Zobrazeno 1 - 10
of 17
pro vyhledávání: '"Moshe Balass"'
Autor:
Moshe Balass, Mati Fridkin, Michal Harel, Ephraim Katchalski-Katzir, Roni Kasher, Sara Fuchs, Tali Scherf, Joel L. Sussman
Publikováno v:
Annals of the New York Academy of Sciences. 998:93-100
Our group has been employing short synthetic peptides, encompassing sequences from the acetylcholine receptor (AChR) alpha-subunit for the analysis of the binding site of the AChR. A 13-mer peptide mimotope, with similar structural motifs to the AChR
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::f83b500f61584e5551eb4a54d34b17f6
https://doi.org/10.1196/annals.1254.011
https://doi.org/10.1196/annals.1254.011
Autor:
Roni Kasher, Mati Fridkin, Michal Harel, Moshe Balass, Sara Fuchs, Ephraim Katchalski-Katzir, Joel L. Sussman, Tali Scherf
Publikováno v:
Biophysical Chemistry. 100:293-305
a-Bungarotoxin (a-BTX) is a highly toxic snake neurotoxin that binds to acetylcholine receptor (AChR) at the neuromuscular junction, and is a potent inhibitor of this receptor. In the following we review multi-phase research of the design, synthesis
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::d5e845e860d5c25be7c1c81e92afb1f2
https://doi.org/10.1016/s0301-4622(02)00287-9
https://doi.org/10.1016/s0301-4622(02)00287-9
Publikováno v:
Chemistry & Biology. 8(2):147-155
Background: α-Bungarotoxin (α-BTX) is a highly toxic snake venom α-neurotoxin that binds to acetylcholine receptor (AChR) at the neuromuscular junction, and is a potent inhibitor of this receptor. We describe the design and synthesis of peptides t
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::3b6d8c7493f752edcd129ada36074a00
Publikováno v:
Proceedings of the National Academy of Sciences. 97:761-766
Many pathogenic antibodies in myasthenia gravis (MG) and its animal model, experimental autoimmune MG (EAMG), are directed against the main immunogenic region (MIR) of the acetylcholine receptor (AcChoR). These antibodies are highly conformation depe
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::c3bbff7d20b6d275ef818edbd48e2d33
https://doi.org/10.1073/pnas.97.2.761
https://doi.org/10.1073/pnas.97.2.761
Autor:
Ephraim Katchalski-Katzir, Edward A. Bayer, Sara Fuchs, Meir Wilchek, Moshe Balass, Ely Morag
Publikováno v:
Analytical Biochemistry. 243:264-269
A novel approach for the selection of high-affinity phage from phage–peptide libraries is described. The methodology employs a chemically modified form of streptavidin, termed nitrostreptavidin, which exhibits a reversible attraction for biotin. Th
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::9837a80977e10934d0fc60f53b4490e6
https://doi.org/10.1006/abio.1996.0515
https://doi.org/10.1006/abio.1996.0515
Autor:
David Givol, Moshe Balass, Shmuel Cabilly, Sara Fuchs, Ephraim Katchalski-Katzir, Yehudit Heldman
Publikováno v:
Proceedings of the National Academy of Sciences. 90:10638-10642
Monoclonal antibody (mAb) 5.5 is directed against the ligand-binding site of the nicotinic acetylcholine receptor. The epitope for this antibody is conformation-dependent, and the antibody does not react with synthetic peptides derived from the recep
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::30b356d2da52ae895b423120bfa3de23
https://doi.org/10.1073/pnas.90.22.10638
https://doi.org/10.1073/pnas.90.22.10638
Autor:
Sara, Fuchs, Roni, Kasher, Moshe, Balass, Tali, Scherf, Mchal, Harel, Mati, Fridkin, Joel L, Sussman, Ephraim, Katchalski-Katzir
Publikováno v:
Annals of the New York Academy of Sciences. 998
Our group has been employing short synthetic peptides, encompassing sequences from the acetylcholine receptor (AChR) alpha-subunit for the analysis of the binding site of the AChR. A 13-mer peptide mimotope, with similar structural motifs to the AChR
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid________::79aa2d4b99915dcf18875511d3369bda
https://pubmed.ncbi.nlm.nih.gov/14592866
https://pubmed.ncbi.nlm.nih.gov/14592866
Autor:
Moshe Balass, Ephraim Katchalski-Katzir, Sara Fuchs, Joel L. Sussman, Mati Fridkin, Michal Harel, Tali Scherf, Roni Kasher
Publikováno v:
ChemInform. 34
a-Bungarotoxin (a-BTX) is a highly toxic snake neurotoxin that binds to acetylcholine receptor (AChR) at the neuromuscular junction, and is a potent inhibitor of this receptor. In the following we review multi-phase research of the design, synthesis
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::89d411037fed7132c5732e8c29a46d0e
https://doi.org/10.1002/chin.200338270
https://doi.org/10.1002/chin.200338270
Snake-venom α-bungarotoxin is a member of the α-neurotoxin family that binds with very high affinity to the nicotinic acetylcholine receptor (AChR) at the neuromuscular junction. The structure of the complex between α-bungarotoxin and a 13-mer pep
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::32e85f429db53aa080c0bebb07eb979a
https://europepmc.org/articles/PMC34404/
https://europepmc.org/articles/PMC34404/
