Sequence conservation in Ig-like domains: the role of highly conserved proline residues in the fibronectin type III superfamily (Q34675827)

3 August 2017

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title

Sequence conservation in Ig-like domains: the role of highly conserved proline residues in the fibronectin type III superfamily (English)

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3 August 2017

Annette Steward

1

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3 August 2017

Sima Adhya

series ordinal

2

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3 August 2017

Jane Clarke

series ordinal

3

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3 August 2017

language of work or name

English

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publication date

1 May 2002

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Journal of Molecular Biology

3 August 2017

number of pages

6

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based on heuristic

inferred from page(s)

published in

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3 August 2017

volume

318

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3 August 2017

issue

4

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3 August 2017

page(s)

935-940

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The tyrosine corner: a feature of most Greek key beta-barrel proteins

3 August 2017

cites work

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Conservation of folding and stability within a protein family: the tyrosine corner as an evolutionary cul-de-sac

7 January 2021

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Folding studies of immunoglobulin-like β-sandwich proteins suggest that they share a common folding pathway

7 January 2021

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The folding of an immunoglobulin-like Greek key protein is defined by a common-core nucleus and regions constrained by topology

7 January 2021

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The folding nucleus of a fibronectin type III domain is composed of core residues of the immunoglobulin-like fold

7 January 2021

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Mapping the folding pathway of an immunoglobulin domain: structural detail from Phi value analysis and movement of the transition state

7 January 2021

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Contribution of a proline residue and a salt bridge to the stability of a type I reverse turn in chymotrypsin inhibitor-2

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Multiple roles of prolyl residues in structure and folding

7 January 2021

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Stable proline box motif at the N-terminal end of alpha-helices

7 January 2021

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

7 January 2021

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

7 January 2021

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Structure of a Fibronectin Type III Domain from Tenascin Phased by MAD Analysis of the Selenomethionyl Protein

7 January 2021

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2.0 A crystal structure of a four-domain segment of human fibronectin encompassing the RGD loop and synergy region

7 January 2021

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The effect of boundary selection on the stability and folding of the third fibronectin type III domain from human tenascin

7 January 2021

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7 January 2021

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7 January 2021

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7 January 2021

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7 January 2021

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Formation of amyloid-like fibrils by self-association of a partially unfolded fibronectin type III module

7 January 2021

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Immunoglobulin-like modules from titin I-band: extensible components of muscle elasticity

7 January 2021

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Structure and stability of an immunoglobulin superfamily domain from twitchin, a muscle protein of the nematode Caenorhabditis elegans

7 January 2021

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The structure of a PKD domain from polycystin-1: implications for polycystic kidney disease

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Designed protein tetramer zipped together with a hydrophobic Alzheimer homology: A structural clue to amyloid assembly

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10.1016/S0022-2836(02)00184-5

7 January 2021

Identifiers

DOI

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3 August 2017

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