Probing the Dark State Tertiary Structure in the Cytoplasmic Domain of Rhodopsin:  Proximities between Amino Acids Deduced from Spontaneous Disulfide Bond Formation between Cysteine Pairs Engineered in Cytoplasmic Loops 1, 3, and 4

Kewen Cai; Judith Klein-Seetharaman; Christian Altenbach; Wayne L. Hubbell; H. Gobind Khorana

doi:10.1021/bi010747h

Probing the Dark State Tertiary Structure in the Cytoplasmic Domain of Rhodopsin: Proximities between Amino Acids Deduced from Spontaneous Disulfide Bond Formation between Cysteine Pairs Engineered in Cytoplasmic Loops 1, 3, and 4

Biochemistry ◽

10.1021/bi010747h ◽

2001 ◽

Vol 40 (42) ◽

pp. 12479-12485 ◽

Cited By ~ 19

Author(s):

Kewen Cai ◽

Judith Klein-Seetharaman ◽

Christian Altenbach ◽

Wayne L. Hubbell ◽

H. Gobind Khorana

Keyword(s):

Amino Acids ◽

Disulfide Bond ◽

Tertiary Structure ◽

Bond Formation ◽

Cytoplasmic Domain ◽

Disulfide Bond Formation ◽

Dark State ◽

Cytoplasmic Loops

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Faculty Opinions recommendation of Probing the dark state tertiary structure in the cytoplasmic domain of rhodopsin: proximities between amino acids deduced from spontaneous disulfide bond formation between cysteine pairs engineered in cytoplasmic loops 1, 3, and 4.

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

10.3410/f.1002026.15614 ◽

2001 ◽

Author(s):

Christopher Miller

Keyword(s):

Amino Acids ◽

Disulfide Bond ◽

Tertiary Structure ◽

Bond Formation ◽

Cytoplasmic Domain ◽

Disulfide Bond Formation ◽

Dark State ◽

Cytoplasmic Loops

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Probing the Dark State Tertiary Structure in the Cytoplasmic Domain of Rhodopsin: Proximities between Amino Acids Deduced from Spontaneous Disulfide Bond Formation between Cys316 and Engineered Cysteines in Cytoplasmic Loop 1†,‡

Biochemistry ◽

10.1021/bi010746p ◽

2001 ◽

Vol 40 (42) ◽

pp. 12472-12478 ◽

Cited By ~ 20

Author(s):

Judith Klein-Seetharaman ◽

John Hwa ◽

Kewen Cai ◽

Christian Altenbach ◽

Wayne L. Hubbell ◽

...

Keyword(s):

Amino Acids ◽

Disulfide Bond ◽

Tertiary Structure ◽

Bond Formation ◽

Cytoplasmic Domain ◽

Disulfide Bond Formation ◽

Cytoplasmic Loop ◽

Dark State

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Faculty Opinions recommendation of Probing the dark state tertiary structure in the cytoplasmic domain of rhodopsin: proximities between amino acids deduced from spontaneous disulfide bond formation between Cys316 and engineered cysteines in cytoplasmic loop 1.

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

10.3410/f.1001318.15613 ◽

2001 ◽

Author(s):

Christopher Miller

Keyword(s):

Amino Acids ◽

Disulfide Bond ◽

Tertiary Structure ◽

Bond Formation ◽

Cytoplasmic Domain ◽

Disulfide Bond Formation ◽

Cytoplasmic Loop ◽

Dark State

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Volume354,Number 1 (1998), in Article No. BB980671, “Cross-Linking and Disulfide Bond Formation of Introduced Cysteine Residues Suggest a Modified Model for the Tertiary Structure of URF13 in the Pore-Forming Oligomers,” by David M. Rhoads, Barbara Brunner-Neuenschwander, Charles S. Levings, III, and James N. Siedow, pages 158–164:

Archives of Biochemistry and Biophysics ◽

10.1006/abbi.1998.0923 ◽

1998 ◽

Vol 359 (2) ◽

pp. 320

Keyword(s):

Disulfide Bond ◽

Tertiary Structure ◽

Bond Formation ◽

Cross Linking ◽

Cysteine Residues ◽

Disulfide Bond Formation ◽

Modified Model

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Cross-Linking and Disulfide Bond Formation of Introduced Cysteine Residues Suggest a Modified Model for the Tertiary Structure of URF13 in the Pore-Forming Oligomers

Archives of Biochemistry and Biophysics ◽

10.1006/abbi.1998.0671 ◽

1998 ◽

Vol 354 (1) ◽

pp. 158-164 ◽

Cited By ~ 12

Author(s):

David M. Rhoads ◽

Barbara Brunner-Neuenschwander ◽

Charles S. Levings ◽

James N. Siedow

Keyword(s):

Disulfide Bond ◽

Tertiary Structure ◽

Bond Formation ◽

Cross Linking ◽

Cysteine Residues ◽

Disulfide Bond Formation ◽

Modified Model

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Key Amino Acids of Arabidopsis VKOR in the Activity of Phylloquinone Reduction and Disulfide Bond Formation

Protein and Peptide Letters ◽

10.2174/0929866521666140926115347 ◽

2014 ◽

Vol 22 (1) ◽

pp. 81-86 ◽

Cited By ~ 3

Author(s):

Xiao-Jian Yang ◽

Hao-Ran Cui ◽

Zhi-Bo Yu ◽

Jia-Jia Du ◽

Jia-Ning Xu ◽

...

Keyword(s):

Amino Acids ◽

Disulfide Bond ◽

Bond Formation ◽

Disulfide Bond Formation

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Disulfide bond formation between the N-terminal region of p56lck and the cytoplasmic domain of CD8 studied by Electrospray Ionization and Matrix-Assisted Desorption/Ionization time-of-flight mass spectrometry

IUBMB Life ◽

10.1080/15216549600201912 ◽

1996 ◽

Vol 40 (2) ◽

pp. 409-416

Author(s):

Gwan-Su Yi ◽

Chaejoon Cheong

Keyword(s):

Mass Spectrometry ◽

Electrospray Ionization ◽

Disulfide Bond ◽

Bond Formation ◽

Time Of Flight ◽

Cytoplasmic Domain ◽

Disulfide Bond Formation ◽

Ionization Time ◽

Desorption Ionization ◽

Flight Mass Spectrometry

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Faculty Opinions recommendation of Shedding light on disulfide bond formation: engineering a redox switch in green fluorescent protein.

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

10.3410/f.1002310.28155 ◽

2001 ◽

Author(s):

Thomas Nystrom

Keyword(s):

Green Fluorescent Protein ◽

Disulfide Bond ◽

Fluorescent Protein ◽

Bond Formation ◽

Disulfide Bond Formation ◽

Redox Switch ◽

Green Fluorescent

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Faculty Opinions recommendation of Protein disulfide bond formation in the cytoplasm during oxidative stress.

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

10.3410/f.1018579.218434 ◽

2004 ◽

Author(s):

Ruma Banerjee

Keyword(s):

Oxidative Stress ◽

Disulfide Bond ◽

Bond Formation ◽

Disulfide Bond Formation ◽

Protein Disulfide

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Faculty Opinions recommendation of Modulation of cellular disulfide-bond formation and the ER redox environment by feedback regulation of Ero1.

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

10.3410/f.1082833.535764 ◽

2007 ◽

Author(s):

Davis Ng

Keyword(s):

Disulfide Bond ◽

Bond Formation ◽

Feedback Regulation ◽

Disulfide Bond Formation ◽

Redox Environment

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