A General Name Binding Mechanism

Trustworthy Global Computing - Lecture Notes in Computer Science ◽

10.1007/11580850_5 ◽

2005 ◽

pp. 61-74 ◽

Cited By ~ 4

Author(s):

Michele Boreale ◽

Maria Grazia Buscemi ◽

Ugo Montanari

Keyword(s):

Binding Mechanism ◽

Name Binding

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Faculty Opinions recommendation of A binding mechanism in protein-nucleotide interactions: implication for U1A RNA binding.

Faculty Opinions – Post-Publication Peer Review of the Biomedical Literature ◽

10.3410/f.1027627.334661 ◽

2005 ◽

Author(s):

Matthew Jacobson

Keyword(s):

Rna Binding ◽

Binding Mechanism ◽

Nucleotide Interactions

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Faculty Opinions recommendation of The TATA-binding protein core domain in solution variably bends TATA sequences via a three-step binding mechanism.

Faculty Opinions – Post-Publication Peer Review of the Biomedical Literature ◽

10.3410/f.1157880.619132 ◽

2009 ◽

Author(s):

Herschel Wade

Keyword(s):

Binding Protein ◽

Tata Binding Protein ◽

Binding Mechanism ◽

Core Domain ◽

Protein Core

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Faculty Opinions recommendation of Analysis of activator-binding sites on the APC/C supports a cooperative substrate-binding mechanism.

Faculty Opinions – Post-Publication Peer Review of the Biomedical Literature ◽

10.3410/f.1159981.619666 ◽

2009 ◽

Author(s):

Jane Endicott

Keyword(s):

Binding Sites ◽

Substrate Binding ◽

Binding Mechanism

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Faculty Opinions recommendation of A competitive transcription factor binding mechanism determines the timing of late cell cycle-dependent gene expression.

Faculty Opinions – Post-Publication Peer Review of the Biomedical Literature ◽

10.3410/f.2947957.5387054 ◽

2010 ◽

Author(s):

Robert De Bruin

Keyword(s):

Gene Expression ◽

Cell Cycle ◽

Transcription Factor ◽

Transcription Factor Binding ◽

Binding Mechanism ◽

Factor Binding ◽

Cycle Dependent

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Faculty Opinions recommendation of A folding-after-binding mechanism describes the recognition between the transactivation domain of c-Myb and the KIX domain of the CREB-binding protein.

Faculty Opinions – Post-Publication Peer Review of the Biomedical Literature ◽

10.3410/f.717967973.793467639 ◽

2012 ◽

Author(s):

Vladimir Uversky ◽

Christopher Boehme

Keyword(s):

Binding Protein ◽

Transactivation Domain ◽

Creb Binding Protein ◽

Binding Mechanism ◽

Kix Domain

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Faculty Opinions recommendation of Staggered ATP binding mechanism of eukaryotic chaperonin TRiC (CCT) revealed through high-resolution cryo-EM.

Faculty Opinions – Post-Publication Peer Review of the Biomedical Literature ◽

10.3410/f.726880892.793527718 ◽

2017 ◽

Author(s):

Michael B Sherman

Keyword(s):

High Resolution ◽

Atp Binding ◽

Binding Mechanism

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Design, Selection and Binding Mechanism of Bivalent Miniproteins Targeting Human Thrombin

Advances in Experimental Medicine and Biology - Peptides for Youth ◽

10.1007/978-0-387-73657-0_180 ◽

2009 ◽

pp. 417-418

Author(s):

Andy Ng ◽

Jamshid Tanha ◽

Saran Narang ◽

Feng Ni

Keyword(s):

Binding Mechanism ◽

Human Thrombin ◽

Design Selection

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Recognizing adsorption of Cd(Ⅱ) by a novel core-shell mesoporous ion-imprinted polymer: Characterization, binding mechanism and practical application

Chemosphere ◽

10.1016/j.chemosphere.2021.130369 ◽

2021 ◽

pp. 130369

Author(s):

Hui Cao ◽

Pu Yang ◽

Tai Ye ◽

Min Yuan ◽

Jinsong Yu ◽

...

Keyword(s):

Core Shell ◽

Ion Imprinted Polymer ◽

Binding Mechanism ◽

Practical Application ◽

Imprinted Polymer ◽

Polymer Characterization ◽

Ion Imprinted

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Binding mechanism and functional evaluation of quercetin 3-rhamnoside on lipase

Food Chemistry ◽

10.1016/j.foodchem.2021.129960 ◽

2021 ◽

Vol 359 ◽

pp. 129960

Author(s):

Di Wu ◽

Ran Duan ◽

Lan Tang ◽

Xia Hu ◽

Fang Geng ◽

...

Keyword(s):

Functional Evaluation ◽

Binding Mechanism

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Kinetic Constraints in the Specific Interaction between Phosphorylated Ubiquitin and Proteasomal Shuttle Factors

Biomolecules ◽

10.3390/biom11071008 ◽

2021 ◽

Vol 11 (7) ◽

pp. 1008

Author(s):

Ling-Yun Qin ◽

Zhou Gong ◽

Kan Liu ◽

Xu Dong ◽

Chun Tang

Keyword(s):

Exchange Rate ◽

Self Assembly ◽

Solution Structure ◽

Specific Interaction ◽

Dissociation Rate ◽

Fine Tuning ◽

Binding Mechanism ◽

Kinetics Analysis ◽

Kinetic Constraint ◽

Thermodynamic Basis

Ubiquitin (Ub) specifically interacts with the Ub-associating domain (UBA) in a proteasomal shuttle factor, while the latter is involved in either proteasomal targeting or self-assembly coacervation. PINK1 phosphorylates Ub at S65 and makes Ub alternate between C-terminally relaxed (pUbRL) and retracted conformations (pUbRT). Using NMR spectroscopy, we show that pUbRL but not pUbRT preferentially interacts with the UBA from two proteasomal shuttle factors Ubqln2 and Rad23A. Yet discriminatorily, Ubqln2-UBA binds to pUb more tightly than Rad23A does and selectively enriches pUbRL upon complex formation. Further, we determine the solution structure of the complex between Ubqln2-UBA and pUbRL and uncover the thermodynamic basis for the stronger interaction. NMR kinetics analysis at different timescales further suggests an indued-fit binding mechanism for pUb-UBA interaction. Notably, at a relatively low saturation level, the dissociation rate of the UBA-pUbRL complex is comparable with the exchange rate between pUbRL and pUbRT. Thus, a kinetic constraint would dictate the interaction between Ub and UBA, thus fine-tuning the functional state of the proteasomal shuttle factors.

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