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Mechanical resistance in unstructured proteins

by Sigurður Ægir Jónsson, Simon Mitternacht, Anders Irbäck - Biophys. J , 2013
"... Abstract. Single-molecule pulling experiments on unstructured proteins linked to neurodegen-erative diseases have measured rupture forces comparable to those for stable folded proteins. To investigate the structural mechanisms of this unexpected force resistance, we perform pul-ling simulations of t ..."
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Abstract. Single-molecule pulling experiments on unstructured proteins linked to neurodegen-erative diseases have measured rupture forces comparable to those for stable folded proteins. To investigate the structural mechanisms of this unexpected force resistance, we perform pul-ling simulations

Intrinsically unstructured proteins: re-assessing the protein structure-function paradigm

by Peter E. Wright, H. Jane Dyson , 1999
"... *Corresponding authors A major challenge in the post-genome era will be determination of the functions of the encoded protein sequences. Since it is generally assumed that the function of a protein is closely linked to its three-dimensional structure, prediction or experimental determination of the ..."
Abstract - Cited by 246 (3 self) - Add to MetaCart
*Corresponding authors A major challenge in the post-genome era will be determination of the functions of the encoded protein sequences. Since it is generally assumed that the function of a protein is closely linked to its three-dimensional structure, prediction or experimental determination

Intrinsically Unstructured Proteins: Potential Targets for Drug Discovery

by Pathan Salma, Chintan Chhatbar, Sriram Seshadri - Am. J. Infect. Dis. 2009
"... Abstract: Problem statement: The function of a protein is dependent on its three-dimensional structure. However, numerous proteins lacking intrinsic globular 3D structure under physiological conditions had been recognized. These proteins are frequently involved in some of the most critical cellular ..."
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control mechanisms and it appears that their rapid turnover, aided by their unstructured nature in the unbound state, provides a level of control that allows rapid and accurate responses of the cell to changing environmental conditions. Approach: A significant number of proteins known to be involved

Tight regulation of unstructured proteins: From transcript synthesis to protein degradation

by Jörg Gsponer, Matthias E. Futschik, Sarah A. Teichmann, M. Madan Babu - Science
"... Altered abundance of several intrinsically unstructured proteins (IUPs) has been associated with perturbed cellular signalling that may lead to pathological conditions such as cancer. Therefore, it is important to understand how cells precisely regulate availability of IUPs. We observe that regulati ..."
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Altered abundance of several intrinsically unstructured proteins (IUPs) has been associated with perturbed cellular signalling that may lead to pathological conditions such as cancer. Therefore, it is important to understand how cells precisely regulate availability of IUPs. We observe

Operational Definition of Intrinsically Unstructured Protein Sequences Based on Susceptibility to the 20S Proteasome

by John Wiley, Yosef Shaul, John Wiley
"... Operational definition of intrinsically unstructured protein sequences based on susceptibility to the 20S Proteasome ..."
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Operational definition of intrinsically unstructured protein sequences based on susceptibility to the 20S Proteasome

The pairwise energy content estimated from amino acid composition discriminates between folded and intrinsically unstructured proteins

by Zsuzsanna Dosztányi, Veronika Csizmók, Péter Tompa, István Simon - J. Mol. Biol , 2005
"... Intrinsically unstructured/disordered proteins/ domains (IUPs), such as p21, 1 the N-terminal domain of p53 2 or the transactivator domain of CREB, 3 exist in a largely disordered structural state, ..."
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Intrinsically unstructured/disordered proteins/ domains (IUPs), such as p21, 1 the N-terminal domain of p53 2 or the transactivator domain of CREB, 3 exist in a largely disordered structural state,

Minireview Regulating highly dynamic unstructured proteins and their coding mRNAs

by Buyong Ma, Ruth Nussinov , 2009
"... electronic version of this article is the complete one and can be ..."
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electronic version of this article is the complete one and can be

An Experimental Study of GFP-Based FRET, with Application to Intrinsically Unstructured Proteins. Protein Sci

by Tomoo Ohashi, Stephane D. Galiacy, Gina Briscoe, Harold, P. Erickson
"... We have experimentally studied the fluorescence resonance energy transfer (FRET) between green fluorescent protein (GFP) molecules by inserting folded or intrinsically unstructured proteins between CyPet and Ypet. We discovered that most of the enhanced FRET signal previously reported for this pair ..."
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We have experimentally studied the fluorescence resonance energy transfer (FRET) between green fluorescent protein (GFP) molecules by inserting folded or intrinsically unstructured proteins between CyPet and Ypet. We discovered that most of the enhanced FRET signal previously reported for this pair

A Novel Two-dimensional Electrophoresis Technique for the Identification of Intrinsically Unstructured Proteins*□S

by Peter Friedrich, Peter Tompa
"... Intrinsically unstructured proteins (IUPs) lack a well de-fined three-dimensional structure under physiological conditions. They constitute a significant fraction of vari-ous proteomes, but only a handful of them have so far been identified. Here we report the development of a two-dimensional electr ..."
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Intrinsically unstructured proteins (IUPs) lack a well de-fined three-dimensional structure under physiological conditions. They constitute a significant fraction of vari-ous proteomes, but only a handful of them have so far been identified. Here we report the development of a two

Rwdd1, a Thymus Aging Related Molecule, Is a New Member of the Intrinsically Unstructured Protein Family

by Ning Kang, Dai Chen, Li Wang, Lian Duan, Shirong Liu, Long Tang, Qingfeng Liu, Lianxian Cui, Wei He
"... We had previously identified a novel protein termed Rwdd1 whose expression in thymus is decreased in aged or oxidatively stressed mice. In the present study, we found that Rwdd1 expressed in both prokaryotic and eukaryotic cells showed a slower migration rate on SDS-PAGE gel. In addition, Rwdd1 was ..."
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was more sensitive to proteinase proteolysis. Furthermore, being a highly acidic protein which contains an RWD domain, Rwdd1 shared a high level of sequence similarity with Gir2, a member of the intrinsically unstructured protein (IUP). These findings suggest that Rwdd1 is a novel member of the IUP family
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