but Not the Chaperone-like Activity mā Raju, Murugesan, Santhoshkumar, Puttur, Xie, Leike, Sharma, K. Krishna

Functional rescue of cataract-causing αA-G98R-crystallin by targeted compensatory suppressor mutations in human αA-crystallin mā Phadte, Ashutosh S., Mahalingam, Sundararajan, Santhoshkumar, Puttur, Sharma, Krishna K.

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