scholarly journals "Peptabody": A new type of high avidity binding protein

1997 ◽  
Vol 94 (5) ◽  
pp. 1663-1668 ◽  
Author(s):  
A. V. Terskikh ◽  
J.-M. Le Doussal ◽  
R. Crameri ◽  
I. Fisch ◽  
J.-P. Mach ◽  
...  
Keyword(s):  
Binding Protein ◽  
High Avidity ◽  
New Type

Nucleotide sequence ofCab-8, a new type I gene encoding a chlorophylla/b-binding protein of LHC II inPisum

1991 ◽  
Vol 17 (3) ◽  
pp. 523-526 ◽  
Author(s):  
Laura Alexander ◽  
Denis Falconet ◽  
Brian W. Fristensky ◽  
Michael J. White ◽  
John C. Watson ◽  
...  
Keyword(s):  
Nucleotide Sequence ◽  
Binding Protein ◽  
Type I ◽  
Gene Encoding ◽  
Lhc Ii ◽  
New Type ◽  
I Gene

The PSII-S Protein of Higher Plants: A New Type of Pigment-Binding Protein

Biochemistry ◽  
1995 ◽  
Vol 34 (35) ◽  
pp. 11133-11141 ◽  
Author(s):  
Christiane Funk ◽  
Wolfgang P. Schroeder ◽  
Artur Napiwotzki ◽  
Staffan E. Tjus ◽  
Gernot Renger ◽  
...  
Keyword(s):  
Higher Plants ◽  
Binding Protein ◽  
S Protein ◽  
New Type

scholarly journals A non-canonical mechanism for Crm1-export cargo complex assembly

eLife ◽  
2015 ◽  
Vol 4 ◽  
Author(s):  
Ute Fischer ◽  
Nico Schäuble ◽  
Sabina Schütz ◽  
Martin Altvater ◽  
Yiming Chang ◽  
...  
Keyword(s):  
Complex Formation ◽  
Nuclear Export ◽  
Binding Protein ◽  
Complex Assembly ◽  
Stepwise Mechanism ◽  
Weak Binding ◽  
New Type ◽  
Ribosome Export ◽  
Transport Receptor

The transport receptor Crm1 mediates the export of diverse cargos containing leucine-rich nuclear export signals (NESs) through complex formation with RanGTP. To ensure efficient cargo release in the cytoplasm, NESs have evolved to display low affinity for Crm1. However, mechanisms that overcome low affinity to assemble Crm1-export complexes in the nucleus remain poorly understood. In this study, we reveal a new type of RanGTP-binding protein, Slx9, which facilitates Crm1 recruitment to the 40S pre-ribosome-associated NES-containing adaptor Rio2. In vitro, Slx9 binds Rio2 and RanGTP, forming a complex. This complex directly loads Crm1, unveiling a non-canonical stepwise mechanism to assemble a Crm1-export complex. A mutation in Slx9 that impairs Crm1-export complex assembly inhibits 40S pre-ribosome export. Thus, Slx9 functions as a scaffold to optimally present RanGTP and the NES to Crm1, therefore, triggering 40S pre-ribosome export. This mechanism could represent one solution to the paradox of weak binding events underlying rapid Crm1-mediated export.

Competitive idiotype--anti-idiotype immunoassay for adenosine deaminase binding protein in urine.

1985 ◽  
Vol 31 (11) ◽  
pp. 1833-1837 ◽  
Author(s):  
R E Thompson ◽  
C R Hewitt ◽  
D J Piper ◽  
W P Hansen ◽  
R H Rubin ◽  
...  
Keyword(s):  
Monoclonal Antibody ◽  
Renal Disease ◽  
Adenosine Deaminase ◽  
Binding Protein ◽  
Normal Subjects ◽  
Urine Samples ◽  
Competitive Immunoassay ◽  
Sandwich Type ◽  
New Type

Abstract This competitive immunoassay, based on inhibition by antigen of the idiotype-anti-idiotype interaction, detects adenosine deaminase binding protein (ABP), and involves use of monoclonal anti-idiotype antibodies prepared to a monoclonal antibody specific for ABP. The conditions for this new type of competitive immunoassay are investigated. This competitive immunoassay is as sensitive and reproducible as an earlier described "sandwich"-type immunoassay for ABP (Clin Chem 31: 679-683, 1985). Evaluation of urine samples from normal subjects and from patients showed increased concentrations of ABP in patients with renal disease.

scholarly journals The Inner Nuclear Membrane Protein Nemp1 Is a New Type of RanGTP-Binding Protein in Eukaryotes

PLoS ONE ◽  
2015 ◽  
Vol 10 (5) ◽  
pp. e0127271 ◽  
Author(s):  
Takashi Shibano ◽  
Hiroshi Mamada ◽  
Fumihiko Hakuno ◽  
Shin-Ichiro Takahashi ◽  
Masanori Taira
Keyword(s):  
Membrane Protein ◽  
Nuclear Membrane ◽  
Binding Protein ◽  
Inner Nuclear Membrane ◽  
New Type ◽  
Inner Nuclear Membrane Protein ◽  
Nuclear Membrane Protein

scholarly journals IscR of Rhodobacter sphaeroides functions as repressor of genes for iron‐sulfur metabolism and represents a new type of iron‐sulfur‐binding protein

2015 ◽  
Vol 4 (5) ◽  
pp. 790-802 ◽  
Author(s):  
Bernhard Remes ◽  
Benjamin D. Eisenhardt ◽  
Vasundara Srinivasan ◽  
Gabriele Klug
Keyword(s):  
Rhodobacter Sphaeroides ◽  
Binding Protein ◽  
Sulfur Metabolism ◽  
Iron Sulfur ◽  
New Type

scholarly journals SFS, a Novel Fibronectin-Binding Protein from Streptococcus equi, Inhibits the Binding between Fibronectin and Collagen

1999 ◽  
Vol 67 (5) ◽  
pp. 2383-2388 ◽  
Author(s):  
Hans Lindmark ◽  
Bengt Guss
Keyword(s):  
Binding Protein ◽  
Surface Protein ◽  
Upper Respiratory Tract ◽  
Gene Encoding ◽  
Sequence Comparisons ◽  
Streptococcus Equi ◽  
New Type ◽  
Fibronectin Binding Protein ◽  
Serious Disease

ABSTRACT The obligate parasitic bacterium Streptococcus equisubsp. equi is the causative agent of strangles, a serious disease of the upper respiratory tract in horses. In this study we have, using shotgun phage display, cloned from S. equisubsp. equi and characterized a gene, calledsfs, encoding a protein termed SFS, representing a new type of fibronectin (Fn)-binding protein. The sfs gene was found to be present in all 50 isolates of S. equi subsp.equi tested and in 41 of 48 S. equi subsp.zooepidemicus isolates tested. The sfs gene is down-regulated during growth in vitro compared to fnz, a previously characterized gene encoding an Fn-binding protein fromS. equi subsp. zooepidemicus. Sequence comparisons revealed no similarities to previously characterized Fn-binding proteins, but high scores were obtained against collagen. Besides similarity due to the high content of glycine, serine, and proline residues present in both proteins, there was a nine-residue motif present both in collagen and in the Fn-binding domain of SFS. By searching the Oklahoma S. pyogenes database, we found that this motif is also present in a potential cell surface protein fromS. pyogenes. Protein SFS was found to inhibit the binding between Fn and collagen in a concentration-dependent way.

A new type of reusable piezoimmunosensor fabricated by a recombinant IgG-binding protein

The Analyst ◽  
2000 ◽  
Vol 125 (4) ◽  
pp. 669-671 ◽  
Author(s):  
Xuezhen Ren ◽  
Eiry Kobatake ◽  
Masuo Aizawa
Keyword(s):  
Binding Protein ◽  
Igg Binding ◽  
New Type

scholarly journals Structure and function of phage p2 ORF34p2, a new type of single-stranded DNA binding protein

2009 ◽  
Vol 73 (6) ◽  
pp. 1156-1170 ◽  
Author(s):  
Erika Scaltriti ◽  
Mariella Tegoni ◽  
Claudio Rivetti ◽  
Hélène Launay ◽  
Jean-Yves Masson ◽  
...  
Keyword(s):  
Dna Binding ◽  
Binding Protein ◽  
Dna Binding Protein ◽  
Structure And Function ◽  
Single Stranded Dna ◽  
New Type ◽  
And Function
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