Crystallographic studies on protein misfolding: Domain swapping and amyloid formation in the SH3 domain
A Cámara-Artigas - Archives of Biochemistry and Biophysics, 2016 - Elsevier
Oligomerization by 3D domain swapping is found in a variety of proteins of diverse size, fold
and function. In the early 1960s this phenomenon was postulated for the oligomers of …
and function. In the early 1960s this phenomenon was postulated for the oligomers of …
Electrostatic effects in the folding of the SH3 domain of the c-Src tyrosine kinase: pH-dependence in 3D-domain swapping and amyloid formation
J Bacarizo, S Martinez-Rodriguez, JM Martin-Garcia… - PloS one, 2014 - journals.plos.org
The SH3 domain of the c-Src tyrosine kinase (c-Src-SH3) aggregates to form intertwined
dimers and amyloid fibrils at mild acid pHs. In this work, we show that a single mutation of …
dimers and amyloid fibrils at mild acid pHs. In this work, we show that a single mutation of …
A new physiological role for the DNA molecule as a protector against drying stress in desiccation-tolerant microorganisms
C García-Fontana, JJ Narváez-Reinaldo… - Frontiers in …, 2016 - frontiersin.org
The DNA molecule is associated with the role of encoding information required to produce
RNA which is translated into proteins needed by the cell. This encoding involves information …
RNA which is translated into proteins needed by the cell. This encoding involves information …
Small molecule AX-024 reduces T cell proliferation independently of CD3ϵ/Nck1 interaction, which is governed by a domain swap in the Nck1-SH3. 1 domain
K Richter, AC Rufer, M Muller, D Burger… - Journal of Biological …, 2020 - ASBMB
Activation of the T cell receptor (TCR) results in binding of the adapter protein Nck
(noncatalytic region of tyrosine kinase) to the CD3ϵ subunit of the TCR. The interaction was …
(noncatalytic region of tyrosine kinase) to the CD3ϵ subunit of the TCR. The interaction was …
Modified properties of alternan polymers arising from deletion of SH3-like motifs in Leuconostoc citreum ABK-1 alternansucrase
K Wangpaiboon, C Pitakchatwong, P Panpetch… - Carbohydrate …, 2019 - Elsevier
Abstract Alternansucrase (ALT, EC 2.4. 1.140) catalyses the formation of an alternating<-1,
3/1, 6-linked glucan, with periodic branch points, from sucrose substrate. Beyond the …
3/1, 6-linked glucan, with periodic branch points, from sucrose substrate. Beyond the …
Discovery of anti-tumor small molecule lead compounds targeting the SH3 domain of c-Src protein through virtual screening and biological evaluation
H Hao, Y Bian, N Yang, X Ji, J Bao, K Zhu - Archives of Biochemistry and …, 2024 - Elsevier
Abstract c-Src, also known as cellular Src, is a non-receptor tyrosine kinase that plays a
crucial role in various cellular processes, including cell proliferation, adhesion, and …
crucial role in various cellular processes, including cell proliferation, adhesion, and …
The promiscuous binding of the Fyn SH3 domain to a peptide from the NS5A protein
The hepatitis C virus nonstructural 5A (NS5A) protein is a large zinc-binding phosphoprotein
that plays an important role in viral RNA replication and is involved in altering signal …
that plays an important role in viral RNA replication and is involved in altering signal …
Atomic resolution structures of the c-Src SH3 domain in complex with two high-affinity peptides from classes I and II
J Bacarizo, A Camara-Artigas - Acta Crystallographica Section D …, 2013 - journals.iucr.org
The atomic resolution crystal structures of complexes between the SH3 domain of the c-Src
tyrosine kinase and two high-affinity peptides belonging to class I and class II have been …
tyrosine kinase and two high-affinity peptides belonging to class I and class II have been …
Structure of the c-Src-SH3 domain in complex with a proline-rich motif of NS5A protein from the hepatitis C virus
J Bacarizo, S Martinez-Rodriguez… - Journal of structural …, 2015 - Elsevier
The non-structural hepatitis C virus proteins NS5A and NS5B form a complex through
interaction with the SH2 and SH3 domains of the non-receptor Src tyrosine kinase, which …
interaction with the SH2 and SH3 domains of the non-receptor Src tyrosine kinase, which …
Cosolvent effects on the growth of protein aggregates formed by a single domain globular protein and an intrinsically disordered protein
Cosolvents modulate the stability of protein conformations and exhibit contrasting effects on
the kinetics of aggregation by globular proteins and intrinsically disordered proteins (IDPs) …
the kinetics of aggregation by globular proteins and intrinsically disordered proteins (IDPs) …