Articles

Search Articles

Advanced search
Help

Catalogue

Articles

Databases

X
Search Filters
Format Format
Subjects Subjects
Subjects Subjects
X
Sort by Item Count (A-Z)
Filter by Count
peptides (224) 224
index medicus (167) 167
chemistry (165) 165
organic chemistry (159) 159
metallurgy (156) 156
physics (150) 150
investigating or analysing materials by determining theirchemical or physical properties (135) 135
measuring (135) 135
testing (135) 135
human necessities (118) 118
hygiene (118) 118
medical or veterinary science (118) 118
preparations for medical, dental, or toilet purposes (116) 116
humans (108) 108
biochemistry & molecular biology (97) 97
alzheimer's disease (89) 89
proteins (87) 87
amino acid sequence (66) 66
animals (65) 65
protein binding (51) 51
specific therapeutic activity of chemical compounds ormedicinal preparations (51) 51
alzheimers-disease (48) 48
biochemistry (48) 48
molecular sequence data (46) 46
models, molecular (45) 45
oligomers (45) 45
protein (44) 44
multidisciplinary sciences (41) 41
protein structure, tertiary (41) 41
biophysics (40) 40
protein structure, secondary (37) 37
protein conformation (35) 35
analysis (33) 33
ligands (33) 33
magnetic resonance spectroscopy (33) 33
amyloid beta-peptides - chemistry (32) 32
binding sites (32) 32
nmr (32) 32
binding (31) 31
crystal-structure (30) 30
medicine (30) 30
neurology (30) 30
aggregation (29) 29
amyloid beta-peptides - metabolism (29) 29
neurodegenerative diseases (29) 29
science (29) 29
research article (27) 27
in-vitro (26) 26
mice (26) 26
nuclear magnetic resonance, biomolecular (26) 26
identification (25) 25
nuclear magnetic resonance spectroscopy (25) 25
research (25) 25
alzheimer disease - metabolism (24) 24
protein folding (24) 24
kinetics (23) 23
peptide fragments - chemistry (23) 23
amyloid (22) 22
circular dichroism (22) 22
microbiology (22) 22
neurosciences (21) 21
transgenic mice (20) 20
cell biology (19) 19
image phage display (19) 19
life sciences (19) 19
nmr spectroscopy (19) 19
peptide fragments - metabolism (19) 19
amino acids (18) 18
nmr-spectroscopy (18) 18
peptide (18) 18
phage display (18) 18
spectroscopy (18) 18
a-beta (17) 17
alzheimers disease (17) 17
alzheimer’s disease (17) 17
crystallography, x-ray (17) 17
fibrils (17) 17
health aspects (17) 17
brain (16) 16
chemistry, multidisciplinary (16) 16
hiv (16) 16
mice, transgenic (16) 16
nuclear magnetic resonance--nmr (16) 16
peptides - chemistry (16) 16
toxicity (16) 16
biology (15) 15
chemical properties (15) 15
enzymology (15) 15
gabarap (15) 15
physiological aspects (15) 15
recombinant proteins - chemistry (15) 15
secondary structure (15) 15
alzheimer disease - diagnosis (14) 14
beer (14) 14
disease models, animal (14) 14
fluorescence (14) 14
microtubule-associated proteins - chemistry (14) 14
mutation or genetic engineering (14) 14
nuclear magnetic resonance (14) 14
protein aggregation (14) 14
more...
Language Language
Language Language
X
Sort by Item Count (A-Z)
Filter by Count
English (651) 651
German (139) 139
French (97) 97
Chinese (9) 9
Japanese (3) 3
Portuguese (2) 2
Spanish (2) 2
Danish (1) 1
more...
Publication Date Publication Date
Click on a bar to filter by decade
Slide to change publication date range


1. Full Text High Resolution Fibril Structure of Amyloid-β(1-42) by Cryoelectron Microscopy
by Willbold, Dieter
Biophysical Journal, ISSN 0006-3495, 02/2018, Volume 114, Issue 3, pp. 185a - 185a
Journal Article
Details down arrow
Digital rights down arrow
loading Loading Rights
2. Full Text Aβ OLIGOMER ELIMINATING D-ENANTIOMERIC PEPTIDES ENHANCE COGNITION AND IMPEDE NEURODEGENERATION EVEN BY ORAL APPLICATION
by Willbold, Dieter
Alzheimer's & Dementia, ISSN 1552-5260, 07/2017, Volume 13, Issue 7, p. P591
Journal Article
Details down arrow
Digital rights down arrow
loading Loading Rights
3. Full Text Aβ OLIGOMER ELIMINATING D-ENANTIOMERIC PEPTIDES ENHANCE COGNITION AND IMPEDE NEURODEGENERATION EVEN BY ORAL APPLICATION
by Willbold, Dieter
Alzheimer's & Dementia: The Journal of the Alzheimer's Association, ISSN 1552-5260, 07/2017, Volume 13, Issue 7, pp. P591 - P591
Journal Article
Details down arrow
Digital rights down arrow
loading Loading Rights
4. Full Text A[beta] OLIGOMER ELIMINATING D-ENANTIOMERIC PEPTIDES ENHANCE COGNITION AND IMPEDE NEURODEGENERATION EVEN BY ORAL APPLICATION
by Willbold, Dieter
Alzheimer's & Dementia: The Journal of the Alzheimer's Association, ISSN 1552-5260, 07/2017, Volume 13, Issue 7, p. P591
Peptides | Cognition
Journal Article
Details down arrow
Digital rights down arrow
loading Loading Rights
5. Full Text A[beta] OLIGOMER ELIMINATING COMPOUNDS IMPEDE NEURODEGENERATION IN VIVO
by Willbold, Dieter
Alzheimer's & Dementia: The Journal of the Alzheimer's Association, ISSN 1552-5260, 07/2016, Volume 12, Issue 7, p. P439
Journal Article
Details down arrow
Digital rights down arrow
loading Loading Rights
6. Full Text Aβ OLIGOMER ELIMINATING COMPOUNDS IMPEDE NEURODEGENERATION IN VIVO
by Willbold, Dieter
Alzheimer's & Dementia: The Journal of the Alzheimer's Association, ISSN 1552-5260, 2016, Volume 12, Issue 7, pp. P439 - P439
Neurology
Journal Article
Details down arrow
Digital rights down arrow
loading Loading Rights
7. Full Text Do we need anti-prion compounds to treat Alzheimer’s disease?
by Willbold, Dieter and Kutzsche, Janine
Molecules, ISSN 1420-3049, 06/2019, Volume 24, Issue 12, p. 2237
Background: While phase III clinical trials for the treatment of Alzheimer’s disease (AD) keep failing regardless of the target, more and more data suggest... 
D-enantiomeric peptides | Oral treatment | Alzheimer’s disease | Amyloid β | Anti-prion | Aβ oligomers | anti-prion | oral treatment | d -enantiomeric peptides | amyloid β
Journal Article
Details down arrow
Digital rights down arrow
loading Loading Rights
8. Full Text Monomeric Amyloid beta peptide in hexafluoroisopropanol detected by small angle neutron scattering
by Zhang-Haagen, Bo and Biehl, Ralf and Nagel-Steger, Luitgard and Radulescu, Aurel and Richter, Dieter and Willbold, Dieter
PLoS ONE, ISSN 1932-6203, 02/2016, Volume 11, Issue 2, p. e0150267
Small proteins like amyloid beta (A beta) monomers are related to neurodegenerative disorders by aggregation to insoluble fibrils. Small angle neutron... 
NEURODEGENERATIVE DISEASE | PROTEIN | ALZHEIMERS-DISEASE | MULTIDISCIPLINARY SCIENCES | CONFORMATIONAL TRANSITION | DYNAMICS | X-RAY-SCATTERING | TOXICITY | OLIGOMERS | AGGREGATION | HYDRATION | Solvents | Propanols | Models, Chemical | Humans | Models, Molecular | Scattering, Small Angle | Hydrodynamics | Protein Aggregation, Pathological | Peptide Fragments - analysis | Peptide Fragments - chemistry | Hydrogen Bonding | Amyloid beta-Peptides - analysis | Protein Conformation | Amyloid beta-Peptides - chemistry | Neutron Diffraction | Amyloid beta-protein | Physiological aspects | Nervous system | Development and progression | Genetic aspects | Degeneration | Research | Diagnosis | Fourier transforms | Nuclear magnetic resonance--NMR | Neurodegenerative diseases | Hydration | Nondestructive testing | Light scattering | Fibrils | Neutrons | Biochemistry | Agglomeration | Photon correlation spectroscopy | Crystallography | Monomers | Molecular weight | Proteins | Studies | Brain research | X rays | Neutron scattering | Microscopy | β-Amyloid | Surface layers | NMR | Nuclear magnetic resonance
Journal Article
Details down arrow
Digital rights down arrow
loading Loading Rights
9. Full Text C‐Src is required for complex formation between the hepatitis C virus–encoded proteins NS5A and NS5B: A prerequisite for replication
by Pfannkuche, Andreas and Büther, Katrin and Karthe, Juliane and Poenisch, Marion and Bartenschlager, Ralf and Trilling, Mirko and Hengel, Hartmut and Willbold, Dieter and Häussinger, Dieter and Bode, Johannes Georg
Hepatology, ISSN 0270-9139, 04/2011, Volume 53, Issue 4, pp. 1127 - 1136
Hepatitis C virus (HCV) is a leading cause of chronic liver disease worldwide and establishes a persistent infection in more than 60% of infected individuals.... 
SIGNAL-TRANSDUCTION | CELLS | RNA REPLICATION | SARCOMA VIRUS | IN-VIVO | HERBIMYCIN-A | TYROSINE KINASES | REPLICON | IDENTIFICATION | GASTROENTEROLOGY & HEPATOLOGY | FAMILY | Benzoquinones - pharmacology | Viral Nonstructural Proteins | Virus Replication | RNA Replicase - genetics | Humans | Rifabutin - analogs & derivatives | Cell Line, Tumor | Hepacivirus - genetics | Hepacivirus - physiology | src Homology Domains - genetics | src-Family Kinases - physiology | Lactams, Macrocyclic - pharmacology | Proteins | Hepatitis | Human immunodeficiency virus--HIV
Journal Article
Details down arrow
Digital rights down arrow
loading Loading Rights
10. Full Text Kinetic titration series with biolayer interferometry
by Frenzel, Daniel and Willbold, Dieter
PLoS ONE, ISSN 1932-6203, 09/2014, Volume 9, Issue 9, p. e106882
Biolayer interferometry is a method to analyze protein interactions in real-time. In this study, we illustrate the usefulness to quantitatively analyze high... 
MOLECULAR-INTERACTIONS | DESIGN | AFFINITY | MULTIDISCIPLINARY SCIENCES | PROTEIN-G | SURFACE-PLASMON RESONANCE | DOMAINS | Surface Plasmon Resonance | Protein Binding | Interferometry - methods | Kinetics | Immunoglobulin G | Data analysis | Immunoglobulins | Protein G | Biochemistry | Experiments | Exports | Design | Proteins | Ligands | Titration | Surface plasmon resonance | Sensors | Biosensors | Protein interaction | Interferometry
Journal Article
Details down arrow
Digital rights down arrow
loading Loading Rights
11. Peptides for therapy and diagnosis of alzheimer's disease
by Funke, Susanne Aileen and Willbold, Dieter
Current Pharmaceutical Design, ISSN 1381-6128, 01/2012, Volume 18, Issue 6, pp. 755 - 767
Alzheimer's disease (AD) is a progressive neurodegenerative disorder with devastating effects. The greatest risk factor to develop AD is age. Today, only... 
Therapy | Amyloid-β | Diagnosis | Peptides | Alzheimer's disease | FIBRIL FORMATION | NEUROFIBRILLARY TANGLES | LEARNING-DEFICITS | therapy | diagnosis | peptides | IMAGE PHAGE DISPLAY | COGNITIVE FUNCTION | APOLIPOPROTEIN-E | amyloid-beta | TAU HYPERPHOSPHORYLATION | AMYLOID-BETA-PEPTIDE | MOUSE MODEL | PHARMACOLOGY & PHARMACY | I MIMETIC PEPTIDES | Alzheimer Disease - diagnosis | Amino Acid Sequence | Humans | Alzheimer Disease - drug therapy | Peptide Library | Drug Discovery | Amyloid beta-Protein Precursor | Peptides - therapeutic use
Journal Article
Details down arrow
12. Full Text Enhancing the Catalytic Deamination Activity of APOBEC3C Is Insufficient to Inhibit Vif-Deficient HIV-1
by Jaguva Vasudevan, Ananda Ayyappan and Hofmann, Henning and Willbold, Dieter and Häussinger, Dieter and Koenig, Bernd W and Münk, Carsten
Journal of Molecular Biology, ISSN 0022-2836, 04/2017, Volume 429, Issue 8, pp. 1171 - 1191
The retroviral restriction factors of the APOBEC3 (A3) cytidine deaminase family catalyze the deamination of cytidines in single-stranded viral DNA. APOBEC3C... 
APOBEC3C | deamination-dependent virus restriction | retrovirus | cytidine deaminase | human immunodeficiency virus (HIV) | Retrovirus | Deamination-dependent virus restriction | Cytidine deaminase | Human immunodeficiency virus (HIV) | CYTIDINE DEAMINASES | DNA-BINDING | RESTRICTION FACTOR APOBEC3G | CRYSTAL-STRUCTURE | REVERSE TRANSCRIPTION | BIOCHEMISTRY & MOLECULAR BIOLOGY | INTRINSIC IMMUNITY | HUMAN-IMMUNODEFICIENCY-VIRUS | IN-VITRO | ANTIVIRAL ACTIVITY | HEPATITIS-B | HIV-1 - pathogenicity | Simian Immunodeficiency Virus - pathogenicity | Zinc - metabolism | Cytidine Deaminase - genetics | DNA, Single-Stranded - metabolism | Humans | DNA, Viral - metabolism | Pan troglodytes | vif Gene Products, Human Immunodeficiency Virus - genetics | HIV-1 - genetics | DNA, Single-Stranded - chemistry | HEK293 Cells - virology | Host-Pathogen Interactions | vif Gene Products, Human Immunodeficiency Virus - metabolism | Animals | Cytosine - metabolism | Leukemia Virus, Murine - metabolism | Cytidine Deaminase - metabolism | Leukemia Virus, Murine - pathogenicity | Protein Conformation | Simian Immunodeficiency Virus - metabolism | Cytidine Deaminase - chemistry | Amino Acid Substitution | Antiviral agents | Enzymes | Monkeys | Leukemia | Proteins | HIV (Viruses) | Denaturation
Journal Article
Details down arrow
Digital rights down arrow
loading Loading Rights
13. Full Text BEST-TROSY experiments for time-efficient sequential resonance assignment of large disordered proteins
by Solyom, Zsofia and Schwarten, Melanie and Geist, Leonhard and Konrat, Robert and Willbold, Dieter and Brutscher, Bernhard
Journal of Biomolecular NMR, ISSN 0925-2738, 4/2013, Volume 55, Issue 4, pp. 311 - 321
The characterization of the conformational properties of intrinsically disordered proteins (IDPs), and their interaction modes with physiological partners has... 
Biochemistry, general | Spectroscopy/Spectrometry | TROSY | IDP | Viral protein | Biophysics and Biological Physics | Amino-acid-type editing | Longitudinal-relaxation enhancement | BEST | Physics | Longitudinal- relaxation enhancement | SET | NMR-SPECTROSCOPY | BIOCHEMISTRY & MOLECULAR BIOLOGY | INTRINSICALLY UNSTRUCTURED PROTEINS | RELAXATION | PULSES | SPECTROSCOPY | RESIDUES | Protein Conformation | Proteins - analysis | Proteins - chemistry | Nuclear Magnetic Resonance, Biomolecular - methods | Proteins | Proline | Physiological aspects | Nuclear magnetic resonance spectroscopy | Life Sciences | Biomolecules | Biochemistry, Molecular Biology
Journal Article
Details down arrow
Digital rights down arrow
loading Loading Rights
14. Full Text Structural insights into ion conduction by channelrhodopsin 2
by Volkov, Oleksandr and Kovalev, Kirill and Polovinkin, Vitaly and Borshchevskiy, Valentin and Bamann, Christian and Astashkin, Roman and Marin, Egor and Popov, Alexander and Balandin, Taras and Willbold, Dieter and Büldt, Georg and Bamberg, Ernst and Gordeliy, Valentin
Science, ISSN 0036-8075, 11/2017, Volume 358, Issue 6366, p. eaan8862
The light-gated ion channel channelrhodopsin 2 (ChR2) from is a major optogenetic tool. Photon absorption starts a well-characterized photocycle, but the... 
ACTIVATION | PROTEIN | CHANNEL | CONVERSION | CRYSTAL-STRUCTURE | MEMBRANE | MULTIDISCIPLINARY SCIENCES | LIGHT | PHOTOCYCLE | BOUND WATER-MOLECULES | PROTON-TRANSFER | Amino Acid Sequence | Sequence Alignment | Channelrhodopsins - chemistry | Chlamydomonas reinhardtii | Crystallography, X-Ray | Protein Conformation | Channelrhodopsins - ultrastructure | Ion Transport | Optogenetics | Channelrhodopsins - genetics | Glutamic acid | Cell culture | Conduction | Fourier transforms | High resolution | Hydrogen | Amino acids | Action potential | Retina | Helices | Hydrogen bonding | Remote control | Proteins | Depolarization | Biological effects | Microorganisms | Absorption | Imines | Light | Chemical bonds | Genetics | Aspartic acid | Ion channels | Membrane potential | Dimerization | Gating | Bonding | Hydrogen ion concentration | Crystal structure | EKG | Channel opening | Neurons | Channel gating | Algae | Isomerization | Crystallization | Muscles | Tools | Data processing | Membrane proteins | Cores | Information processing | Electrochemistry | Holes | Gates | Conformation | Life Sciences | Biomolecules | Biochemistry, Molecular Biology
Journal Article
Details down arrow
Digital rights down arrow
loading Loading Rights
15. Full Text Solution‐Based Determination of Dissociation Constants for the Binding of Aβ42 to Antibodies
by Zhang, Tao and Nagel‐Steger, Luitgard and Willbold, Dieter
ChemistryOpen, ISSN 2191-1363, 07/2019, Volume 8, Issue 7, pp. 989 - 994
Amyloid β‐peptides (Aβ) play a major role in the pathogenesis of Alzheimer's disease. Therefore, numerous monoclonal antibodies against Aβ have been developed... 
microscale thermophoresis | analytical ultracentrifugation | amyloid β-peptides | monoclonal antibodies | protein-protein interactions | Viscosity | Binding | Antigens | Immunoglobulins | Peptides | Low concentrations | Pathogenesis | Fluorescence | Monomers | Proteins | Aqueous solutions | Monoclonal antibodies | Affinity | Alzheimers disease | Alzheimer's disease | Thermophoresis | Sedimentation & deposition
Journal Article
Details down arrow
Digital rights down arrow
loading Loading Rights
16. Full Text Blick in den viralen Baukasten
by Willbold, Dieter and Hoffmann, Silke
forschung, ISSN 0172-1518, 04/2018, Volume 43, Issue 1, pp. 12 - 15
Anhand der HIV‐Infektion wollen Strukturbiologen die Wechselbeziehungen zwischen dem krank machenden Virus und seinem Wirt besser verstehen. Ergeben sich... 
Journal Article
Details down arrow
Digital rights down arrow
loading Loading Rights
17. Full Text Crystal structure of a light-driven sodium pump
by Gushchin, Ivan and Shevchenko, Vitaly and Polovinkin, Vitaly and Kovalev, Kirill and Alekseev, Alexey and Round, Ekaterina and Borshchevskiy, Valentin and Balandin, Taras and Popov, Alexander and Gensch, Thomas and Fahlke, Christoph and Bamann, Christian and Willbold, Dieter and Büldt, Georg and Bamberg, Ernst and Gordeliy, Valentin
Nature Structural and Molecular Biology, ISSN 1545-9993, 05/2015, Volume 22, Issue 5, pp. 390 - 396
Recently, the first known light-driven sodium pumps, from the microbial rhodopsin family, were discovered. We have solved the structure of one of them,... 
SITE | PROTEORHODOPSIN | BIOPHYSICS | MEMBRANE | BIOCHEMISTRY & MOLECULAR BIOLOGY | RHODOPSIN | HALORHODOPSIN | BACTERIORHODOPSIN | PROTEINS | CELL BIOLOGY | Potassium - metabolism | Protein Structure, Tertiary | Rhodopsin - ultrastructure | Models, Molecular | Crystallography, X-Ray | Flavobacteriaceae - enzymology | Ion Transport | Sodium - metabolism | Sodium-Potassium-Exchanging ATPase - ultrastructure | Physiological aspects | Sodium channels | Rhodopsin | Research | Structure | Proteins | Genetics | Biophysics | Crystal structure | Life Sciences | Biomolecules | Biochemistry, Molecular Biology
Journal Article
Details down arrow
Digital rights down arrow
loading Loading Rights
18. Full Text Guidelines for the use and interpretation of assays for monitoring autophagy
by Klionsky, Daniel J and Abdalla, Fabio C and Abeliovich, Hagai and Abraham, Robert T and Acevedo-Arozena, Abraham and Adeli, Khosrow and Agholme, Lotta and Agnello, Maria and Agostinis, Patrizia and Aguirre-Ghiso, Julio A and Ahn, Hyung Jun and Ait-Mohamed, Ouardia and Ait-Si-Ali, Slimane and Akematsu, Takahiko and Akira, Shizuo and Al-Younes, Hesham M and Al-Zeer, Munir A and Albert, Matthew L and Albin, Roger L and Alegre-Abarrategui, Javier and Aleo, Maria Francesca and Alirezaei, Mehrdad and Almasan, Alexandru and Almonte-Becerril, Maylin and Amano, Atsuo and Amaravadi, Ravi K and Amarnath, Shoba and Amer, Amal O and Andrieu-Abadie, Nathalie and Anantharam, Vellareddy and Ann, David K and Anoopkumar-Dukie, Shailendra and Aoki, Hiroshi and Apostolova, Nadezda and Arancia, Giuseppe and Aris, John P and Asanuma, Katsuhiko and Asare, Nana Y.O and Ashida, Hisashi and Askanas, Valerie and Askew, David S and Auberger, Patrick and Baba, Misuzu and Backues, Steven K and Baehrecke, Eric H and Bahr, Ben A and Bai, Xue-Yuan and Bailly, Yannick and Baiocchi, Robert and Baldini, Giulia and Balduini, Walter and Ballabio, Andrea and Bamber, Bruce A and Bampton, Edward T.W and Juhász, Gábor and Bartholomew, Clinton R and Bassham, Diane C and Bast, Robert C and Batoko, Henri and Bay, Boon-Huat and Beau, Isabelle and Béchet, Daniel M and Begley, Thomas J and Behl, Christian and Behrends, Christian and Bekri, Soumeya and Bellaire, Bryan and Bendall, Linda J and Benetti, Luca and Berliocchi, Laura and Bernardi, Henri and Bernassola, Francesca and Besteiro, Sébastien and Bhatia-Kissova, Ingrid and Bi, Xiaoning and Biard-Piechaczyk, Martine and Blum, Janice S and Boise, Lawrence H and Bonaldo, Paolo and Boone, David L and Bornhauser, Beat C and Bortoluci, Karina R and Bossis, Ioannis and Bost, Frédéric and Bourquin, Jean-Pierre and Boya, Patricia and Boyer-Guittaut, Michaël and Bozhkov, Peter V and Brady, Nathan R and Brancolini, Claudio and Brech, Andreas and Brenman, Jay E and Brennand, Ana and Bresnick, Emery H and Brest, Patrick and Bridges, Dave and Bristol, Molly L and Brookes, Paul S and Brown, Eric J and Brumell, John H and ... and Linköpings universitet and Institutionen för klinisk och experimentell medicin and Geriatrik and Institutionen för medicin och hälsa and Farmakologi and Experimentell patologi and Hälsouniversitetet and Cellbiologi
Autophagy, ISSN 1554-8627, 04/2012, Volume 8, Issue 4, pp. 445 - 544
In 2008 we published the first set of guidelines for standardizing research in autophagy. Since then, research on this topic has continued to accelerate, and... 
stress | vacuole | autolysosome | flux | LC3 | autophagosome | lysosome | phagophore | Binding | Proteins | Landes | Calcium | Bioscience | Biology | Cell | Cycle | Cancer | Organogenesis | Phagophore | Lysosome | Autolysosome | Flux | Autophagosome | Vacuole | Stress | ACTIVATED PROTEIN-KINASE | CHAPERONE-MEDIATED AUTOPHAGY | VACUOLE TARGETING PATHWAY | ENDOPLASMIC-RETICULUM STRESS | ISOLATED RAT HEPATOCYTES | STARVATION-INDUCED AUTOPHAGY | GLUCAGON-INDUCED AUTOPHAGY | CELL BIOLOGY | PROGRAMMED CELL-DEATH | BREAST-CANCER CELLS | BETAINE HOMOCYSTEINE METHYLTRANSFERASE | Biological Assay - methods | Animals | Autophagy - genetics | Models, Biological | Humans | Life Sciences | Cellular Biology | Review | Medical and Health Sciences | Medicin och hälsovetenskap
Journal Article
Details down arrow
Digital rights down arrow
loading Loading Rights