Phytotropin-binding sites and auxin transport in Cucurbita pepo: evidence for two recognition sites

Planta ◽  
1992 ◽  
Vol 187 (2) ◽  
Author(s):  
Wolfgang Michalke ◽  
GerardF. Katekar ◽  
ArtE. Geissler
Keyword(s):  
Binding Sites ◽  
Cucurbita Pepo ◽  
Auxin Transport ◽  
Recognition Sites

Visualization of molecular binding sites at the nanoscale in the lift-up mode by amplitude-modulation atomic force microscopy

Nanoscale ◽  
2021 ◽  
Vol 13 (7) ◽  
pp. 4213-4220
Author(s):  
Tatsuhiro Maekawa ◽  
Takashi Nyu ◽  
Evan Angelo Quimada Mondarte ◽  
Hiroyuki Tahara ◽  
Kasinan Suthiwanich ◽  
...  
Keyword(s):  
Atomic Force Microscopy ◽  
Molecular Recognition ◽  
Amplitude Modulation ◽  
Binding Sites ◽  
Local Distribution ◽  
New Approach ◽  
Molecular Binding ◽  
Force Microscopy ◽  
Atomic Force ◽  
Recognition Sites

We report a new approach to visualize the local distribution of molecular recognition sites with nanoscale resolution by amplitude-modulation atomic force microscopy.

scholarly journals Recognition of highly restricted regions in the β-propeller domain of αIIb by platelet-associated anti-αIIbβ3 autoantibodies in primary immune thrombocytopenia

Blood ◽  
2012 ◽  
Vol 120 (7) ◽  
pp. 1499-1509 ◽  
Author(s):  
Kazunobu Kiyomizu ◽  
Hirokazu Kashiwagi ◽  
Tsuyoshi Nakazawa ◽  
Seiji Tadokoro ◽  
Shigenori Honda ◽  
...  
Keyword(s):  
Binding Sites ◽  
Immune Thrombocytopenia ◽  
Essential Role ◽  
Recognition Sites ◽  
Primary Immune Thrombocytopenia ◽  
Binding Regions ◽  
Critical Binding

AbstractPlatelet-associated (PA) IgG autoantibodies play an essential role in primary immune thrombocytopenia (ITP). However, little is known about the epitopes of these Abs. This study aimed to identify critical binding regions for PA anti-αIIbβ3 Abs. Because PA anti-αIIbβ3 Abs bound poorly to mouse αIIbβ3, we created human-mouse chimera constructs. We first examined 76 platelet eluates obtained from patients with primary ITP. Of these, 26 harbored PA anti-αIIbβ3 Abs (34%). Further analysis of 15 patients who provided sufficient materials showed that the epitopes of these Abs were mainly localized in the N-terminal half of the β-propeller domain in αIIb (L1-W235). We could identify 3 main recognition sites in the region; 2 eluates recognized a conformation formed by the W1:1-2 and W2:3-4 loops, 5 recognized W1:2-3, and 4 recognized W3:4-1. The remaining 4 eluates could not be defined by the binding sites. Within these regions, we identified residues critical for binding, including S29 and R32 in W1:1-2; G44 and P45 in W1:2-3; and P135, E136, and R139 in W2:3-4. Of 11 eluates whose recognition sites were identified, 5 clearly showed restricted κ/λ-chain usage. These results suggested that PA anti-αIIbβ3 Abs in primary ITP tended to recognize highly restricted regions of αIIb with clonality.

Auxin transport in membrane vesicles from Cucurbita pepo L.

Planta ◽  
1983 ◽  
Vol 157 (3) ◽  
pp. 193-201 ◽  
Author(s):  
Rainer Hertel ◽  
Terri L. Lomax ◽  
Winslow R. Briggs
Keyword(s):  
Cucurbita Pepo ◽  
Auxin Transport ◽  
Membrane Vesicles
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