The domain-swapped dimer of cyanovirin-N is in a metastable folded state: reconciliation of X-ray and NMR structures (Q27639001)

8

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Angela Gronenborn

object named as

Angela M Gronenborn

9

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Barry R O'Keefe

6

object named as

Barry R O'Keefe

0 references

Istvan Botos

3

object named as

Istvan Botos

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author name string

Laura G Barrientos

1

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John M Louis

2

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Toshiyuki Mori

4

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Zhaozhong Han

5

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Michael R Boyd

Refined structure of monomeric diphtheria toxin at 2.3 A resolution

7

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publication date

May 2002

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published in

Structure

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volume

10

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issue

5

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page(s)

673-86

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cites work

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Domain swapping: entangling alliances between proteins

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One sequence, two folds: a metastable structure of CD2

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Crystal structure of the human cell cycle protein CksHs1: single domain fold with similarity to kinase N-lobe domain

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The 2.2 Å Crystal Structure of Hsp33

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Bovine seminal ribonuclease: structure at 1.9 A resolution

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Assignment and Secondary-Structure Determination of Monomeric Bovine Seminal Ribonuclease Employing Computer-Assisted Evaluation of Homonuclear Three-Dimensional 1H-NMR Spectra

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Solution structure of cyanovirin-N, a potent HIV-inactivating protein

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Crystal structure of cyanovirin-N, a potent HIV-inactivating protein, shows unexpected domain swapping

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The crystal structure of a 3D domain-swapped dimer of RNase A at a 2.1-A resolution

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Human cystatin C, an amyloidogenic protein, dimerizes through three-dimensional domain swapping

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Glutamine repeats and neurodegenerative diseases: molecular aspects

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A domain-swapped RNase A dimer with implications for amyloid formation

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Measurement of J and dipolar couplings from simplified two-dimensional NMR spectra

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Order matrix analysis of residual dipolar couplings using singular value decomposition.

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Domain orientation and dynamics in multidomain proteins from residual dipolar couplings

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Design of three-dimensional domain-swapped dimers and fibrous oligomers

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A proposed structural model for amyloid fibril elongation: domain swapping forms an interdigitating beta-structure polymer

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Glutamine repeats as polar zippers: their possible role in inherited neurodegenerative diseases

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Orienting domains in proteins using dipolar couplings measured by liquid-state NMR: differences in solution and crystal forms of maltodextrin binding protein loaded with beta-cyclodextrin

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Influence of proline residues on protein conformation

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Enhanced protein thermostability from site-directed mutations that decrease the entropy of unfolding

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Sequence conservation provides the best prediction of the role of proline residues in p13suc1 1 1Edited by J. Thornton

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Three-dimensional domain swapping in p13suc1 occurs in the unfolded state and is controlled by conserved proline residues.

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Cause of neural death in neurodegenerative diseases attributable to expansion of glutamine repeats

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Design and initial characterization of a circular permuted variant of the potent HIV-inactivating protein cyanovirin-N.

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Isolation, primary sequence determination, and disulfide bond structure of cyanovirin-N, an anti-HIV (human immunodeficiency virus) protein from the cyanobacterium Nostoc ellipsosporum

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Identifiers

DOI

1 reference

Consolidated OpenCitations Corpus – April 2017

1 reference

Consolidated OpenCitations Corpus – April 2017

PubMed publication ID

12015150

1 reference

Consolidated OpenCitations Corpus – April 2017