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11
Engineering the Active Site Lid Dynamics to Improve the Catalytic Efficiency of Yeast Cytosine Deaminase
Engineering the Active Site Lid Dynamics to Improve the Catalytic Efficiency of Yeast Cytosine Deaminase
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Engineering the Active Site Lid Dynamics to Improve the Catalytic Efficiency of Yeast Cytosine Deaminase

Deng, Hanzhong ; Qin, Mingming ; Liu, Zhijun ; Yang, Ying ; Wang, Yefei ; Yao, Lishan

International journal of molecular sciences, 2023-04, Vol.24 (7), p.6592 [Periódico revisado por pares]

Switzerland: MDPI AG

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12
Comparison of backbone dynamics of the p50 dimerization domain of NFκB in the homodimeric transcription factor NFκB1 and in its heterodimeric complex with RelA (p65)
Comparison of backbone dynamics of the p50 dimerization domain of NFκB in the homodimeric transcription factor NFκB1 and in its heterodimeric complex with RelA (p65)
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Comparison of backbone dynamics of the p50 dimerization domain of NFκB in the homodimeric transcription factor NFκB1 and in its heterodimeric complex with RelA (p65)

Kohl, Bastian ; Granitzka, Vanessa ; Singh, Amrinder ; Quintas, Pedro ; Xiromeriti, Elli ; Mörtel, Fabian ; Wright, Peter E. ; Kroon, Gerard ; Dyson, H. Jane ; Stoll, Raphael

Protein science, 2019-12, Vol.28 (12), p.2064-2072 [Periódico revisado por pares]

Hoboken, USA: John Wiley & Sons, Inc

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13
The impact of different mutations at arginine141 on the structure, subunit exchange dynamics and chaperone activity of Hsp16.3
The impact of different mutations at arginine141 on the structure, subunit exchange dynamics and chaperone activity of Hsp16.3
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The impact of different mutations at arginine141 on the structure, subunit exchange dynamics and chaperone activity of Hsp16.3

Panda, Alok Kumar ; Chakraborty, Ayon ; Nandi, Sandip Kumar ; Biswas, Ashis

Proteins, structure, function, and bioinformatics, 2020-06, Vol.88 (6), p.759-774 [Periódico revisado por pares]

Hoboken, USA: John Wiley & Sons, Inc

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14
Structures of three polycystic kidney disease-like domains from Clostridium histolyticum collagenases ColG and ColH
Structures of three polycystic kidney disease-like domains from Clostridium histolyticum collagenases ColG and ColH
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Structures of three polycystic kidney disease-like domains from Clostridium histolyticum collagenases ColG and ColH

Bauer, Ryan ; Janowska, Katarzyna ; Taylor, Kelly ; Jordan, Brad ; Gann, Steve ; Janowski, Tomasz ; Latimer, Ethan C. ; Matsushita, Osamu ; Sakon, Joshua

Acta crystallographica. Section D, Biological crystallography., 2015-03, Vol.71 (3), p.565-577 [Periódico revisado por pares]

5 Abbey Square, Chester, Cheshire CH1 2HU, England: International Union of Crystallography

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15
The Role of Rigid Residues in Modulating TEM-1 β-Lactamase Function and Thermostability
The Role of Rigid Residues in Modulating TEM-1 β-Lactamase Function and Thermostability
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The Role of Rigid Residues in Modulating TEM-1 β-Lactamase Function and Thermostability

Kolbaba-Kartchner, Bethany ; Kazan, I Can ; Mills, Jeremy H ; Ozkan, S Banu

International journal of molecular sciences, 2021-03, Vol.22 (6), p.2895 [Periódico revisado por pares]

Switzerland: MDPI AG

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16
Identification of specificity and promiscuity of PDZ domain interactions through their dynamic behavior
Identification of specificity and promiscuity of PDZ domain interactions through their dynamic behavior
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Identification of specificity and promiscuity of PDZ domain interactions through their dynamic behavior

Gerek, Z. Nevin ; Keskin, Ozlem ; Ozkan, S. Banu

Proteins, structure, function, and bioinformatics, 2009-12, Vol.77 (4), p.796-811 [Periódico revisado por pares]

Hoboken: Wiley Subscription Services, Inc., A Wiley Company

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17
Leukemia Fusion Target AF9 Is an Intrinsically Disordered Transcriptional Regulator that Recruits Multiple Partners via Coupled Folding and Binding
Leukemia Fusion Target AF9 Is an Intrinsically Disordered Transcriptional Regulator that Recruits Multiple Partners via Coupled Folding and Binding
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Leukemia Fusion Target AF9 Is an Intrinsically Disordered Transcriptional Regulator that Recruits Multiple Partners via Coupled Folding and Binding

Leach, Benjamin I. ; Kuntimaddi, Aravinda ; Schmidt, Charles R. ; Cierpicki, Tomasz ; Johnson, Stephanie A. ; Bushweller, John H.

Structure (London), 2013-01, Vol.21 (1), p.176-183 [Periódico revisado por pares]

United States: Elsevier Ltd

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18
VAP‐SCRN1 interaction regulates dynamic endoplasmic reticulum remodeling and presynaptic function
VAP‐SCRN1 interaction regulates dynamic endoplasmic reticulum remodeling and presynaptic function
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VAP‐SCRN1 interaction regulates dynamic endoplasmic reticulum remodeling and presynaptic function

Lindhout, Feline W ; Cao, Yujie ; Kevenaar, Josta T ; Bodzęta, Anna ; Stucchi, Riccardo ; Boumpoutsari, Maria M ; Katrukha, Eugene A ; Altelaar, Maarten ; MacGillavry, Harold D ; Hoogenraad, Casper C

The EMBO journal, 2019-10, Vol.38 (20), p.e101345-n/a [Periódico revisado por pares]

England: Blackwell Publishing Ltd

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19
Different dynamics and pathway of disulfide bonds reduction of two human defensins, a molecular dynamics simulation study
Different dynamics and pathway of disulfide bonds reduction of two human defensins, a molecular dynamics simulation study
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Different dynamics and pathway of disulfide bonds reduction of two human defensins, a molecular dynamics simulation study

Zhang, Liqun

Proteins, structure, function, and bioinformatics, 2017-04, Vol.85 (4), p.665-681 [Periódico revisado por pares]

United States: Wiley Subscription Services, Inc

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20
The C‐terminal extension of Mycobacterium tuberculosis Hsp16.3 regulates its oligomerization, subunit exchange dynamics and chaperone function
The C‐terminal extension of Mycobacterium tuberculosis Hsp16.3 regulates its oligomerization, subunit exchange dynamics and chaperone function
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The C‐terminal extension of Mycobacterium tuberculosis Hsp16.3 regulates its oligomerization, subunit exchange dynamics and chaperone function

Panda, Alok Kumar ; Chakraborty, Ayon ; Nandi, Sandip Kumar ; Kaushik, Abhishek ; Biswas, Ashis

The FEBS journal, 2017-01, Vol.284 (2), p.277-300 [Periódico revisado por pares]

England: Blackwell Publishing Ltd

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