about
Seventy years of publications.An unprecedented dioxygen species revealed by serial femtosecond rotation crystallography in copper nitrite reductase.Enzyme catalysis captured using multiple structures from one crystal at varying temperatures.X-ray and cryo-EM structures of inhibitor-bound cytochrome bc1 complexes for structure-based drug discovery.The expanding toolkit for structural biology: synchrotrons, X-ray lasers and cryoEMMolecular recognition and maturation of SOD1 by its evolutionarily destabilised cognate chaperone hCCSSeventy years of publicationsIdentification of a tyrosine switch in copper-haem nitrite reductasesEbselen as template for stabilization of A4V mutant dimer for motor neuron disease therapyThe biophysics of superoxide dismutase-1 and amyotrophic lateral sclerosisReverse protein engineering of a novel 4-domain copper nitrite reductase reveals functional regulation by protein-protein interactionLAT1 (SLC7A5) and CD98hc (SLC3A2) complex dynamics revealed by single-particle cryo-EMCatalytically important damage-free structures of a copper nitrite reductase obtained by femtosecond X-ray laser and room-temperature neutron crystallographyDimeric structures of quinol-dependent nitric oxide reductases (qNORs) revealed by cryo-electron microscopyThe active form of quinol-dependent nitric oxide reductase from Neisseria meningitidis is a dimerStructures of substrate- and product-bound forms of a multi-domain copper nitrite reductase shed light on the role of domain tethering in protein complexesPurification and Structural Characterization of Aggregation-Prone Human TDP-43 Involved in Neurodegenerative DiseasesStructural basis of the dominant inheritance of hypermethioninemia associated with the Arg264His mutation in the MAT1A gene
P50
Q42359325-8A2789E8-04E6-489A-8FD4-C347D342BC96Q48200913-039D2AE9-D6B8-4D75-A376-7CBD85EF4E97Q54972648-2996CA0A-6968-4751-8E08-74B196A540BCQ55004502-D1C41D1D-7769-4521-8707-F1E3FBB4D63EQ64079360-67B70450-202D-41EB-9C84-4FDE38058C56Q64265968-D71AAD35-4BFC-42EF-B466-76926B2DAFCFQ88910548-154DF019-D818-4DB6-B2BB-C1142666E2DBQ90014528-B6266905-2274-430D-B41A-E74B10DA7127Q90091543-DD61F658-499F-4BFF-B422-C8CE38C3B5E0Q91419222-B52852E6-07B9-4DB2-8459-B403A6F10CE2Q91626304-866D23EC-7553-46B2-985D-CB63B034E26AQ91698103-57B7C99C-8AD2-4D5B-B526-6B5F27404DB0Q91974249-9A082814-74ED-4ECA-BDE4-11EB92101FEBQ93137494-5004F33A-CCC6-4EBC-B57C-2F36808BC07DQ95295096-3ACD855B-3A76-4D04-8262-27A014807A12Q95295306-0F8129D9-A3E5-4EF1-A67B-71683F49B3C9Q96110261-40AFE197-3407-4063-B855-DC1A581A5CC3Q96116766-748092E0-2919-4CAB-BC56-D67102A06ACE
P50
description
researcher
@en
wetenschapper
@nl
name
Samar Hasnain
@en
Samar Hasnain
@nl
type
label
Samar Hasnain
@en
Samar Hasnain
@nl
prefLabel
Samar Hasnain
@en
Samar Hasnain
@nl
P31
P496
0000-0002-2854-4718