about
Structural basis of heteromeric smad protein assembly in TGF-beta signalingStructures of the G85R variant of SOD1 in familial amyotrophic lateral sclerosisInhibition of fast axonal transport by pathogenic SOD1 involves activation of p38 MAP kinaseMutant SOD1 instability: implications for toxicity in amyotrophic lateral sclerosis.Familial amyotrophic lateral sclerosis mutants of copper/zinc superoxide dismutase are susceptible to disulfide reduction.Destabilization of apoprotein is insufficient to explain Cu,Zn-superoxide dismutase-linked ALS pathogenesis.Screening preeclamptic cord plasma for proteins associated with decreased breast cancer susceptibility.Disulfide-bond scrambling promotes amorphous aggregates in lysozyme and bovine serum albumin.Preformed Seeds Modulate Native Insulin Aggregation Kinetics.Highly water-soluble, near-infrared emissive BODIPY polymeric dye bearing RGD peptide residues for cancer imaging.Detergent-insoluble aggregates associated with amyotrophic lateral sclerosis in transgenic mice contain primarily full-length, unmodified superoxide dismutase-1.Unusual Fluorescent Responses of Morpholine-functionalized Fluorescent Probes to pH via Manipulation of BODIPY's HOMO and LUMO Energy Orbitals for Intracellular pH DetectionMetal deficiency increases aberrant hydrophobicity of mutant superoxide dismutases that cause amyotrophic lateral sclerosisAxonal transport defects in neurodegenerative diseases.Decreased metallation and activity in subsets of mutant superoxide dismutases associated with familial amyotrophic lateral sclerosis.Facile electrochemical synthesis of antimicrobial TiO₂ nanotube arraysAberrantly increased hydrophobicity shared by mutants of Cu,Zn-superoxide dismutase in familial amyotrophic lateral sclerosis.Tuning thermoresponsive behavior of diblock copolymers and their gold core hybrids: part 1. Importance of placement of amphiphilic end groups on the diblock copolymers.Effect of pH on the stability and structure of yeast hexokinase A. Acidic amino acid residues in the cleft region are critical for the opening and the closing of the structure.Familial amyotrophic lateral sclerosis-associated mutations decrease the thermal stability of distinctly metallated species of human copper/zinc superoxide dismutase.Near-Infrared Fluorescent Probes with Large Stokes Shifts for Sensing Zn(II) Ions in Living Cells.A novel near-infrared fluorescent probe for sensitive detection of β-galactosidase in living cells.Fluorescent Probes for Sensitive and Selective Detection of pH Changes in Live Cells in Visible and Near-infrared Channels.Stabilization of yeast hexokinase A by polyol osmolytes: Correlation with the physicochemical properties of aqueous solutionsInhibition of Chaperone Activity Is a Shared Property of Several Cu,Zn-Superoxide Dismutase Mutants That Cause Amyotrophic Lateral SclerosisAn Efficient and Cost-Effective Procedure for Preparing Samples for Differential Scanning Calorimetry ExperimentsAcetylation of Aβ42 at Lysine 16 Disrupts Amyloid Formation
P50
Q24302541-33895538-4CF8-426A-83DA-28D2EAA6A124Q24644037-0719A53B-0B10-490B-B0CE-B41E9866227FQ28533850-B9D60F57-C121-43E3-AD1C-9B947B367EC5Q30159679-E3468910-64D8-4ABD-B569-B0A4C065F20BQ30165054-A4666A63-4DDC-49CB-8086-5ACDA4CC1D67Q33897544-AAFCAA3C-6EB9-45A7-9B39-F0026C5CF717Q35171916-BB60E2FF-ECC0-46F0-A390-104677864B78Q35562790-91338199-F5AC-4256-A1E9-1672719EB71AQ35839250-9FAD6C38-DF4C-4014-B184-BE775F20F39EQ36481543-94E47DA9-A531-4C8E-A7EA-BF2C9B471AE9Q36512177-C3401413-CF24-48D6-8F67-0F3E131364CCQ37183480-6706D7E5-1489-4133-A42D-0D8182DDD43AQ37448164-EEF37DD5-CA9E-4D85-AF36-CEECF22126EDQ37614744-FC3FE8CE-E718-42A4-9914-9DAD6C26CA68Q38291855-5CE51108-8797-432E-BCA2-A278452D076FQ38937397-485EFEA2-88DB-4BB5-A70C-CC39B055A8D2Q40409233-CCC2E8BE-CD22-4E93-A827-1B4052D2D599Q44570271-CBF872FA-09A4-4875-99D0-D40F0ED419ACQ44897854-E75FCB4A-BE74-4E71-8134-CD2F3DA22B8EQ46566731-3BBC6322-D779-48B1-87C1-CC467758E6E0Q49220432-CD482E46-E946-4527-A087-6F4D90757726Q53365802-37F3BCF0-780B-476F-94AB-F184357F9324Q53833384-C2903D7E-89D6-4FF9-9DF7-54B64B12F6ECQ57204415-305431CF-1C19-411A-BAE2-5355A3019FFAQ57204416-8ACD98FE-89F3-4314-B648-0FDB7910E699Q57204418-20C274A9-6120-4D18-B682-440A3AEFECA5Q90620606-2BD99B8B-6699-4824-9382-E9081D57F5A9
P50
description
researcher
@en
wetenschapper
@nl
հետազոտող
@hy
name
Ashutosh Tiwari
@ast
Ashutosh Tiwari
@en
Ashutosh Tiwari
@es
Ashutosh Tiwari
@nl
আশুতোষ তিয়ারি
@bn
type
label
Ashutosh Tiwari
@ast
Ashutosh Tiwari
@en
Ashutosh Tiwari
@es
Ashutosh Tiwari
@nl
আশুতোষ তিয়ারি
@bn
prefLabel
Ashutosh Tiwari
@ast
Ashutosh Tiwari
@en
Ashutosh Tiwari
@es
Ashutosh Tiwari
@nl
আশুতোষ তিয়ারি
@bn
P1053
A-7458-2008
P106
P31
P3829
P496
0000-0001-7373-349X