{"_id":"Xo5nBsCuj9xYm8JRz","bibbaseid":"anonymous-naturalnterminalfragmentsofbrainabundantmyristoylatedproteinbasp1-2003","bibdata":{"bibtype":"article","type":"article","author":[{"propositions":[],"lastnames":["Zakharov"],"firstnames":["V.V."],"suffixes":[]},{"propositions":[],"lastnames":["Capony"],"firstnames":["J.-P."],"suffixes":[]},{"propositions":[],"lastnames":["Derancourt"],"firstnames":["J."],"suffixes":[]},{"propositions":[],"lastnames":["Kropolova"],"firstnames":["E.S."],"suffixes":[]},{"propositions":[],"lastnames":["Novitskaya"],"firstnames":["V.A."],"suffixes":[]},{"propositions":[],"lastnames":["Bogdanova"],"firstnames":["M.N."],"suffixes":[]},{"propositions":[],"lastnames":["Mosevitsky"],"firstnames":["M.I."],"suffixes":[]}],"title":"Natural N-terminal fragments of brain abundant myristoylated protein BASP1","journal":"Biochimica et Biophysica Acta - General Subjects","year":"2003","volume":"1622","number":"1","pages":"14-19","doi":"10.1016/S0304-4165(03)00099-0","note":"cited By 23","url":"https://www.scopus.com/inward/record.uri?eid=2-s2.0-0038771933&doi=10.1016%2fS0304-4165%2803%2900099-0&partnerID=40&md5=719b1e87e24861e5b17ed878dab56d34","affiliation":"Molec./Radiation Biophysics Division, Petersburg Nucl. Phys. Inst. R., 188300 Gatchina, Leningrad District, Russian Federation; Ctr. Rech. Biochim. Macromoleculaire, Ctr. Natl. de la Rech. Scientifique, INSERM U 249, BP 5051, 34033 Montpellier, France","abstract":"BASP1 (also known as CAP-23 and NAP-22) is a novel myristoylated calmodulin-binding protein, abundant in nerve terminals. It is considered as a signal protein participating in neurite outgrowth and synaptic plasticity. BASP1 is also present in significant amounts in kidney, testis, and lymphoid tissues. In this study, we show that BASP1 is accompanied by at least six BASP1 immunologically related proteins (BIRPs), which are present in all animal species studied (rat, bovine, human, chicken). BIRPs have lower molecular masses than that of BASP1. Similarly to BASP1, they are myristoylated. Peptide mapping and partial sequencing have shown that BIRPs represent a set of BASP1 N-terminal fragments devoid of C-terminal parts of different length. In a definite species, the same set of BASP1 fragments is present in both brain and other tissues. The sum amount of the fragments is about 50% of the BASP1 amount in a tissue. Obligatory accompanying of BASP1 by a set of specific fragments indicates that these fragments are of physiological significance. © 2003 Elsevier Science B.V. All rights reserved.","author_keywords":"BASP1; CAP-23; Myristoylation; N-terminal fragment; NAP-22; Protein form","funding_details":"97-1249, 01-0064, YSF 2001/2-0105","key":"Zakharov200314","id":"Zakharov200314","bibbaseid":"anonymous-naturalnterminalfragmentsofbrainabundantmyristoylatedproteinbasp1-2003","role":"author","urls":{"Paper":"https://www.scopus.com/inward/record.uri?eid=2-s2.0-0038771933&doi=10.1016%2fS0304-4165%2803%2900099-0&partnerID=40&md5=719b1e87e24861e5b17ed878dab56d34"},"metadata":{"authorlinks":{}}},"bibtype":"article","biburl":"https://bio.pnpi.nrcki.ru/wp-content/uploads/2019/12/lbp_2019_10.txt","dataSources":["6vPsRbdrk6L6BBWH9"],"keywords":[],"search_terms":["natural","terminal","fragments","brain","abundant","myristoylated","protein","basp1"],"title":"Natural N-terminal fragments of brain abundant myristoylated protein BASP1","year":2003}